Interplay between the cpSRP pathway components, the substrate LHCP and the translocase Alb3: An in vivo and in vitro study

The chloroplast signal recognition particle (cpSRP) and its receptor, cpFtsY, posttranslationally target the nuclear-encoded light-harvesting chlorophyll-binding proteins (LHCPs) to the translocase Alb3 in the thylakoid membrane. In this study, we analyzed the interplay between the cpSRP pathway components, the substrate protein LHCP and the translocase Alb3 by using in vivo and in vitro techniques. We propose that cpSRP43 is crucial for the binding of LHCP-loaded cpSRP and cpFtsY to Alb3. In addition, our data suggest that a direct interaction between Alb3 and LHCP contributes to the formation of this complex.

Structured summary

MINT-7992851: Alb3 (uniprotkb:Q8LBP4) physically interacts (MI:0915) with cpSRP43 (uniprotkb:O22265) by two hybrid (MI:0018)MINT-7992897: cpSRP43 (uniprotkb:O22265) and Alb3 (uniprotkb:Q8LBP4) physically interact (MI:0915) by bimolecular fluorescence complementation (MI:0809)MINT-7993251: SRP43 (uniprotkb:O22265) binds (MI:0407) to LHCP (uniprotkb:P27490) by pull down (MI:0096)MINT-7993207: cpSRP43 (uniprotkb:O22265) physically interacts (MI:0915) with ftsY (uniprotkb:O80842), LHCP (uniprotkb:P27490), SRP-54 (uniprotkb:P37106) and Alb3 (uniprotkb:Q8LBP4) by pull down (MI:0096)MINT-7993272: Alb3 (uniprotkb:Q8LBP4) and LHCB (uniprotkb:P27490) physically interact (MI:0915) by bimolecular fluorescence complementation (MI:0809)MINT-7992960: cpSRP43 (uniprotkb:O22265) binds (MI:0407) to Alb3 (uniprotkb:Q8LBP4) by pull down (MI:0096)MINT-7993236: Alb3 (uniprotkb:Q8LBP4) binds (MI:0407) to LHCP (uniprotkb:P27490) by pull down (MI:0096)MINT-7993166: cpSRP43 (uniprotkb:O22265) physically interacts (MI:0915) with LHCP (uniprotkb:P27490) and Alb3 (uniprotkb:Q8LBP4) by pull down (MI:0096)MINT-7993118: cpSRP43 (uniprotkb:O22265) physically interacts (MI:0915) with Alb3 (uniprotkb:Q8LBP4), SRP-54 (uniprotkb:P37106) and LHCP (uniprotkb:P27490) by pull down (MI:0096)MINT-7993046: cpSRP43 (uniprotkb:O22265) physically interacts (MI:0915) with ftsY (uniprotkb:O80842), SRP-54 (uniprotkb:P37106) and Alb3 (uniprotkb:Q8LBP4) by pull down (MI:0096)MINT-7993004: cpSRP43 (uniprotkb:O22265) physically interacts (MI:0915) with SRP54 (uniprotkb:P37106) and Alb3 (uniprotkb:Q8LBP4) by pull down (MI:0096)     

Interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall

It has not yet been reported how the secondary CESA (cellulose synthase) proteins are organized in the rosette structure. A membrane-based yeast two-hybrid (MbYTH) approach was used to analyze the interactions between the CESA proteins involved in secondary cell wall synthesis of Arabidopsis and the findings were confirmed in planta by bimolecular fluorescence complementation (BiFC) assay. Results indicated that although all CESA proteins can interact with each other, only CESA4 is able to form homodimers. A model is proposed for the secondary rosette structure. The RING-motif proved not to be essential for the interaction between the CESA proteins.

Structured summary

MINT-6951243: PIP2-1 (uniprotkb:P43286) physically interacts (MI:0218) with PIP2-1 (uniprotkb:P43286) by bimolecular fluorescence complementation (MI:0809)MINT-6950816: CESA4 (uniprotkb:Q84JA6) physically interacts (MI:0218) withCESA4 (uniprotkb:Q84JA6) by membrane bound complementation assay (MI:0230)MINT-6951056, MINT-6951071, MINT-6951088, MINT-6951103: CESA7 (uniprotkb:Q9SWW6) physically interacts (MI:0218) with CESA4 (uniprotkb:Q84JA6) by bimolecular fluorescence complementation (MI:0809)MINT-6950949, MINT-6950990: CESA4 (uniprotkb:Q84JA6) physically interacts (MI:0218) with CESA8 (uniprotkb:Q8LPK5) by membrane bound complementation assay (MI:0230)MINT-6950909, MINT-6951030: CESA4 (uniprotkb:Q8LPK5) physically interacts (MI:0218) with CESA7 (uniprotkb:Q9SWW6) by membrane bound complementation assay (MI:0230)MINT-6951042: CESA4 (uniprotkb:Q84JA6) physically interacts (MI:0218) with CESA4 (uniprotkb:Q84JA6) by bimolecular fluorescence complementation (MI:0809)MINT-6951004, MINT-6951016: CESA8 (uniprotkb:Q8LPK5) physically interacts (MI:0218) with CESA7 (uniprotkb:Q9SWW6) by membrane bound complementation assay (MI:0230)MINT-6951217, MINT-6951230: CESA4 (uniprotkb:Q84JA6) physically interacts (MI:0218) with CESA8 (uniprotkb:Q8LPK5) by bimolecular fluorescence complementation (MI:0809)MINT-6951120, MINT-6951140, MINT-6951156, MINT-6951170, MINT-6951185: CESA8 (uniprotkb:Q8LPK5) physically interacts (MI:0218) withCESA7 (uniprotkb:Q9SWW6) by bimolecular fluorescence complementation (MI:0809)MINT-6951199: CESA8 (uniprotkb:Q8LPK5) physically interacts (MI:0218) withCESA8 (uniprotkb:Q8LPK5) by bimolecular fluorescence complementation (MI:0809)     

Checklist of the species of the aseptate Gregarine family Urosporidae

A checklist is given of the 45 named species of the family Urosporidae (phylum Protozoa, subphylum Apicomplexa, class Sporozoa, subclass Gregarinia, order Eugregarinida, suborder Aseptatina) together with their synonyms, the names of their hosts, their locations in the hosts, their known geographic distribution, and key references. Another list is given of synonyms, lapsi calami, nomina nuda, etc. associated with the genera of this family. The following taxonomic-nomenclatural innovations are introduced—NEW NAME: Gonospora good-richae nom. nov. in the polychaete Arenicola ecaudata; NEW COMBINATIONS: Urospora grassei (Changeux, 1961) in the sea cucumbers Holothuria spp.; Urospora schneideri (Mingazzini, 1891) in the sea cucumbers Holothuria spp; Gonospora gonadipertha (Djakonov, 1923) in the sea cucumber Cucumaria frondosa; Gonospora stichopi (Lützen, 1967) in the sea cucumber Stichopus tremulus.     

Reassessment of the role of FKBP38 in the Rheb/mTORC1 pathway

The small G-protein Rheb regulates cell growth via the mTORC1 complex by incompletely understood mechanisms. Recent studies document that Rheb activates mTORC1 via direct, GTP-dependent interaction with the peptidyl-prolyl-cis/trans-isomerase FKBP38, which is proposed to act as an inhibitor of mTORC1. We have conducted a comprehensive biochemical characterization of the Rheb/FKBP38 interaction. Using three different in vitro assays we did not detect an interaction between Rheb and FKBP38. Cell biological experiments illustrate that FKBP38 plays only a very minor, if any, role in mTORC1 activation. Our data document that FKBP38 is not the long-sought Rheb effector linking Rheb to mTORC1 activation.

Structured summary

MINT-6946532: Ral (uniprotkb:P11233) binds (MI:0407) to Ha-Ras (uniprotkb:P01112) by pull down (MI:0096)MINT-6946500: RAF (uniprotkb:P04049) binds (MI:0407) to RHEB2 (uniprotkb:Q15382) by pull down (MI:0096)MINT-6946517: RAF (uniprotkb:P04049) binds (MI:0407) to Ha-Ras (uniprotkb:P01112) by pull down (MI:0096)     

A review of the genus Rusa in the indo-malayan archipelago and conservation efforts

Genus Rusa, belonging to the deer family Cervidae is native to the Indo-Malaya Archipelago (IMA). However, detailed information on the Rusa genus in the IMA is limited. This review provides comprehensive information on the Rusa genus in the IMA including, threats and conservation efforts. There are four species of deer in Rusa genus, which is Sambar deer (Rusa unicolor), Javan deer (Rusa timorensis), Visayan spotted deer (Rusa alfredi) and Philippine deer (Rusa marianna). Despite their wide distribution in the South Asian and Southeast Asian regions, they are under serious threats. Some conservation efforts that are being done to protect and conserve them among others are; (1) facilities protection, (2) habitat enrichment programme, (3) Ex-situ conservation, (4) legislations, and (5) captive breeding. Conservation through genetics is also an important step in conserving these species. Recommendations for conservation of the genus are also discussed; 1. maintenance of ecosystem. 2. more effective monitoring system on the existing protected area. 3. ex-situ conservation, and 4. habitat monitoring.     

Old and new hypotheses about the homology of the compound bones from the cheek and otico-occipital regions of the anuran skull

We studied the larval development of compound bones from the otico-occipital and cheek regions in species of the neobatrachian genera Batrachyla, Hylorina, Leptodactylus, Odontophrynus and Pleurodema. Comparisons were made using a set of Ambystoma spp. (Caudata) and Ceratophrys ornata (Anura; Ceratophryidae) larvae. As suggested by previous studies, we verified the compound nature of the exoccipital (two centers, anurans only), frontoparietal (one center, most anurans and Ambystoma; three centers, some anurans), and squamosal (two centers, all anurans and Ambystoma) bones. We discuss old and new homology hypotheses for each of the compound bone centers in the context of the most widely accepted scenario of lissamphibian origins and relationships, i.e., monophyletic Lissamphibia that includes the clade Batrachia (Caudata + Anura) and the most divergent Gymnophiona. Our findings have a direct impact on our understanding of the composition of the skull in Lissamphibia. We recognized the presence of the following bones: (i) opisthotic (fused to the exoccipital) and tabular (fused to the squamosal) in Batrachia (Anura + Caudata) and (ii) supratemporal (fused to the parietal portion of the frontoparietal) in Anura. Separate centers of the parietal were found only in Pleurodema.     

Synthesis of the tetrasaccharide repeating-unit of the O-specific polysaccharide from Salmonella senftenberg

The oligosaccharide β-d-Man-(1 → 4)-α-l-Rha (1 → 3)-d-Gal-(6 ← 1)-α-d-Glc, which is the repeating unit of the O-specific polysaccharide chain of the lipopolysaccharide from Salmonella senftenberg, was obtained by glycosylation of benzyl 2,4-di-O-benzyl-6-O-(2,3,4-tri-O-benzyl-6-O-p-nitrobenzoyl-α-d-glucopyranosyl)-β-d-galactopyranoside or benzyl 2-O-acetyl-6-O-(2,3,4-tri-O-benzyl-6-O-p-nitrobenzoyl-α-d-glucopyranosyl)-β-d-galactopyranoside with 3-O-acetyl-4-O-(2,3,4,6-tetra-O-acetyl-β-d-mannopyranosyl)-β-l-rhamnopyranose 1,2-(methyl orthoacetate) followed by removal of protecting groups.     

On the occurrence of the ammonite aptychi Lamellaptychus cf. rectecostatus (Peters, 1854) from the Ogrodzieniec quarry (southern Poland)

The largely Kimmeridgian-Tithonian (Late Jurassic) aptychus Lamellaptychus rectecostatus (Peters, 1854) is considered to represent the jaw apparatus of the ammonite superfamily Haploceratoidea (Family Oppeliidae). However, here, from the Ogrodzieniec quarry (southern Poland), we present its unusual allochthonous occurrence embedded in a perisphinctid, Perisphinctes (Kranosphinctes) sp., and co-occurring with a late early Oxfordian Cordatum Subzone (Cordatum Zone) ammonite assemblage. The assemblage includes Cardioceras (Cardioceras) cf. cordatum (Sowerby), Neocampylites delmontanus (Oppel), Lissoceratoides erato (d’Orbigny), Bukowskites distortus (Bukowski), Trimarginites cf. arolicus (Oppel), Glochiceras sp., Holcophylloceras zignodianum (d’Orbigny) and Euaspidoceras (Euaspidoceras) perarmatum (Sowerby).     

Revision and new data of the ammonite family Pseudotissotiidae in the Iberian Trough, Spain

The ammonites assigned to the family Pseudotissotiidae of the Wiedmann (Tübingen, Germany) and Goy, Carretero and Meléndez (Madrid, Spain) collections obtained from the Iberian Trough have been revised. New, mainly lower Turonian, specimens of the species Pseudotissotia sp., Choffaticeras (Choffaticeras) quaasi (Peron, 1904), C. (C.) pavillieri (Pervinquière, 1907), C. (C.) segne (Solger, 1903), C. (C.) sinaiticum (Douvillé, 1928), C. (Leoniceras) luciae (Pervinquière, 1907), C. (L.) barjonai (Choffat, 1898), Wrightoceras llarenai (Karrenberg, 1935), W. munieri (Pervinquière, 1907), W. submunieri Wiedmann, 1975b, and Donenriquoceras forbesiceratiforme Wiedmann, 1960, have been also presented. In addition, we designate and refigure the lectotype of Pseudotissotia (Leoniceras) alaouitense Basse, 1937, and refigure the lectotype of P. barjonai Choffat, 1898. Studies on the morphologies and the geographical and temporal distributions of all of these species have led to the identification of several phylogenetic relationships between them, and to distinguish four main phases in the evolution of the family, characterized by the successive dominance of Choffaticeras (Choffaticeras), Choffaticeras (Leoniceras), Donenriquoceras and Wrightoceras with Donenriquoceras.     

Resolution of the long-standing controversy over the type species of the genus Pseudotypotherium (Notoungulata,Typotheria, Mesotheriidae)

Mesotheres (Notoungulata: Typotheria) are among the most common mammals found in upper Miocene to Pliocene deposits of central Argentina, including the classic type Monte Hermoso locality, which defines the Montehermosan South American Land Mammal “Age”. Nevertheless, the correct name for the mesothere species from this site has been shrouded in uncertainty for well over a century due to questions of taxonomic priority, specimen provenance, and ontogenetic changes in dental formula. Since the mesotheres from Monte Hermoso were named, three distinct species have been formally considered as the type species of the genus: (1) Pseudotypotherium bravardi; (2) “Pseudotypotherium” maendrum; and (3) Pseudotypotherium exiguum. However, none of these species is a nominal species of the Pseudotypotherium genus; all three were originally referred to Typotherium. Article 67.2 of the International Code of Zoological Nomenclature (ICZN, 1999) indicates that only species considered as nominal species are eligible to set the type; in the case of Pseudotypotherium, these include: P. pulchrum, P. carlesi, P. hystatum, and P. carhuense. We conclude that Pseudotypotherium pulchrum F. Ameghino, 1904 (holotype MACN A 10299, Museo Argentino de Ciencias Naturales “Bernardino Rivadavia”, Ameghino Collection), is the type species of the mesotheriid notoungulate genus from Monte Hermoso. According to Article 68.2, F. Ameghino fixed the type by original designation in 1904 when he described P. pulchrum and included “n. g., n. sp.”. Two of the other species previously considered species P. (= T.) bravardi and P. (= T.) exiguum are invalid as type species according to Article 70.2, since their designations overlooked the previous type fixation. The third species (M. (= T.) maendrum) represents a different mesothere genus (Mesotherium) that only occurs in younger (Pleistocene) deposits. Our analysis puts an end to a historical debate that has been ongoing for more than a century regarding the identity of this well-represented late Miocene–Pliocene mesotheriine genus (Pseudotypotherium). This study provides a solid taxonomic foundation for future studies on intraspecific and ontogenetic variation of Pseudotypotherium pulchrum.     

The archaeal exosome localizes to the membrane

We studied the cellular localization of the archaeal exosome, an RNA-processing protein complex containing orthologs of the eukaryotic proteins Rrp41, Rrp42, Rrp4 and Csl4, and an archaea-specific subunit annotated as DnaG. Fractionation of cell-free extracts of Sulfolobus solfataricus in sucrose density gradients revealed that DnaG and the active-site comprising subunit Rrp41 are enriched together with surface layer proteins in a yellow colored ring, implicating that the exosome is membrane-bound. In accordance with this assumption, DnaG and Rrp41 were detected at the periphery of the cell by immunofluorescence microscopy. Our finding suggests that RNA processing in Archaea is spatially organized.

Structured summary

MINT-7891213: Rrp41 (uniprotkb:Q9UXC2) and DnaG (uniprotkb:P95980) colocalize (MI:0403) by cosedimentation in solution (MI:0028)MINT-7891235: Rrp41 (uniprotkb:Q9UXC2), DnaG (uniprotkb:P95980) and SlaA (uniprotkb:Q2M1E7) colocalize (MI:0403) by cosedimentation through density gradient (MI:0029)MINT-7891278: Rrp41 (uniprotkb:Q9UXC2) and DnaG (uniprotkb:P95980) colocalize (MI:0403) by fluorescence microscopy (MI:0416)     

Site-specific cleavage of the 40S ribosomal subunit reveals eukaryote-specific ribosomal protein S28 in the subunit head

After resolving the crystal structure of the prokaryotic ribosome, mapping the proteins in the eukaryotic ribosome is a challenging task. We applied RNase H digestion to split the human 40S ribosomal subunit into head and body parts. Mass spectrometry of the proteins in the 40S subunit head revealed the presence of eukaryote-specific ribosomal protein S28e. Recombinant S28e was capable of specific binding to the 3′ major domain of the 18S rRNA (K_a = 8.0 ± 0.5 × 10⁹ M⁻¹). We conclude that S28e has a binding site on the 18S rRNA within the 40S subunit head.

Structured summary

MINT-8044084: S8 (uniprotkb:P62241) and S19 (uniprotkb:P39019) colocalize (MI:0403) by cosedimentation through density gradient (MI:0029)MINT-8044095: S8 (uniprotkb:P62241), S19 (uniprotkb:P39019) and S13 (uniprotkb:P62277) colocalize (MI:0403) by cosedimentation through density gradient (MI:0029)MINT-8044024: S29 (uniprotkb:P62273), S28 (uniprotkb:P62857), S21 (uniprotkb:P63220), S20 (uniprotkb:P60866), S26 (uniprotkb:P62854), S25 (uniprotkb:P62851), S12 (uniprotkb:P25398), S17 (uniprotkb:P08708), S19 (uniprotkb:P39019), S14 (uniprotkb:P62263), S16 (uniprotkb:P62249) and S11 (uniprotkb:P62280) colocalize (MI:0403) by cosedimentation through density gradient (MI:0029)MINT-8044065: S29 (uniprotkb:P62273), S28 (uniprotkb:P62857), S19 (uniprotkb:P39019), S14 (uniprotkb:P62263) and S16 (uniprotkb:P62249) colocalize (MI:0403) by cosedimentation through density gradient (MI:0029)     

Annotated type catalogue of the Bulimulidae (Mollusca,Gastropoda, Orthalicoidea) in the Natural History Museum,London

The type status is described of 404 taxa classified within the family Bulimulidae (superfamily Orthalicoidea) and kept in the London museum. Lectotypes are designated for Bulimus aurifluus Pfeiffer, 1857; Otostomus bartletti H. Adams, 1867; Helix cactorum d’Orbigny, 1835; Bulimus caliginosus Reeve, 1849; Bulimus chemnitzioides Forbes, 1850; Bulimus cinereus Reeve, 1849; Helix cora d’Orbigny, 1835; Bulimus fallax Pfeiffer, 1853; Bulimus felix Pfeiffer, 1862; Bulimus fontainii d’Orbigny, 1838; Bulimus fourmiersi d’Orbigny, 1837; Bulimus (Mesembrinus) gealei H. Adams, 1867; Bulimus gruneri Pfeiffer, 1846; Bulimus humboldtii Reeve, 1849; Helix hygrohylaea d’Orbigny, 1835; Bulimus jussieui Pfeiffer, 1846; Bulimulus (Drymaeus) binominis lascellianus E.A. Smith, 1895; Helix lichnorum d’Orbigny, 1835; Bulimulus (Drymaeus) lucidus da Costa, 1898; Bulimus luridus Pfeiffer, 1863; Bulimus meleagris Pfeiffer, 1853; Bulimus monachus Pfeiffer, 1857; Bulimus montagnei d’Orbigny, 1837; Helix montivaga d’Orbigny, 1835; Bulimus muliebris Reeve, 1849; Bulimus nigrofasciatus Pfeiffer in Philippi 1846; Bulimus nitelinus Reeve, 1849; Helix oreades d’Orbigny, 1835; Helix polymorpha d’Orbigny, 1835; Bulimus praetextus Reeve, 1849; Bulinus proteus Broderip, 1832; Bulimus rusticellus Morelet, 1860; Helix sporadica d’Orbigny, 1835; Bulimus sulphureus Pfeiffer, 1857; Helix thamnoica var. marmorata d’Orbigny, 1835; Bulinus translucens Broderip in Broderip and Sowerby I 1832; Helix trichoda d’Orbigny, 1835; Bulinus ustulatus Sowerby I, 1833; Bulimus voithianus Pfeiffer, 1847; Bulimus yungasensis d’Orbigny, 1837.The type status of the following taxa is changed to lectotype in accordance with Art. 74.6 ICZN: Bulimulus (Drymaeus) caucaensis da Costa, 1898; Drymaeus exoticus da Costa, 1901; Bulimulus (Drymaeus) hidalgoi da Costa, 1898; Bulimulus (Drymaeus) interruptus Preston, 1909; Bulimulus (Drymaeus) inusitatus Fulton, 1900; Bulimulus latecolumellaris Preston, 1909; Bulimus (Otostomus) napo Angas, 1878; Drymaeus notabilis da Costa, 1906; Drymaeus notatus da Costa, 1906; Bulimulus (Drymaeus) nubilus Preston, 1903; Drymaeus obliquistriatus da Costa, 1901; Bulimus (Drymaeus) ochrocheilus E.A. Smith, 1877; Bulimus (Drymaeus) orthostoma E.A. Smith, 1877; Drymaeus expansus perenensis da Costa, 1901; Bulimulus pergracilis Rolle, 1904; Bulimulus (Drymaeus) plicatoliratus da Costa, 1898; Drymaeus prestoni da Costa, 1906; Drymaeus punctatus da Costa, 1907; Bulimus (Leptomerus) sanctaeluciae E.A. Smith, 1889; Bulimulus (Drymaeus) selli Preston, 1909; Drymaeus subventricosus da Costa, 1901; Bulimulus (Drymaeus) tigrinus da Costa, 1898; Drymaeus volsus Fulton, 1907; Drymaeus wintlei Finch, 1929; Bulimus zhorquinensis Angas, 1879; Bulimulus (Drymaeus) ziczac da Costa, 1898.The following junior subjective synonyms are established: Bulimus antioquensis Pfeiffer, 1855 = Bulimus baranguillanus Pfeiffer, 1853; Drymaeus bellus da Costa, 1906 = Drymaeus blandi Pilsbry, 1897; Bulimus hachensis Reeve 1850 = Bulimus gruneri Pfeiffer, 1846 = Bulimus columbianus Lea, 1838; Bulimus (Otostomus) lamas Higgins 1868 = Bulimus trujillensis Philippi, 1867; Bulimulus (Drymaeus) binominis lascellianus E.A. Smith, 1895 = Bulimulus (Drymaeus) binominis E.A. Smith, 1895; Drymaeus multispira da Costa, 1904 = Helix torallyi d’Orbigny, 1835; Bulimulus (Drymaeus) plicatoliratus Da Costa, 1898 = Bulimus convexus Pfeiffer, 1855; Bulimus sugillatus Pfeiffer, 1857 = Bulimus rivasii d’Orbigny, 1837; Bulimus meridionalis Reeve 1848 [June] = Bulimus voithianus Pfeiffer, 1847.New combinations are: Bostryx montagnei (d’Orbigny, 1837); Bostryx obliquiportus (da Costa, 1901); Bulimulus heloicus (d’Orbigny, 1835); Drymaeus (Drymaeus) lusorius (Pfeiffer, 1855); Drymaeus (Drymaeus) trigonostomus (Jonas, 1844); Drymaeus (Drymaeus) wintlei Finch, 1929; Drymaeus (Mesembrinus) conicus da Costa, 1907; Kuschelenia (Kuschelenia) culminea culminea (d’Orbigny, 1835); Kuschelenia (Kuschelenia) culmineus edwardsi (Morelet, 1863); Kuschelenia (K.) gayi (Pfeiffer, 1857); Kuschelenia (Kuschelenia) tupacii (d’Orbigny, 1835); Kuschelenia (Vermiculatus) anthisanensis (Pfeiffer, 1853); Kuschelenia (Vermiculatus) aquilus (Reeve, 1848); Kuschelenia (Vermiculatus) bicolor (Sowerby I, 1835); Kuschelenia (Vermiculatus) caliginosus (Reeve, 1849); Kuschelenia (Vermiculatus) cotopaxiensis (Pfeiffer, 1853); Kuschelenia (Vermiculatus) filaris (Pfeiffer, 1853); Kuschelenia (Vermiculatus) ochracea (Morelet, 1863); Kuschelenia (Vermiculatus) petiti (Pfeiffer, 1846); Kuschelenia (Vermiculatus) purpuratus (Reeve, 1849); Kuschelenia (Vermiculatus) quechuarum (Crawford, 1939); Naesiotus cinereus (Reeve, 1849); Naesiotus dentritis (Morelet, 1863); Naesiotus fontainii (d’Orbigny, 1838); Naesiotus orbignyi (Pfeiffer, 1846); Protoglyptus pilosus (Guppy, 1871); Protoglyptus sanctaeluciae (E.A. Smith, 1889).Type material of the following taxa is figured herein for the first time: Bulimus cinereus Reeve, 1849; Bulimus coriaceus Pfeiffer, 1857; Bulimulus laxostylus Rolle, 1904; Bulimus pliculatus Pfeiffer, 1857; Bulimus simpliculus Pfeiffer, 1855.     

Some metabolites of 1-bromobutane in the rabbit and the rat

1. Rabbits and rats dosed with 1-bromobutane excrete in urine, in addition to butylmercapturic acid, (2-hydroxybutyl)mercapturic acid, (3-hydroxybutyl)mercapturic acid and 3-(butylthio)lactic acid. 2. Although both species excrete both the hydroxybutylmercapturic acids, only traces of the 2-isomer are excreted by the rabbit. The 3-isomer has been isolated from rabbit urine as the dicyclohexylammonium salt. 3. 3-(Butylthio)lactic acid is formed more readily in the rabbit; only traces are excreted by the rat. 4. Traces of the sulphoxide of butylmercapturic acid have been found in rat urine but not in rabbit urine. 5. In the rabbit about 14% and in the rat about 22% of the dose of 1-bromobutane is excreted in the form of the hydroxymercapturic acids. 6. Slices of rat liver incubated with S-butylcysteine or butylmercapturic acid form both (2-hydroxybutyl)mercapturic acid and (3-hydroxybutyl)mercapturic acid, but only the 3-hydroxy acid is formed by slices of rabbit liver. 7. S-Butylglutathione, S-butylcysteinylglycine and S-butylcysteine are excreted in bile by rats dosed with 1-bromobutane. 8. Rabbits and rats dosed with 1,2-epoxybutane excrete (2-hydroxybutyl)mercapturic acid to the extent of about 4% and 11% of the dose respectively. 9. The following have been synthesized: N-acetyl-S-(2-hydroxybutyl)-l-cysteine [(2-hydroxybutyl)mercapturic acid] and N-acetyl-S-(3-hydroxybutyl)-l-cysteine [(3-hydroxybutyl)mercapturic acid] isolated as dicyclohexylammonium salts, N-toluene-p-sulphonyl-S-(2-hydroxybutyl)-l-cysteine, S-butylglutathione and N-acetyl-S-butylcysteinyl-glycine ethyl ester.     

Reconsidering locomotor habits and life style of the Balearic insular giant rodent Hypnomys Bate, 1918 from the allometry of the limb long bones

The genus Hypnomys Bate, 1918 includes some endemic Neogene chronospecies from Mallorca and Menorca, evolved in insularity conditions from the Lower Pliocene to the human arrival at the archipelago. The study of the allometric proportions (functional length and sagittal diameter) of the limbs’ long bones of Hypnomys eliomyoides Agusti, 1980 (Lower Pleistocene of Menorca), Hypnomys sp. (Pleistocene of Menorca), Hypnomys onicensis (Reumer, 1994) (Upper Pliocene-Lower Pleistocene of Mallorca) and Hypnomys morpheus Bate, 1918 (Upper Pleistocene of Mallorca) only indicates small differences with the garden dormouse (Eliomys quercinus Linnaeus, 1776) and other mainland rodents and insectivores. The study about the locomotion type by means of Similarity Matrix of Bou indicates that 1) Hypnomys spp. presents the greater similarities with the arboreal, jumping and gliding species; 2) the jumping and digging life style of Hypnomys spp. are more developed (25%) than in E. quercinus; 3) the walking locomotion of Hypnomys spp. is only a 7% greater than in E. quercinus; and 4) the degree of similarity with the gliding locomotion of Hypnomys sp. is greater (17%) than in E. quercinus. Some of this data indicates that Hypnomys spp. was better adapted to the arboreal life than E. quercinus, due to the relationship between the jumping and gliding capacities with the arboreal locomotion. The greater similarity of Hypnomys spp. with the walking locomotion does not necessarily involve more terrestrial habits. Our interpretation contrasts with earlier conclusions of Hypnomys life style (Hypnomys cf. onicensis and Hypnomys morpheus) where the terrestrial locomotion was overestimated in front of the arboreal locomotion. The locomotion type of Hypnomys would be related with the presence of important forest masses on the Balearic Islands during the Neogene, a different degree of environmental stress from that of the mainland ecosystems and a probable expansion of the ecological niche occupied by these species.     

S100 proteins interact with the N-terminal domain of MDM2

S100 proteins interact with the transactivation domain and the C-terminus of p53. Further, S100B has been shown to interact with MDM2, a central negative regulator of p53. Here, we show that S100B bound directly to the folded N-terminal domain of MDM2 (residues 2-125) by size exclusion chromatography and surface plasmon resonance experiments. This interaction with MDM2 (2-125) is a general feature of S100 proteins; S100A1, S100A2, S100A4 and S100A6 also interact with MDM2 (2-125). These interactions with S100 proteins do not result in a ternary complex with MDM2 (2-125) and p53. Instead, we observe the ability of a subset of S100 proteins to disrupt the extent of MDM2-mediated p53 ubiquitylation in vitro.

Structured summary

MINT-7905256: MDM2 (uniprotkb:Q00987) binds (MI:0407) to s100A6 (uniprotkb:P06703) by surface plasmon resonance (MI:0107)MINT-7905063: MDM2 (uniprotkb:Q00987) and s100A1 (uniprotkb:P23297) bind (MI:0407) by molecular sieving (MI:0071)MINT-7905376: s100A4 (uniprotkb:P26447) and MDM2 (uniprotkb:Q00987) physically interact (MI:0915) by competition binding (MI:0405)MINT-7905130: s100A6 (uniprotkb:P06703) and MDM2 (uniprotkb:Q00987) bind (MI:0407) by molecular sieving (MI:0071)MINT-7905207: s100A6 (uniprotkb:P06703) and p53 (uniprotkb:P04637) bind (MI:0407) by molecular sieving (MI:0071)MINT-7905043: s100B (uniprotkb:P04271) and MDM2 (uniprotkb:Q00987) bind (MI:0407) by molecular sieving (MI:0071)MINT-7905196: p53 (uniprotkb:P04637) and s100A4 (uniprotkb:P26447) bind (MI:0407) by molecular sieving (MI:0071)MINT-7905358: p53 (uniprotkb:P04637) and s100A4 (uniprotkb:P26447) physically interact (MI:0915) by fluorescence polarization spectroscopy (MI:0053)MINT-7905220: MDM2 (uniprotkb:Q00987) binds (MI:0407) to s100B (uniprotkb:P04271) by surface plasmon resonance (MI:0107)MINT-7905104: s100A4 (uniprotkb:P26447) and MDM2 (uniprotkb:Q00987) bind (MI:0407) by molecular sieving (MI:0071)MINT-7905229: MDM2 (uniprotkb:Q00987) binds (MI:0407) to s100A1 (uniprotkb:P23297) by surface plasmon resonance (MI:0107)MINT-7905317, MINT-7905162: s100B (uniprotkb:P04271) and p53 (uniprotkb:P04637) bind (MI:0407) by molecular sieving (MI:0071)MINT-7905238: MDM2 (uniprotkb:Q00987) binds (MI:0407) to s100A2 (uniprotkb:P29034) by surface plasmon resonance (MI:0107)MINT-7905174, MINT-7905308: s100A1 (uniprotkb:P23297) and p53 (uniprotkb:P04637) bind (MI:0407) by molecular sieving (MI:0071)MINT-7905247: MDM2 (uniprotkb:Q00987) binds (MI:0407) to s100A4 (uniprotkb:P26447) by surface plasmon resonance (MI:0107)MINT-7905090: s100A2 (uniprotkb:P29034) and MDM2 (uniprotkb:Q00987) bind (MI:0407) by molecular sieving (MI:0071)MINT-7905142, MINT-7905326: MDM2 (uniprotkb:Q00987) and p53 (uniprotkb:P04637) bind (MI:0407) by molecular sieving (MI:0071)MINT-7905185, MINT-7905347: s100A2 (uniprotkb:P29034) and p53 (uniprotkb:P04637) bind (MI:0407) by molecular sieving (MI:0071)     

Evidence for leptin receptor isoforms heteromerization at the cell surface

Leptin mediates its metabolic effects through several leptin receptor (LEP-R) isoforms. In humans, long (LEPRb) and short (LEPRa,c,d) isoforms are generated by alternative splicing. Most of leptin’s effects are believed to be mediated by the OB-Rb isoform. However, the role of short LEPR isoforms and the possible existence of heteromers between different isoforms are poorly understood. Using BRET1 and optimized co-immunoprecipitation, we observed LEPRa/b and LEPRb/c heteromers located at the plasma membrane and stabilized by leptin. Given the widespread coexpression of LEPRa and LEPRb, our results suggest that LEPRa/b heteromers may represent a major receptor species in most tissues.

Structured summary

MINT-7714817: LEPRb (uniprotkb:P48357-1) physically interacts (MI:0915) with LEPRb (uniprotkb:P48357-1) by anti tag co-immunoprecipitation (MI:0007)MINT-7714785: LEPRc (uniprotkb:P48357-2) physically interacts (MI:0915) with LEPRc (uniprotkb:P48357-2) by bioluminescence resonance energy transfer (MI:0012)MINT-7714951, MINT-7714744: LEPRa (uniprotkb:P48357-3) physically interacts (MI:0915) with LEPRa (uniprotkb:P48357-3) by bioluminescence resonance energy transfer (MI:0012)MINT-7714859: LEPRb (uniprotkb:P48357-1) physically interacts (MI:0915) with LEPRa (uniprotkb:P48357-3) by anti tag co-immunoprecipitation (MI:0007)MINT-7714885, MINT-7714672: LEPRb (uniprotkb:P48357-1) physically interacts (MI:0915) with LEPRb (uniprotkb:P48357-1) by bioluminescence resonance energy transfer (MI:0012)MINT-7714835: LEPRa (uniprotkb:P48357-3) physically interacts (MI:0915) with LEPRa (uniprotkb:P48357-3) by anti tag co-immunoprecipitation (MI:0007)MINT-7714914, MINT-7714723, MINT-7714759: LeprB (uniprotkb:P48357-1) physically interacts (MI:0915) with LEPRa (uniprotkb:P48357-3) by bioluminescence resonance energy transfer (MI:0012)MINT-7714703, MINT-7714936, MINT-7714772: LEPRb (uniprotkb:P48357-1) physically interacts (MI:0915) with LEPRc (uniprotkb:P48357-2) by bioluminescence resonance energy transfer (MI:0012)MINT-7714872: LEPRb (uniprotkb:P48357-1) physically interacts (MI:0915) with LEPRc (uniprotkb:P48357-2) by anti tag co-immunoprecipitation (MI:0007)     

NLS-mediated NPC functions of the nucleoporin Pom121

RanGTP mediates nuclear import and mitotic spindle assembly by dissociating import receptors from nuclear localization signal (NLS) bearing proteins. We investigated the interplay between import receptors and the transmembrane nucleoporin Pom121. We found that Pom121 interacts with importin α/β and a group of nucleoporins in an NLS-dependent manner. In vivo, replacement of Pom121 with an NLS mutant version resulted in defective nuclear transport, induction of aberrant cytoplasmic membrane stacks and decreased cell viability. We propose that the NLS sites of Pom121 affect its function in NPC assembly both by influencing nucleoporin interactions and pore membrane structure.

Structured summary

MINT-7951230: pom121 (uniprotkb:Q5EWX9) physically interacts (MI:0914) with nup155 (uniprotkb:O75694), Nup133 (uniprotkb:Q8WUM0) and Importin beta (uniprotkb:Q14974) by pull down (MI:0096)MINT-7951210: pom121 (uniprotkb:Q5EWX9) physically interacts (MI:0915) with Importin alpha (uniprotkb:P52170) and Importin beta (uniprotkb:P52297) by pull down (MI:0096)MINT-7951183: pom121 (uniprotkb:Q5EWX9) physically interacts (MI:0914) with nup155 (uniprotkb:Q7ZWL0), nup160 (uniprotkb:P83722), nup205 (uniprotkb:Q642R6), nup93 (uniprotkb:Q7ZX96), Importin beta (uniprotkb:P52297) and nup62 (uniprotkb:Q91349) by pull down (MI:0096)MINT-7951416: pom121 (uniprotkb:Q5EWX9) physically interacts (MI:0914) with nup155 (uniprotkb:Q7ZWL0), nup93 (uniprotkb:Q7ZX96) and Importin beta (uniprotkb:P52297) by pull down (MI:0096)MINT-7951276: pom121 (uniprotkb:Q5EWX9) physically interacts (MI:0914) with nup155 (uniprotkb:Q7ZWL0), nup205 (uniprotkb:Q642R6), nup93 (uniprotkb:Q7ZX96), Importin beta (uniprotkb:P52297) and nup62 (uniprotkb:Q91349) by pull down (MI:0096)MINT-7951306, MINT-7951362: pom121 (uniprotkb:Q5EWX9) physically interacts (MI:0914) with nup155 (uniprotkb:Q7ZWL0), nup160 (uniprotkb:P83722), nup93 (uniprotkb:Q7ZX96), Importin beta (uniprotkb:P52297) and nup62 (uniprotkb:Q91349) by pull down (MI:0096)     

Integrated biostratigraphy for the Santonian/Campanian boundary interval,the Kurdistan Region,northeast Iraq

The first high-resolution integrated biostratigraphic study for Santonian/Campanian sediments of the Tabin section in the Kurdistan Region, northeast Iraq is provided. The study, based on 28 closely spaced samples, combines data from planktic foraminifers (25 species), calcareous nannofossils (32 species) and two ammonite genera in the Kometan Formation, marking the Santonian/Campanian boundary (S/C boundary) in the Kurdistan Region. In the absence of the crinoid Marsupites testudinarius, the proposed boundary marker, secondary markers such as calcareous nannofossils, planktic foraminifers and ammonites, have been used to establish a multi-stratigraphic biozonation for the late Santonian–early Campanian duration. Based on the occurrences of calcareous nannofossils, three biozones are identified — Lucianorhabdus cayeuxii (late Santonian), Calculites obscurus (latest Santonian–earliest Campanian), and Broinsonia parca parca (early Campanian). Seven calcareous nannofossil bioevents and three planktic foraminiferal bioevents are also identified. The Santonian/Campanian boundary is marked by: (a) the LO (Last Occurrence) of the planktic foraminifera D. asymetrica, (b) the FOs (First Occurrence) of the calcareous nannofossil species B. parca parca and B. parca constricta, (c) the extinction of several planktic foraminiferal species of Dicarinella and Marginotruncana, (d) the abundance and diversification of the planktic foraminifera genera, Globotruncana and Globotruncanita at the beginning of the Campanian, and (e) the disappearance of the ammonite genus Texanites, 0.5 m below (i.e., at 19 m) the disappearance of all Dicarinella and Marginotruncana species in the study section. Similar to several other Tethyan sections, the FO of B. parca parca is above the LOs of D. concavata and D. asymetrica; the LO of D. asymetrica is used here to mark the S/C boundary