螺序草属三新种

本文发表了螺序草属三新种, 即粘毛螺序草Spiradiclis tomentosa, 糙边螺序草S.scabrida, 锈茎螺序草S.ferruginea.     

大兴安岭花■属一新亚种

兴安花葱 新亚种 图 Polemonium boreal. Adams subsp. hingganicum P. H. Huanget S. Y. Li, subsp. nov. A typo differt statura multo majore, 30-70cm alta, folio-     

广西螺序草属一新种

本文发表了螺序草属一新种,即毛螺序草Spiradiclis villosa X.X.Chen et W.L.Sha.     

广西螺序草属药用植物一新种

<正> 矮小草本,通常莲座状;茎不分枝,下部生根;节间缩短,长3—4毫米。叶密集对生,叶片纸质,匙形或卵状倒披针形,长8—13厘米,宽2—4.5厘米,先端钝或圆形,基部狭楔形,下延,边全缘,有睫毛,干时上面榄绿色,疏被短柔毛,下面苍白色,沿中脉和侧脉密被柔毛;侧脉每边15—25条,和中脉均在下面突起;叶柄长5—8毫米;托叶披针状线形或线形,长7—9毫米,密被柔毛。聚伞花序顶生,有花10多朵;花序梗长7—12厘     

贵州菝葜属一新种

花叶菝葜 新种 图1 Smilax guiyangensis C. X. Fu et C. D. Shen, sp. nov. Species habitu S. basilatae Wang et Tang similis, sed rhizomatibus horizontalibus insolo, caulibus 5～40 cm altis longitudinaliter quadrangulatis, foliorum laminis supra albo-striatis, pedunculis petiolis multo longioribus differt.     

GEOPHILA EXIGUA LI名实辨正

李惠林(1944)曾发表爱地草属一新种,即Geophila exigua Li,该新种的正模(Holotype)曾怀德62112采自广东仁化万池山,副模(Paratype)曾怀德20330采自广东增城南昆山。二者都是花标本,没有果实。近年来在上述产地或其邻近地区采到了更多更完整的标本。作者在仔细研究了这些材料以后,发现:1.Geophila exigua Li的正模和副模(作者只看到同号复份)分别代表两种完全不同的植物;2.这两种植物均不属爱地草属Geophila Don;3.这两种植物应归入不同的属。 为便于说明问题,现根据作者研究上述正模和副模(复份标本)的结果,并参考后来采到的果实标本,将其主要异同点列于表1。     

广西扁担杆属(椴树科)-新种-阔腺扁担杆

阔腺扁担杆新种图1 Grewia latiglandulosa Z. Y. Huang et S. Y. Liu,sp. nov. Fig. 1 Affinis G. oligandro Peirre, sed foliis in sicco viridibus, supra minutis stellato-pilosis, subtus dense stellato-pilosis, margine aeque serrulotis, petiolis brevioribus 2-3 mm longis, cymis 1-3 -floriferis, pedunculis pedicellisque longioribus, sepalis multo majoribus,1-1.2 cm longis, 2-3 mm latis, glandulis magnis subquadratis, androgynophoris praeditis, stylis pilosis,drupis indivisis vel bifidis differt.     

药用贝母新资源

1.宁国贝母 新种 图1,1—4 Fritillaria ningguoensis S.C.Chen et S.F.Yin,sp.nov. Proxima F.monanthac Migo,quae planta multo altiore,foliis pro 2/3longitudinem caulis sparsim dispositis,lobis stigmatis 3.5—5mm longis differt. Planta pumilior,16—27cm longa,bulbis interdum binis,ovoideo-globosis,ca 1.5—2cm in diam.,squamis paucis(2—3),albidis,carnosis.Caulis gla-ber,plerumque 8-foliatus.Folia supra medium caulis densiuscule disposita,vulgo opposita,erecto-patentia,oblonga vel suboblonga,5.5—9.5cm longa,     

杜鹃属一新种(英文)

Rhododendron brevicaudatum R. C. Fang et S. S. Chang, sp. nov. (Subgen. Rhododendron, Sect. Rhododendron, Subsect. Micrantha) Species affinis R, mieranlhi Turcz., sed foliis multo majoribus, 9—12.5×2.5—3.3 cm, apice breve caudato-acuminatis, basi subrotundatis, subtus indumento arachnoideo obsolete obtectis, corollis et capsulis majoribus differt.     

螺序草属(茜草科)的种子形态

对螺序草属(Spiradiclis B1、)16种2变型共18个样品的种子形态特征的初步研究表明,本属植物种子为小型（0．2—0、3mm)或中型(0．3—2mm),整体形状不太规则,表面纹饰为蜂窝状,种脐稍突出。种子的外壁由内外2层种皮组成。依据表面突起分布方式,螺序草属的种子大致分为2种类型：(1)平周壁微下陷,疣突均匀分布于其上,如大叶螺序草、螺序草、尖叶螺序草、柳叶螺序草、峨嵋螺序草和龙州螺序草;(2)平周壁下陷成穴状,突起分布在穴边缘,如红花螺序草、心叶螺序草、两广螺序草、广东螺序草、海南螺序草、宽昭螺序草、疏花螺序草、多枝螺序草、罗氏螺序草、小叶螺序草、石生螺序草和紫花螺序草。螺序草属的种子形态特征对属下类群的划分具有重要的参考价值。     

Leishmaniasis worldwide and global estimates of its incidence

As part of a World Health Organization-led effort to update the empirical evidence base for the leishmaniases, national experts provided leishmaniasis case data for the last 5 years and information regarding treatment and control in their respective countries and a comprehensive literature review was conducted covering publications on leishmaniasis in 98 countries and three territories (see 'Leishmaniasis Country Profiles Text S1, S2, S3, S4, S5, S6, S7, S8, S9, S10, S11, S12, S13, S14, S15, S16, S17, S18, S19, S20, S21, S22, S23, S24, S25, S26, S27, S28, S29, S30, S31, S32, S33, S34, S35, S36, S37, S38, S39, S40, S41, S42, S43, S44, S45, S46, S47, S48, S49, S50, S51, S52, S53, S54, S55, S56, S57, S58, S59, S60, S61, S62, S63, S64, S65, S66, S67, S68, S69, S70, S71, S72, S73, S74, S75, S76, S77, S78, S79, S80, S81, S82, S83, S84, S85, S86, S87, S88, S89, S90, S91, S92, S93, S94, S95, S96, S97, S98, S99, S100, S101'). Additional information was collated during meetings conducted at WHO regional level between 2007 and 2011. Two questionnaires regarding epidemiology and drug access were completed by experts and national program managers. Visceral and cutaneous leishmaniasis incidence ranges were estimated by country and epidemiological region based on reported incidence, underreporting rates if available, and the judgment of national and international experts. Based on these estimates, approximately 0.2 to 0.4 cases and 0.7 to 1.2 million VL and CL cases, respectively, occur each year. More than 90% of global VL cases occur in six countries: India, Bangladesh, Sudan, South Sudan, Ethiopia and Brazil. Cutaneous leishmaniasis is more widely distributed, with about one-third of cases occurring in each of three epidemiological regions, the Americas, the Mediterranean basin, and western Asia from the Middle East to Central Asia. The ten countries with the highest estimated case counts, Afghanistan, Algeria, Colombia, Brazil, Iran, Syria, Ethiopia, North Sudan, Costa Rica and Peru, together account for 70 to 75% of global estimated CL incidence. Mortality data were extremely sparse and generally represent hospital-based deaths only. Using an overall case-fatality rate of 10%, we reach a tentative estimate of 20,000 to 40,000 leishmaniasis deaths per year. Although the information is very poor in a number of countries, this is the first in-depth exercise to better estimate the real impact of leishmaniasis. These data should help to define control strategies and reinforce leishmaniasis advocacy.     

Effects of aminoethylation of cysteine residues on the structural and functional activities of the Escherichia coli 30 S ribosomal proteins

The purified 30 S ribosomal proteins from Escherichia coli strain Q13 were chemically modified by reaction with ethyleneimine, specifically converting cysteine residues to S-2-aminoethylcysteine residues. Proteins S1, S2, S4, S8, S11, S12, S13, S14, S17, S18 and S21 were found to contain aminoethylcysteine residues after modification, whereas proteins S3, S5, S6, S7, S9, S10, S15, S16, S19 and S20 did not. Aminoethylated proteins S4, S13, S17 and S18 were active in the reconstitution of 30 S ribosomes and did not have altered functional activities in poly(U)-dependent polyphenylalanine synthesis, R17-dependent protein synthesis, fMet-tRNA binding and Phe-tRNA binding. Aminoethylated proteins S2, S11, S12, S14 and S21 were not active in the reconstitution of complete 30 S ribosomes, either because the aminoethylated protein did not bind stably to the ribosome (S2, S11, S12 and S21) or because the aminoethylated protein did not stabilize the binding of other ribosomal proteins (S14). The functional activities of 30 S ribosomes reconstituted from a mixture of proteins containing one sensitive aminoethylated protein (S2, S11, S12, S14 or S21) were similar to ribosomes reconstituted from mixtures lacking that protein. These results imply that the sulfhydryl groups of the proteins S4, S13, S17 and S18 are not necessary for the structural or functional activities of these proteins, and that aminoethylation of the sulfhydryl groups of S2, S11, S12, S14 and S21 forms either a kinetic or thermodynamic barrier to the assembly of active 30 S ribosomes in vitro.     

Determination of S-genotypes of pear (Pyrus pyrifolia) cultivars by S-RNase sequencing and PCR-RFLP analyses

The pear (Pyrus pyrifolia) has gametophytic self-incompatibility (GSI). To elucidate the S-genotypes of Korean-bred pear cultivars, whose parents are heterozygotes, the PCR amplification using S-RNase primers that are specific for each S-genotype was carried out in 15 Korean-bred pear cultivars and 5 Japanese-bred pear cultivars. The difference of the fragment length was shown in the following order: S6 (355 bp) < S7 (360 bp) < S1 (375 bp) < S4 (376 bp) < S3 and S5 (384 bp) < S8 (442 bp) < S9 (1,323 bp) < S2 (1,355 bp). We analyzed the sequence of the S-RNase gene, which had introns of various sizes in the hypervariable (HV) region between the adjacent exons with a fairly high homology. The sizes of the introns were as follows: S1 = 167 bp, S2 = 1,153 bp, S3 = 179 bp, S4 = 168 bp, S5 = 179 bp, S6 = 147 bp, S7 = 152 bp, S8 = 234 bp, S9 = 1,115 bp. There were five conservative and five hypervariable regions in the introns of S1, S3, S4, S5, S6 and S-RNases. A pairwise comparison of these introns of S-RNases revealed homologies as follows: 93.7% between S1- and S4-RNases, 93.3% between S3- and S5-RNases and 78.9% between S6- and S7-RNases. PCR-RFLP and S-RNases sequencing determined the S-genotypes of the pear cultivars. The S-genotypes were S4S9 for Shinkou, S3S9 for Niitaka, S3S5 for Housui, S1S5 for Kimizukawase, S1S8 for Ichiharawase, S3S5 for Mansoo, S3S4 for Shinil, S3S4 for Whangkeumbae, S3S5 for Sunhwang, S3S5 for Whasan, S3S5 for Mihwang, S5S? for Chengsilri, S3S5 for Gamro, S3S4 for Yeongsanbae, S3S4 for Wonhwang, S3S5 for Gamcheonbae, S3S5 for Danbae, S3S4 for Manpoong, S3S4 for Soowhangbae and S4S6 for Chuwhangbae. The information on the S-genotypes of pear cultivars will be used for the pollinizer selection and breeding program.     

Contacts of ribosomal proteins with tRNAPhe and 16S RNA in analogs of the 30S initiation complex

Direct RNA-protein contacts have been studied by means of ultraviolet-induced (254 nm) cross-links inside complexes of NAcPhe-tRNAPhe, Phe-tRNAPhe and deacylated tRNAPhe with poly(U)-charged 30S subunit of Escherichia coli ribosome. In the first two complexes tRNA directly contacts with the similar sets of proteins (S4, S5, S7, S9/S11; S6 and S8 are found only in the second complex). These sets are similar to that in the fMet-tRNAfMet X 30S X mRNA complex, evidencing similar disposition of tRNAs in these three complexes. 16S RNA contacts in free 30S subunit mainly with proteins S4, S7 and S9/S11. In both complexes, containing NAcPhe-tRNAPhe and Phe-tRNAPhe, 16S RNA contacts with essentially the same proteins (S4, S5, S7, S8, S9/S11, S10, S15, S16 and S17) and in the same ratio, evidencing similar conformation of 30S subunit in these two complexes. In the third complex deacylated tRNAPhe contacts with proteins S4, S5, S6, S8, S9/S11 and S15, 16S RNA-protein interaction differs from those in the first two complexes by a remarkable decrease of cross-linked proteins S8, and S9/S11 and by the appearance of a large amount of cross-linked proteins(s) S13/S14. Hence, this complex differs from the first two by conformation of 30S subunit and, probably, by disposition and/or conformation of tRNA.     

Positions of proteins S14, S18 and S20 in the 30 S ribosomal subunit of Escherichia coli

A map of the 30 S ribosomal subunit is presented giving the positions of 15 of its 21 proteins. The components located in the map are S1, S3, S4, S5, S6, S7, S8, S9, S10, S11, S12, S14, S15, S18 and S20.     

A survey of the genus Sorbaria (Rosaceae)

A taxonomic revision of the Asiatic genus Sorbaria (Rosaceae). 4 species are recognized: S. sorbifolia (including S. stellipila), S. grandiflora (= S. pallasii incl. S. rhoifolia), S. kirilowii,(incl. S. arborea and S. assurgens ) and S. tomentosa (= S. lindleyana , incl. S. olgae and S. gilgitensis ) with var. angustifolia , comb. nov. (= S. aitchisonii ). Hybrids presumably between S. sorbifolia and S. grandiflora and S. sorbifolia and S. kirilowii are found cultivated.     

Central domain assembly: thermodynamics and kinetics of S6 and S18 binding to an S15-RNA complex

The 30 S ribosomal subunit assembles in vitro through the hierarchical binding of 21 ribosomal proteins to 16 S rRNA. The central domain of 16 S rRNA becomes the platform of the 30 S subunit upon binding of ribosomal proteins S6, S8, S11, S15, S18 and S21. The assembly of the platform is nucleated by binding of S15 to 16 S rRNA, followed by the cooperative binding of S6 and S18. The prior binding of S6 and S18 is required for binding of S11 and S21. We have studied the mechanism of the cooperative binding of S6 and S18 to the S15-rRNA complex by isothermal titration calorimetry and gel mobility shift assays with rRNA and proteins from the hyperthermophilic bacterium Aquifex aeolicus. S6 and S18 form a stable heterodimer in solution with an apparent dissociation constant of 8.7 nM at 40 degrees C. The S6:S18 heterodimer binds to the S15-rRNA complex with an equilibrium dissociation constant of 2.7 nM at 40 degrees C. Consistent with previous studies using rRNA and proteins from Escherichia coli, we observed no binding of S6 or S18 in the absence of the other protein or S15. The presence of S15 increases the affinity of S6:S18 for the RNA by at least four orders of magnitude. The kinetics of S6:S18 binding to the S15-rRNA complex are slow, with an apparent bimolecular rate constant of 8.0 x 10(4) M(-1) s(-1) and an apparent unimolecular dissociation rate of 1.6 x 10(-4) s(-1). These results, which are consistent with a model in which S6 and S18 bind as a heterodimer to the S15-rRNA complex, provide a mechanistic framework to describe the previously observed S15-mediated cooperative binding of S6 and S18 in the ordered assembly of a multi-protein ribonucleoprotein complex.     

Binding of 16S rRNA to chloroplast 30S ribosomal proteins blotted on nitrocellulose

Protein-RNA associations were studied by a method using proteins blotted on a nitrocellulose sheet. This method was assayed with Escherichia Coli 30S ribosomal components. In stringent conditions (300 mM NaCl or 20° C) only 9 E. coli ribosomal proteins strongly bound to the 16S rRNA: S4, S5, S7, S9, S12, S13, S14, S19, S20. 8 of these proteins have been previously found to bind independently to the 16S rRNA. The same method was applied to determine protein-RNA interactions in spinach chloroplast 30S ribosomal subunits. A set of only 7 proteins was bound to chloroplast rRNA in stringent conditions: chloroplast S6, S10, S11, S14, S15, S17 and S22. They also bound to E. coli 16S rRNA. This set includes 4 chloroplast-synthesized proteins: S6, S11, S15 and S22. The core particles obtained after treatment by LiCl of chloroplast 30S ribosomal subunit contained 3 proteins (S6, S10 and S14) which are included in the set of 7 binding proteins. This set of proteins probably play a part in the early steps of the assembly of the chloroplast 30S ribosomal subunit.     

Proteomic characterization of the small subunit of Chlamydomonas reinhardtii chloroplast ribosome: identification of a novel S1 domain-containing protein and unusually large orthologs of bacterial S2, S3, and S5

To understand how chloroplast mRNAs are translated into functional proteins, a detailed understanding of all of the components of chloroplast translation is needed. To this end, we performed a proteomic analysis of the plastid ribosomal proteins in the small subunit of the chloroplast ribosome from the green alga Chlamydomonas reinhardtii. Twenty proteins were identified, including orthologs of Escherichia coli S1, S2, S3, S4, S5, S6, S7, S9, S10, S12, S13, S14, S15, S16, S17, S18, S19, S20, and S21 and a homolog of spinach plastid-specific ribosomal protein-3 (PSRP-3). In addition, a novel S1 domain-containing protein, PSRP-7, was identified. Among the identified proteins, S2 (57 kD), S3 (76 kD), and S5 (84 kD) are prominently larger than their E. coli or spinach counterparts, containing N-terminal extensions (S2 and S5) or insertion sequence (S3). Structural predictions based on the crystal structure of the bacterial 30S subunit suggest that the additional domains of S2, S3, and S5 are located adjacent to each other on the solvent side near the binding site of the S1 protein. These additional domains may interact with the S1 protein and PSRP-7 to function in aspects of mRNA recognition and translation initiation that are unique to the Chlamydomonas chloroplast.     

A Comparison of the Native and Derived 30S and 50S Ribosomes of Escherichia coli

Four types of ribosomes occurring in E. coli have been separated by sucrose gradient centrifugation. These are the 30S and 50S particles occurring in E. coli extracts (native particles), and the 30S and 50S particles which are the subunits of 70S ribosomes (derived particles). Two criteria were used in comparing these particles: (1) The type of RNA contained in each, as determined by sedimentation velocity in the analytical ultracentrifuge. (2) The ability of mixtures of 30S and 50S ribosomes (derived 30S + derived 50S, native 30S + native 50S) to undergo the reaction: [Formula: see text] Native and derived 30S particles were found to contain 16S RNA. Derived 50S particles contained 23S RNA and a small amount of 15 to 20S RNA, whereas native 50S ribosomes contained only 16S RNA. Derived 30S and 50S particles combined to form 70S particles. However, under identical conditions, native 30S and 50S particles did not form 70S ribosomes.