Book Reviews

Books review in this article:
The Biochemical Basis of Neuropharmacology (5th edition) by J. R. Cooper, F. E. Bloom, and R. H. Roth
Animal Cell Culture, a Practical Approach by R. I. Freshney
Folates and Pterins. Nutritional Pharmacological and Physiological Aspects , Vol. 3 edited by R. L. Blakley and V. M. Whitehead
MPTP: A Neurotoxin Producing a Parkinsonian Syndrome edited by S. P. Markey, N. Castagnoli Jr., A. J. Trevor, and I. J. Kopin
GABAergic Mechanisms in the Mammalian Periphery edited by S. L. Erdö and N. G. Bowery     

Reviews

Books reviewed in this article:
Molecular Biology of Photosynthesis. Ed. By G ovindjee , H. J. B ohnert , W. B ottomley , D. A. B ryant , J. E. M ullet , W. L. O gren , H. P akrasi and C. R. S omerville .
Biochemical and Physiological Aspects of Ethylene Production in Lower and Higher Plants. Ed. by H. C lijsters , M. de P roft , R. M arcelle and M. V an P oucke .
Nitrogen, Phosphorus and Sulphur Utilisation by Fungi. By L. B oddy , R. M archant and D. J. R ead .
Fungi and Ecological Disturbance. Ed. by L. B oddy , R. W atling and A. J. E. L yon .
Phytoplankton , 2nd Edn. By A. D. B oney .
The Holocene: An Environmental History. By N eil R oberts .
Chambers Biology Dictionary. Ed. by P. M. B. W alker , C.B.E., F.R.S.E.     

Book Reviews

Benzodiazepine Recognition Site Ligands: Biochemistry and Pharmacology (Advances in Biochemical Psychopharmacology, Vol. 38) edited by G. Biggio and E. Costa
Experimental Allergic Encephalomyelitis—A Useful Model for Multiple Sclerosis (Progress in Clinical and Biological Research, Vol. 146) edited by E. C. Alvoid, M. W. Kies, and A. J. Suckling. Alan R. Liss
Cellular Components of the Cerebral Cortex (Cerebral Cortex, Vol. 1) edited by A. Peters and E. G. Jones     

BOOK REVIEWS

Book Review in This Article:
The Endorphins Advances in Biochemical Psychopharmacology, Vol. 18 (Editors E. C osta & M. T rabucchi )
Structure and Function of Cells by C. R. H opkins
Mechanisms, Regulation and Special Functions of Protein Synthesis in the Brain (Editors S. R oberts , A. L ajtha & W. H. G ispen )
Progress in Neurobiology (Editors G. A. K erkut & J. W. P hillis )     

REVIEWS

Environmental Control of Plant Growth . Edited by L. T. E vans .
Flora of the British Isles, Illustrations. Part 3. Boraginaceae to Compositae . Drawings by S ybil J. R oles .
The Germination of Seeds . By A. M. M ayer and A. P oljakoff -M ayber .
Chromosome Botany and the Origins of Cultivated Plants . By C. D. D arlington .
Recherches Physiologiques sur le Repos Vegetatif de la Vigne (Vitis vinifera L .): La Dor-mance des Bourgeons et le Mecanisme de sa Disparition . By R. Pouget.
Radiation Induced Chromosome Aberrations . Edited by S heldon W olff .
John Clayton, Pioneer of American Botany . By E dmund and D orothy S mith B erkeley .
The Absorption of Solutes by Plant Cells . By D. H. J ennings .
Woody Flora of Taiwan . By HUI-LIN LI.
The Annual Species of Medicago. By C haia C lara H eyn .
The Flowering Process . By F rank B. S alisbury .
General Microbiology . By R oger J. S tanier , M ichael D udoroff and E dward A. A delberg .
The Biochemical Approach to Life . By F. R. J evons .     

Reovirus M2 gene is associated with chromium release from mouse L cells.

In this study, we investigated the interaction of reovirus particles with cell membranes by using a 51Cr release assay. We confirmed prior observations (J. Borsa, B. D. Morash, M. D. Sargent, T. P. Copps, P. A. Lievaart, and J. G. Szekely, J. Gen. Virol. 45:161-170, 1979) that intermediate subviral particles (ISVPs) of reovirus type 3 strain Abney (T3A) induced the release of 51Cr from preloaded L cells and showed that the intact virion and core forms did not. Reovirus type 1 strain Lang (T1L) ISVPs were found to be less efficient at 51Cr release than T3A ISVPs. Reassortants between these strains indicated that the 51Cr release phenotype segregates with the M2 gene segment. Biochemical studies indicated that the ISVPs' acquisition of the capacity to induce 51Cr release followed the cleavage of the viral M2 gene product mu 1/mu 1C to fragments delta and phi during virion conversion to ISVP but did not directly correlate with this cleavage. These studies suggest that the reovirus M2 gene product (in its cleaved form) plays a role in interacting with cell membranes.     

BOOK REVIEWS

Book reviewed in this article:
Gardiner, C. H., Fayer, R. & Dubey, J. P. 1988. An Atlas of Protozoan Parasites and Animal Tissues .
Bryant, C. & Behm, C. 1990. Biochemical Adaptation in Parasites .
Dubey, J. P. & Beattie, C. P. 1988. Toxoplasmosis of Animals and Man .
Margulis, L., Corliss, J. O., Melkonian, M. & Chapmann, D. J. (ed.) (with 60 contributors). 1990. Handbook of Protoctistia .
Esch, G., Bush, A. & Aho, J. (ed.) 1990. Parasite Communities: Patterns and Processes .     

Structure and function of a family 10 beta-xylanase chimera of Streptomyces olivaceoviridis E-86 FXYN and Cellulomonas fimi Cex

The catalytic domain of xylanases belonging to glycoside hydrolase family 10 (GH10) can be divided into 22 modules (M1 to M22; Sato, Y., Niimura, Y., Yura, K., and Go, M. (1999) Gene (Amst.) 238, 93-101). Inspection of the crystal structure of a GH10 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A) revealed that the catalytic domain of GH10 xylanases can be dissected into two parts, an N-terminal larger region and C-terminal smaller region, by the substrate binding cleft, corresponding to the module border between M14 and M15. It has been suggested that the topology of the substrate binding clefts of GH10 xylanases are not conserved (Charnock, S. J., Spurway, T. D., Xie, H., Beylot, M. H., Virden, R., Warren, R. A. J., Hazlewood, G. P., and Gilbert, H. J. (1998) J. Biol. Chem. 273, 32187-32199). To facilitate a greater understanding of the structure-function relationship of the substrate binding cleft of GH10 xylanases, a chimeric xylanase between SoXyn10A and Xyn10A from Cellulomonas fimi (CfXyn10A) was constructed, and the topology of the hybrid substrate binding cleft established. At the three-dimensional level, SoXyn10A and CfXyn10A appear to possess 5 subsites, with the amino acid residues comprising subsites -3 to +1 being well conserved, although the +2 subsites are quite different. Biochemical analyses of the chimeric enzyme along with SoXyn10A and CfXyn10A indicated that differences in the structure of subsite +2 influence bond cleavage frequencies and the catalytic efficiency of xylooligosaccharide hydrolysis. The hybrid enzyme constructed in this study displays fascinating biochemistry, with an interesting combination of properties from the parent enzymes, resulting in a low production of xylose.     

REVIEWS

Book Reviewed in this article:
Pigments in Plants . Ed. by F. C zygan .
Nitrogen and Carbon Metabolism . Ed. by J. D erek B ewley .
Advances in Biochemical Engineering . Vol. 18, Plant Cell Cultures II . Managing Editor: A. F iechter .
The Botany of Auckland . By L ucy M. C ranwell .
Photosynthesis . By D. O. H all and K. K. R ao .
Plants and Mineral Salts . By J. F. S utcliffe and D. A. B aker .
The Archives of the Peat Bogs . By S ir H arry G odwin .
The Biology of Mosses . By D. H. S. R ichardson .     

Molecular cloning of putative members of the Na/H exchanger gene family. cDNA cloning, deduced amino acid sequence, and mRNA tissue expression of the rat Na/H exchanger NHE-1 and two structurally related proteins.

Biochemical and pharmacological data support the existence of multiple forms of the Na/H exchanger (NHE). Two isoforms, termed NHE-1 and NHE-2, have recently been isolated from rabbit ileal villus epithelial cells (Tse, C. M., Ma, A. I., Yang, V. W., Watson, A. J. M., Levine, S., Montrose, M. H., Potter, J., Sardet, C., Pouysségur, J., and Donowitz, M. (1991) EMBO J. 10, 1957-1967; Tse, C. M., Watson, A. J. M., Ma, A. I., Pouysségur, J., and Donowitz, M. (1991) Gastroenterology 100, A258). To identify additional molecular forms of the exchanger, rat brain, heart, kidney, stomach, and spleen cDNA libraries were screened for their presence using an NHE-1 cDNA probe under low stringency hybridization conditions. cDNAs encoding rat NHE-1 and two structurally related proteins, designated NHE-3 and NHE-4, have been isolated. Based on the deduced amino acid sequences, NHE-1, -3, and -4 are similar in size, having relative molecular masses of 91,506, 92,997, and 81,427, respectively. Overall, the proteins exhibit approximately 40% amino acid identity to each other and have similar hydropathy profiles, suggesting that they have the same transmembrane organization. The predicted N-terminal transmembrane regions of the three proteins, which span between 453 and 503 amino acids, exhibit the highest degree of identity (45-49%). In contrast, the C-terminal cytoplasmic regions, which span between 247 and 378 amino acids, exhibit very low amino acid identity (24-31%). Tissue distribution studies reveal that the NHE-1 mRNA is present at varying levels in all tissues examined, whereas NHE-3 and NHE-4 mRNAs exhibit a more limited distribution. NHE-3 mRNA is expressed at high levels in colon and small intestine, with significant levels also present in kidney and stomach. NHE-4 mRNA is most abundant in stomach, followed by intermediate levels in small intestine and colon and lesser amounts in kidney, brain, uterus, and skeletal muscle. These data suggest that the molecular basis for the functional diversity of the Na/H exchanger in mammals is based, at least in part, on expression of multiple members of a gene family.     

Transgenic analysis of a hybrid poplar wound-inducible promoter reveals developmental patterns of expression similar to that of storage protein genes.

The wound-inducible win3 multigene family from hybrid poplars (Populus trichocarpa x Populus deltoides) encodes proteins with structural similarities with Kunitz-type protease inhibitors (H.D. Bradshaw Jr., J.B. Hollick, T.J. Parsons, H.R.G. Clarke, M.P. Gordon [1990] Plant Mol Biol 14: 51-59), and at least one member, win3.12, is transcribed de novo in the injured and uninjured leaves of wounded trees (J.B. Hollick, M.P. Gordon [1993] Plant Mol Biol 22: 561-572). A previous study demonstrated that 1352 bp of 5' flanking DNA from the win3.12 gene confers local wound-regulated expression of the beta-glucuronidase gene in transgenic tobacco (Nicotiana tabacum cv Xanthi n.c.) (J.B. Hollick, M.P. Gordon [1993] Plant Mol Biol 22: 561-572). We extend this transgenic analysis here by examining the developmental regulation and systemic wound induction conferred by the same transgene construct in tobacco. Biochemical and histochemical surveys of beta-glucuronidase activity are described for four, independent transgenic lines. The observed spatial and temporal expression patterns coincide with dormant storage tissues and with previously described expression patterns for both seed and vegetative storage protein genes. Developmental northern blot analysis of win3 RNA levels in poplar seeds confirms that proper temporal expression of the reporter gene is maintained during tobacco seed maturation. These results demonstrate that a putative Kunitz-type protease inhibitor can be wound inducible in addition to being expressed in developing seeds.     

Reviews

Book reviewed in this article:
Die Orchideen. By R udolf S chlechter . Ed. by F. G. B rieger , R. M aatsch and K. S enghas .
A Gardener's Dictionary of Plant Names . By A. W. S mith . Revised and enlarged by W illiam T. S tearn and I. L. L. S mith .
Plant Geography of the Pacific. By M. M. J. van B algooy .
Einführung in die Pflanzensoziologie. By R. K napp .
Taxonomy of Fungi Imperfecti (Proceedings of the First International Specialists' Workshop Conference on Criteria and Terminology in the Classification of Fungi Imperfecti, Kananaskis, Alberta, Canada). Ed. by B ryce K endrick .
Introduction to Plant Biochemistry. By T. W. G oodwin and E. I. M ercer .
Symposium on the Biochemical and Ecological Aspects of Plant-Parasite Relations. Ed. by Z. K iráaly and L. S zalay -M arzsó .
IVth Meeting of the International Council for the Study of Viruses and Virus Diseases of Grapevine, Colmar.
Some Common Flowering Plants of Uganda. By E. M. L ind and A. C. T allantire .     

Book review

Chronopharmacology. Cellular and Biochemical Interactions (Cellular Clocks Series/3), by Prof. Dr. Björn Lemmer, Center of Pharmacology, J.W. Goethe‐University, Frankfurt am Main, FRG. 1989. 744 pp., $150.00 (US and Canada), $180.00 (All other countries). ISBN 0–8247–8103–1 Published by Marcel Dekker, Inc. New York, USA.

Chronobiology and chronomedicine. Basic research and applications. Proceedings of the IVth Annual Meeting of the European Society for Chronobiology, Birmingham, July 1988, by E. Morgan. 1990, 407 pp., soft cover sFr. 79.‐ISBN 3–631–42301–2 Published by Verlag Peter Lang, Frankfurt a.M., Bern, New York, Paris.

Biological rhythms in clinical practice by J. Ahrendt, J.M. Waterhouse and D.S. Minors 1989. 299 pp.m, hard cover £ 48.‐ISBN 0–7236–0961–6     

Reviews

Book Reviwed in this article:
The Biochemical Functions of Terpenoids in Plants. Ed. by T. W. G oodwin .
Phytopathologie und Pflanzenschutz. By G erd F rohlich .
Morphology of Seed-plants. By M. G uédès .
Biological Clocks. By J ohn B rady .
Climate and Evolution. By R.G.P earson .
The Identification of Flowering Plant Families Including a Key to Those Native and Cultivated in North Temperate Regions. By P. H. D avis and J. C ullen     

The box VII motif of Escherichia coli DnaA protein is required for DnaA oligomerization at the E. coli replication origin

Escherichia coli DnaA protein initiates DNA replication from the chromosomal origin, oriC, and regulates the frequency of this process. Structure-function studies indicate that the replication initiator comprises four domains. Based on the structural similarity of Aquifex aeolicus DnaA to other AAA+ proteins that are oligomeric, it was proposed that Domain III functions in oligomerization at oriC (Erzberger, J. P., Pirruccello, M. M., and Berger, J. M. (2002) EMBO J. 21, 4763-4773). Because the Box VII motif within Domain III is conserved among DnaA homologues and may function in oligomerization, we substituted conserved Box VII amino acids of E. coli DnaA with alanine by site-directed mutagenesis to examine the role of this motif. All mutant proteins are inactive in initiation from oriC in vivo and in vitro, but they support RK2 plasmid DNA replication in vivo. Thus, RK2 requires only a subset of DnaA functions for plasmid DNA replication. Biochemical studies on a mutant DnaA carrying an alanine substitution at arginine 281 (R281A) in Box VII show that it is inactive in in vitro replication of an oriC plasmid, but this defect is not from the failure to bind to ATP, DnaB in the DnaB-DnaC complex, or oriC. Because the mutant DnaA is also active in the strand opening of oriC, whereas DnaB fails to bind to this unwound region, the open structure is insufficient by itself to load DnaB helicase. Our results show that the mutant fails to form a stable oligomeric DnaA-oriC complex, which is required for the loading of DnaB.     

Book review

Clinical and Biochemical Luminescence (1982). Edited by L.J. Kricka & T.J.N. Carter. 289 pp. New York & Basel: Marcel Dekker, Inc. S.Fr. 135.
Microbial and Viral Pesticides (1982). Edited by E. Kurstak. 720 pp. New York & Basel: Marcel Dekker, Inc. S.Fr. 284.
The Control of Antibiotic-Resistant Bacteria (1982). Edited by Sir Charles H. Stuart-Harris & D.M. Harris. 284 pp. London & New York: Academic Press. £20.00, US$37.00.
Economic Microbiology Vol. 7. Fermented Foods (1983). Edited by A.H. Rose. 337 pp. London & New York: Academic Press. £29.20, $60.00.
Current Developments in Malting, Brewing and Distilling (1983). Edited by F.G. Priest & I. Campbell. 311 pp. London: The Institute of Brewing, 33 Clarges St, London W1Y 8EE. Price not stated.     

Cloning, overexpression, and characterization of a novel thermostable penicillin G acylase from Achromobacter xylosoxidans: probing the molecular basis for its high thermostability

The gene encoding a novel penicillin G acylase (PGA), designated pgaW, was cloned from Achromobacter xylosoxidans and overexpressed in Escherichia coli. The pgaW gene contains an open reading frame of 2586 nucleotides. The deduced protein sequence encoded by pgaW has about 50% amino acid identity to several well-characterized PGAs, including those of Providencia rettgeri, Kluyvera cryocrescens, and Escherichia coli. Biochemical studies showed that the optimal temperature for this novel PGA (PGA650) activity is greater than 60 degrees C and its half-life of inactivation at 55 degrees C is four times longer than that of another previously reported thermostable PGA from Alcaligenes faecalis (R. M. D. Verhaert, A. M. Riemens, J. V. R. Laan, J. V. Duin, and W. J. Quax, Appl. Environ. Microbiol. 63:3412-3418, 1997). To our knowledge, this is the most thermostable PGA ever characterized. To explore the molecular basis of the higher thermostability of PGA650, homology structural modeling and amino acid composition analyses were performed. The results suggested that the increased number of buried ion pair networks, lower N and Q contents, excessive arginine residues, and remarkably high content of proline residues in the structure of PGA650 could contribute to its high thermostability. The unique characteristic of higher thermostability of this novel PGA provides some advantages for its potential application in industry.     

A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding

Formation of non-clathrin-coated vesicles requires the recruitment of several cytosolic factors to the Golgi membrane. To identify membrane proteins involved in this budding process, a highly abundant type I transmembrane protein (p23) was isolated from mammalian Golgi-derived COPI-coated vesicles, and its cDNA was cloned and sequenced. It belongs to the p24 family of proteins involved in the budding of transport vesicles (Stamnes, M.A., M.W. Craighead, M.H. Hoe, N. Lampen, S. Geromanos, P. Tempst, and J.E. Rothman. 1995. Proc. Natl. Acad. Sci. USA. 92:8011-8015). p23 consists of a large NH2-terminal luminal domain and a short COOH-terminal cytoplasmic tail (-LRRFFKAKKLIE-CO2-) that shows similarity, but not identity, with the sequence motif-KKXX-CO2-, known as a signal for retrieval of escaped ER-resident membrane proteins (Jackson, M.R., T. Nilsson, and P.A. Peterson. 1990. EMBO (Eur. Mol. Biol. Organ.) J. 9:3153-3162; Nilsson, T., M. Jackson, and P.A. Peterson. 1989. Cell. 58:707-718). The cytoplasmic tail of p23 binds to coatomer with similar efficiency as known KKXX motifs. However, the p23 tail differs from the KKXX motif in having an additional motif needed for binding of coatomer. p23 is localized to Golgi cisternae and, during vesicle formation, it concentrates into COPI-coated buds and vesicles. Biochemical analysis revealed that p23 is enriched in vesicles by a factor of approximately 20, as compared with the donor Golgi fraction, and is present in amounts stoichiometric to the small GTP-binding protein ADP-ribosylation factor (ARF) and coatomer. From these data we conclude that p23 represents a Golgi- specific receptor for coatomer involved in the formation of COPI-coated vesicles.