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  • American Association for the Advancement of Science (AAAS)  (2)
  • Blackwell Publishing Ltd  (2)
  • 2005-2009  (4)
  • 1975-1979
  • 1950-1954
  • 2005  (4)
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  • 2005-2009  (4)
  • 1975-1979
  • 1950-1954
Year
  • 1
    Electronic Resource
    Electronic Resource
    Branched-chain fatty acid biosynthesis in a branched-chain amino acid aminotransferase mutant of Staphylococcus carnosus (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 243 (2005), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Fatty acid biosynthesis by a mutant strain of Staphylococcus carnosus deficient in branched-chain amino acid aminotransferase (IlvE) activity was analysed. This mutant was unable to produce the appropriate branched-chain α-ketoacid precursors for branched-chain fatty acid biosynthesis from the amino acids valine, isoleucine, and leucine, and required the short branched chain acids 2-methylbutanoic acid or 2-methylpropanoic acid for growth in a defined medium. The isoleucine related metabolites, α-keto-β-methylvaleric acid and 2-methylbutanal also served as growth factors. Growth in rich medium and growth in defined medium supplemented with 2-methylpropanoic acid lead to extensive alteration of the fatty acid composition in the cell membrane. In rich medium, a change from 51.7% to 17.1%anteiso-C15:0, and from 3.6% to 33.9%iso-C14:0 fatty acids as compared to the wild-type strain was observed. Despite the deficiency in IlvE activity, the mutant strain was still able to produce the short chain carboxylic acids, 3-methylbutanoic acid and 2-methylpropanoic acid when cultivated in rich medium. Supplementation experiments employing deuterated glucose induced the valine biosynthetic pathway for 2-methylpropanoic acid production, revealing that the IlvE protein plays an important, but not essential role in the biosynthesis of branched-chain fatty acids and secondary metabolites in S. carnosus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2004.11.041
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of outer membrane protein fractions of Bdellovibrionales (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 243 (2005), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Bdellovibrio-and-like organisms (BALOs) are predatory bacteria that prey upon Gram-negative bacteria and are taxonomically subsumed in the order Bdellovibrionales. Despite their unique lifestyle, these bacteria show remarkable genotypic diversities. The outer membrane of the predators is likely to play an important role during the recognition and invasion stage, as well as in the intraperiplasmic growth phase. In this study, the outer membrane protein fractions of type strains of Bdellovibrio, Bacteriovorax and Peredibacter were investigated, revealing the presence of outer membrane proteins (Omps) similar to the major Omps of Bdellovibrio bacteriovorus. The primary structures of these Omps of Bdellovibrio sp. W, Bacteriovorax stolpii and Peredibacter starrii were elucidated by a combined mass spectrometric–reverse genetic approach. The similarity between the analyzed Omps of the investigated BALOs ranges from 32% to 89% showing conserved amino acid regions in their primary structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2004.12.006
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  • 3
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    The genome of the kinetoplastid parasite, Leishmania major (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-16
    Description: Leishmania species cause a spectrum of human diseases in tropical and subtropical regions of the world. We have sequenced the 36 chromosomes of the 32.8-megabase haploid genome of Leishmania major (Friedlin strain) and predict 911 RNA genes, 39 pseudogenes, and 8272 protein-coding genes, of which 36% can be ascribed a putative function. These include genes involved in host-pathogen interactions, such as proteolytic enzymes, and extensive machinery for synthesis of complex surface glycoconjugates. The organization of protein-coding genes into long, strand-specific, polycistronic clusters and lack of general transcription factors in the L. major, Trypanosoma brucei, and Trypanosoma cruzi (Tritryp) genomes suggest that the mechanisms regulating RNA polymerase II-directed transcription are distinct from those operating in other eukaryotes, although the trypanosomatids appear capable of chromatin remodeling. Abundant RNA-binding proteins are encoded in the Tritryp genomes, consistent with active posttranscriptional regulation of gene expression.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1470643/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1470643/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ivens, Alasdair C -- Peacock, Christopher S -- Worthey, Elizabeth A -- Murphy, Lee -- Aggarwal, Gautam -- Berriman, Matthew -- Sisk, Ellen -- Rajandream, Marie-Adele -- Adlem, Ellen -- Aert, Rita -- Anupama, Atashi -- Apostolou, Zina -- Attipoe, Philip -- Bason, Nathalie -- Bauser, Christopher -- Beck, Alfred -- Beverley, Stephen M -- Bianchettin, Gabriella -- Borzym, Katja -- Bothe, Gordana -- Bruschi, Carlo V -- Collins, Matt -- Cadag, Eithon -- Ciarloni, Laura -- Clayton, Christine -- Coulson, Richard M R -- Cronin, Ann -- Cruz, Angela K -- Davies, Robert M -- De Gaudenzi, Javier -- Dobson, Deborah E -- Duesterhoeft, Andreas -- Fazelina, Gholam -- Fosker, Nigel -- Frasch, Alberto Carlos -- Fraser, Audrey -- Fuchs, Monika -- Gabel, Claudia -- Goble, Arlette -- Goffeau, Andre -- Harris, David -- Hertz-Fowler, Christiane -- Hilbert, Helmut -- Horn, David -- Huang, Yiting -- Klages, Sven -- Knights, Andrew -- Kube, Michael -- Larke, Natasha -- Litvin, Lyudmila -- Lord, Angela -- Louie, Tin -- Marra, Marco -- Masuy, David -- Matthews, Keith -- Michaeli, Shulamit -- Mottram, Jeremy C -- Muller-Auer, Silke -- Munden, Heather -- Nelson, Siri -- Norbertczak, Halina -- Oliver, Karen -- O'neil, Susan -- Pentony, Martin -- Pohl, Thomas M -- Price, Claire -- Purnelle, Benedicte -- Quail, Michael A -- Rabbinowitsch, Ester -- Reinhardt, Richard -- Rieger, Michael -- Rinta, Joel -- Robben, Johan -- Robertson, Laura -- Ruiz, Jeronimo C -- Rutter, Simon -- Saunders, David -- Schafer, Melanie -- Schein, Jacquie -- Schwartz, David C -- Seeger, Kathy -- Seyler, Amber -- Sharp, Sarah -- Shin, Heesun -- Sivam, Dhileep -- Squares, Rob -- Squares, Steve -- Tosato, Valentina -- Vogt, Christy -- Volckaert, Guido -- Wambutt, Rolf -- Warren, Tim -- Wedler, Holger -- Woodward, John -- Zhou, Shiguo -- Zimmermann, Wolfgang -- Smith, Deborah F -- Blackwell, Jenefer M -- Stuart, Kenneth D -- Barrell, Bart -- Myler, Peter J -- R01 AI040599/AI/NIAID NIH HHS/ -- R01 AI053667/AI/NIAID NIH HHS/ -- U01 AI040599/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):436-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridgeshire CB10 1SA, UK. alicat@sanger.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020728" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatin/genetics/metabolism ; Gene Expression Regulation ; Genes, Protozoan ; Genes, rRNA ; *Genome, Protozoan ; Glycoconjugates/biosynthesis/metabolism ; Leishmania major/chemistry/*genetics/metabolism ; Leishmaniasis, Cutaneous/parasitology ; Lipid Metabolism ; Membrane Proteins/biosynthesis/chemistry/genetics/metabolism ; Molecular Sequence Data ; Multigene Family ; Protein Biosynthesis ; Protein Processing, Post-Translational ; Protozoan Proteins/biosynthesis/chemistry/genetics/metabolism ; RNA Processing, Post-Transcriptional ; RNA Splicing ; RNA, Protozoan/genetics/metabolism ; *Sequence Analysis, DNA ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    The great Sumatra-Andaman earthquake of 26 December 2004 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-21
    Description: The two largest earthquakes of the past 40 years ruptured a 1600-kilometer-long portion of the fault boundary between the Indo-Australian and southeastern Eurasian plates on 26 December 2004 [seismic moment magnitude (Mw) = 9.1 to 9.3] and 28 March 2005 (Mw = 8.6). The first event generated a tsunami that caused more than 283,000 deaths. Fault slip of up to 15 meters occurred near Banda Aceh, Sumatra, but to the north, along the Nicobar and Andaman Islands, rapid slip was much smaller. Tsunami and geodetic observations indicate that additional slow slip occurred in the north over a time scale of 50 minutes or longer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lay, Thorne -- Kanamori, Hiroo -- Ammon, Charles J -- Nettles, Meredith -- Ward, Steven N -- Aster, Richard C -- Beck, Susan L -- Bilek, Susan L -- Brudzinski, Michael R -- Butler, Rhett -- DeShon, Heather R -- Ekstrom, Goran -- Satake, Kenji -- Sipkin, Stuart -- New York, N.Y. -- Science. 2005 May 20;308(5725):1127-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Earth Sciences Department, University of California, Santa Cruz, CA 95064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905392" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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