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  • 1
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    Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-10-28
    Description: Thiamine pyrophosphate 1 is an essential cofactor in all living systems. Its biosynthesis involves the separate syntheses of the pyrimidine 2 and thiazole 3 precursors, which are then coupled. Two biosynthetic routes to the thiamine thiazole have been identified. In prokaryotes, five enzymes act on three substrates to produce the thiazole via a complex oxidative condensation reaction, the mechanistic details of which are now well established. In contrast, only one gene product is involved in thiazole biosynthesis in eukaryotes (THI4p in Saccharomyces cerevisiae). Here we report the preparation of fully active recombinant wild-type THI4p, the identification of an iron-dependent sulphide transfer reaction from a conserved cysteine residue of the protein to a reaction intermediate and the demonstration that THI4p is a suicide enzyme undergoing only a single turnover.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3205460/" 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/PMC3205460/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chatterjee, Abhishek -- Abeydeera, N Dinuka -- Bale, Shridhar -- Pai, Pei-Jing -- Dorrestein, Pieter C -- Russell, David H -- Ealick, Steven E -- Begley, Tadhg P -- DK44083/DK/NIDDK NIH HHS/ -- DK67081/DK/NIDDK NIH HHS/ -- R01 DK067081/DK/NIDDK NIH HHS/ -- R37 DK044083/DK/NIDDK NIH HHS/ -- R37 DK044083-21/DK/NIDDK NIH HHS/ -- England -- Nature. 2011 Oct 26;478(7370):542-6. doi: 10.1038/nature10503.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22031445" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Biocatalysis ; Carbon-Nitrogen Lyases/chemistry/*metabolism ; Conserved Sequence ; Cysteine/metabolism ; Iron/metabolism ; Molecular Sequence Data ; Recombinant Proteins ; Saccharomyces cerevisiae/*enzymology ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Sulfides/metabolism ; Sulfur/metabolism ; Thiamine/*metabolism ; Thiamine Pyrophosphate/metabolism ; Thiazoles/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Type VI secretion delivers bacteriolytic effectors to target cells (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-07-22
    Description: Peptidoglycan is the major structural constituent of the bacterial cell wall, forming a meshwork outside the cytoplasmic membrane that maintains cell shape and prevents lysis. In Gram-negative bacteria, peptidoglycan is located in the periplasm, where it is protected from exogenous lytic enzymes by the outer membrane. Here we show that the type VI secretion system of Pseudomonas aeruginosa breaches this barrier to deliver two effector proteins, Tse1 and Tse3, to the periplasm of recipient cells. In this compartment, the effectors hydrolyse peptidoglycan, thereby providing a fitness advantage for P. aeruginosa cells in competition with other bacteria. To protect itself from lysis by Tse1 and Tse3, P. aeruginosa uses specific periplasmically localized immunity proteins. The requirement for these immunity proteins depends on intercellular self-intoxication through an active type VI secretion system, indicating a mechanism for export whereby effectors do not access donor cell periplasm in transit.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3146020/" 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/PMC3146020/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, Alistair B -- Hood, Rachel D -- Bui, Nhat Khai -- LeRoux, Michele -- Vollmer, Waldemar -- Mougous, Joseph D -- R01 AI080609/AI/NIAID NIH HHS/ -- R01 AI080609-03/AI/NIAID NIH HHS/ -- England -- Nature. 2011 Jul 20;475(7356):343-7. doi: 10.1038/nature10244.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Washington, Seattle, Washington 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21776080" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/chemistry/genetics/metabolism ; Amino Acid Sequence ; Bacterial Proteins/antagonists & ; inhibitors/chemistry/genetics/*metabolism/secretion ; *Bacterial Secretion Systems ; Bacterial Toxins/antagonists & inhibitors/metabolism ; *Bacteriolysis ; Gram-Negative Bacteria/*cytology/*metabolism ; Hydrolysis ; *Microbial Interactions ; Muramidase/chemistry/genetics/metabolism ; Peptidoglycan/metabolism ; Periplasm/metabolism ; Pseudomonas aeruginosa/enzymology/genetics/growth & development/*metabolism ; Pseudomonas putida/growth & development/metabolism ; Substrate Specificity
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    TAF1B is a TFIIB-like component of the basal transcription machinery for RNA polymerase I (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-09-17
    Description: Transcription by eukaryotic RNA polymerases (Pols) II and III and archaeal Pol requires structurally related general transcription factors TFIIB, Brf1, and TFB, respectively, which are essential for polymerase recruitment and initiation events. A TFIIB-like protein was not evident in the Pol I basal transcription machinery. We report that TAF1B, a subunit of human Pol I basal transcription factor SL1, is structurally related to TFIIB/TFIIB-like proteins, through predicted amino-terminal zinc ribbon and cyclin-like fold domains. SL1, essential for Pol I recruitment to the ribosomal RNA gene promoter, also has an essential postpolymerase recruitment role, operating through TAF1B. Therefore, a TFIIB-related protein is implicated in preinitiation complex assembly and postpolymerase recruitment events in Pol I transcription, underscoring the parallels between eukaryotic Pol I, II, and III and archaeal transcription machineries.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3566551/" 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/PMC3566551/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Naidu, Srivatsava -- Friedrich, J Karsten -- Russell, Jackie -- Zomerdijk, Joost C B M -- 085441/Wellcome Trust/United Kingdom -- 085441/Z/08/Z/Wellcome Trust/United Kingdom -- Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2011 Sep 16;333(6049):1640-2. doi: 10.1126/science.1207656.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21921199" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; DNA, Ribosomal ; Humans ; Molecular Sequence Data ; Mutant Proteins/chemistry/metabolism ; Mutation ; Pol1 Transcription Initiation Complex Proteins/*chemistry/genetics/*metabolism ; Promoter Regions, Genetic ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; RNA Polymerase I/*metabolism ; Transcription Factor TFIIB/*chemistry/metabolism ; *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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