| ATP binding to the sigma 54-dependent activator XylR triggers a protein multimerization cycle catalyzed by UAS DNA. | |
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MedLine Citation:
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PMID: 8706137 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The events that take place at the prokaryotic enhancer of the Pu promoter of Pseudomonas putida prior to the engagement of the sigma 54-RNA polymerase (sigma 54-RNAP) have been studied in vitro. ATP hydrolysis by XylR, the cognate regulator of the system, is preceded by the multimerization of XylR at the enhancer, which is itself triggered by the sole allosteric effect of ATP binding to the protein. Since ADP is unable to support multimerization, ATP hydrolysis might be followed by a return to the nonmultimerized state. This notion is supported further by the properties of mutant proteins that seem to be frozen, in either the nonmultimerized or the multimerized state, respectively. These results support a cyclic mechanism of ATP-dependent association/dissociation of XylR at the promoter UAS that precedes any involvement of the polymerase in transcription initiation. |
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Authors:
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J Pérez-Martín; V de Lorenzo |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Cell Volume: 86 ISSN: 0092-8674 ISO Abbreviation: Cell Publication Date: 1996 Jul |
Date Detail:
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Created Date: 1996-09-06 Completed Date: 1996-09-06 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0413066 Medline TA: Cell Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 331-9 Citation Subset: IM |
Affiliation:
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Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphatases
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metabolism Adenosine Triphosphate / metabolism* Amino Acid Sequence Bacterial Proteins / chemistry, genetics Cell Cycle / genetics Cross-Linking Reagents DNA Footprinting DNA, Bacterial / physiology* DNA-Binding Proteins / chemistry, genetics* Enhancer Elements, Genetic / genetics Hydrolysis Molecular Sequence Data Mutation / physiology Protein Binding / genetics Protein Conformation Pseudomonas putida / chemistry*, cytology, genetics Transcription Factors / chemistry, genetics* Transcription, Genetic / physiology |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Cross-Linking Reagents; 0/DNA, Bacterial; 0/DNA-Binding Proteins; 0/Transcription Factors; 0/XylR protein, Pseudomonas; 56-65-5/Adenosine Triphosphate; EC 3.6.1.-/Adenosine Triphosphatases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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