| RNase Y in Bacillus subtilis: a Natively disordered protein that is the functional equivalent of RNase E from Escherichia coli. | |
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MedLine Citation:
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PMID: 21803996 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The control of mRNA stability is an important component of regulation in bacteria. Processing and degradation of mRNAs are initiated by an endonucleolytic attack, and the cleavage products are processively degraded by exoribonucleases. In many bacteria, these RNases, as well as RNA helicases and other proteins, are organized in a protein complex called the RNA degradosome. In Escherichia coli, the RNA degradosome is assembled around the essential endoribonuclease E. In Bacillus subtilis, the recently discovered essential endoribonuclease RNase Y is involved in the initiation of RNA degradation. Moreover, RNase Y interacts with other RNases, the RNA helicase CshA, and the glycolytic enzymes enolase and phosphofructokinase in a degradosome-like complex. In this work, we have studied the domain organization of RNase Y and the contribution of the domains to protein-protein interactions. We provide evidence for the physical interaction between RNase Y and the degradosome partners in vivo. We present experimental and bioinformatic data which indicate that the RNase Y contains significant regions of intrinsic disorder and discuss the possible functional implications of this finding. The localization of RNase Y in the membrane is essential both for the viability of B. subtilis and for all interactions that involve RNase Y. The results presented in this study provide novel evidence for the idea that RNase Y is the functional equivalent of RNase E, even though the two enzymes do not share any sequence similarity. |
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Authors:
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Martin Lehnik-Habrink; Joseph Newman; Fabian M Rothe; Alexandra S Solovyova; Cecilia Rodrigues; Christina Herzberg; Fabian M Commichau; Richard J Lewis; Jörg Stülke |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2011-07-29 |
Journal Detail:
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Title: Journal of bacteriology Volume: 193 ISSN: 1098-5530 ISO Abbreviation: J. Bacteriol. Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-09-14 Completed Date: 2011-11-14 Revised Date: 2013-05-23 |
Medline Journal Info:
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Nlm Unique ID: 2985120R Medline TA: J Bacteriol Country: United States |
Other Details:
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Languages: eng Pagination: 5431-41 Citation Subset: IM |
Affiliation:
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Department of General Microbiology, Institute of Microbiology and Genetics, Georg-August University Göttingen, Grisebachstr. 8, D-37077 Göttingen, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Bacillus subtilis / enzymology* Bacterial Proteins / chemistry*, genetics, metabolism* Computational Biology Endoribonucleases / chemistry*, genetics, metabolism* Escherichia coli / enzymology Molecular Sequence Data Multienzyme Complexes / metabolism Polyribonucleotide Nucleotidyltransferase / metabolism Protein Binding / genetics Protein Structure, Tertiary RNA Helicases / metabolism Sequence Homology, Amino Acid Two-Hybrid System Techniques |
| Grant Support | |
ID/Acronym/Agency:
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//Biotechnology and Biological Sciences Research Council |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Multienzyme Complexes; 0/degradosome; EC 2.7.7.-/RNA Helicases; EC 2.7.7.8/Polyribonucleotide Nucleotidyltransferase; EC 3.1.-/Endoribonucleases; EC 3.1.4.-/ribonuclease E |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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