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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2007-2-26
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pubmed:abstractText |
The Escherichia coli protein RhlB is an ATP-dependent motor that unfolds structured RNA for destruction by partner ribonucleases. In E. coli, and probably many other related gamma-proteobacteria, RhlB associates with the essential endoribonuclease RNase E as part of the multi-enzyme RNA degradosome assembly. The interaction with RNase E boosts RhlB's ATPase activity by an order of magnitude. Here, we examine the origins and implications of this effect. The location of the interaction sites on both RNase E and RhlB are refined and analysed using limited protease digestion, domain cross-linking and homology modelling. These data indicate that RhlB's carboxy-terminal RecA-like domain engages a segment of RNase E that is no greater than 64 residues. The interaction between RhlB and RNase E has two important consequences: first, the interaction itself stimulates the unwinding and ATPase activities of RhlB; second, RhlB gains proximity to two RNA-binding sites on RNase E, with which it cooperates to unwind RNA. Our homology model identifies a pattern of residues in RhlB that may be key for recognition of RNase E and which may communicate the activating effects. Our data also suggest that the association with RNase E may partially repress the RNA-binding activity of RhlB. This repression may in fact permit the interplay of the helicase and adjacent RNA binding segments as part of a process that steers substrates to either processing or destruction, depending on context, within the RNA degradosome assembly.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Polyribonucleotide...,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/RhlB protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/degradosome,
http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease E
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
367
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
113-32
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17234211-Adenosine Triphosphatases,
pubmed-meshheading:17234211-Adenosine Triphosphate,
pubmed-meshheading:17234211-DEAD-box RNA Helicases,
pubmed-meshheading:17234211-Endoribonucleases,
pubmed-meshheading:17234211-Escherichia coli,
pubmed-meshheading:17234211-Escherichia coli Proteins,
pubmed-meshheading:17234211-Multienzyme Complexes,
pubmed-meshheading:17234211-Nucleic Acid Denaturation,
pubmed-meshheading:17234211-Polyribonucleotide Nucleotidyltransferase,
pubmed-meshheading:17234211-RNA,
pubmed-meshheading:17234211-RNA Helicases
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pubmed:year |
2007
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pubmed:articleTitle |
Recognition and cooperation between the ATP-dependent RNA helicase RhlB and ribonuclease RNase E.
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pubmed:affiliation |
Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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