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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2004-7-6
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pubmed:abstractText |
The hydrolytic endoribonuclease RNase E, which is widely distributed in bacteria and plants, plays key roles in mRNA degradation and RNA processing in Escherichia coli. The enzymatic activity of RNase E is contained within the conserved amino-terminal half of the 118 kDa protein, and the carboxy-terminal half organizes the RNA degradosome, a multi-enzyme complex that degrades mRNA co-operatively and processes ribosomal and other RNA. The study described herein demonstrates that the carboxy-terminal domain of RNase E has little structure under native conditions and is unlikely to be extensively folded within the degradosome. However, three isolated segments of 10-40 residues, and a larger fourth segment of 80 residues, are predicted to be regions of increased structural propensity. The larger of these segments appears to be a protein-RNA interaction site while the other segments possibly correspond to sites of self-recognition and interaction with the other degradosome proteins. The carboxy-terminal domain of RNase E may thus act as a flexible tether of the degradosome components. The implications of these and other observations for the organization of the RNA degradosome are discussed.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-2836
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pubmed:author |
pubmed-author:AurikkoJukka PJP,
pubmed-author:CallaghanAnastasia JAJ,
pubmed-author:CarpousisAgamennon JAJ,
pubmed-author:ChandranVidyaV,
pubmed-author:Günter GrossmannJJ,
pubmed-author:IlagLeopold LLL,
pubmed-author:KühnelKarinK,
pubmed-author:LuisiBen FBF,
pubmed-author:PoljakLeonoraL,
pubmed-author:RobinsonCarol VCV,
pubmed-author:SymmonsMartyn FMF
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
340
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
965-79
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15236960-Amino Acid Sequence,
pubmed-meshheading:15236960-Binding Sites,
pubmed-meshheading:15236960-Circular Dichroism,
pubmed-meshheading:15236960-Endoribonucleases,
pubmed-meshheading:15236960-Escherichia coli,
pubmed-meshheading:15236960-Molecular Sequence Data,
pubmed-meshheading:15236960-Multienzyme Complexes,
pubmed-meshheading:15236960-Phosphopyruvate Hydratase,
pubmed-meshheading:15236960-Polyribonucleotide Nucleotidyltransferase,
pubmed-meshheading:15236960-Protein Binding,
pubmed-meshheading:15236960-Protein Structure, Tertiary,
pubmed-meshheading:15236960-RNA, Bacterial,
pubmed-meshheading:15236960-RNA Helicases,
pubmed-meshheading:15236960-RNA-Binding Proteins,
pubmed-meshheading:15236960-Spectrometry, Mass, Electrospray Ionization,
pubmed-meshheading:15236960-Spectrometry, Mass, Matrix-Assisted Laser...
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pubmed:year |
2004
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pubmed:articleTitle |
Studies of the RNA degradosome-organizing domain of the Escherichia coli 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, Non-U.S. Gov't
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