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  Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E.

Callaghan, A. J., Aurikko, J. P., Illag, L. L., Grossmann, G., Chandran, V., Kühnel, K., et al. (2004). Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. Journal of Molecular Biology, 340(5), 965-979. doi:10.1016/j.jmb.2004.05.046.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-8B5A-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-3AA2-D
Genre: Journal Article

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 Creators:
Callaghan, A. J., Author
Aurikko, J. P., Author
Illag, L. L., Author
Grossmann, G., Author
Chandran, V., Author
Kühnel, K.1, Author              
Poljak, L., Author
Carpousis, A. J., Author
Robinson, C. V., Author
Symmons, M. F., Author
Luisi, B. F., Author
Affiliations:
1Research Group of Autophagy, MPI for Biophysical Chemistry, Max Planck Society, ou_1933285              

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Free keywords: RNA degradosome; protein–protein interactions; intrinsically unstructured proteins; RNA processing; ribonuclease E
 Abstract: 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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Language(s): eng - English
 Dates: 2004-07-23
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.jmb.2004.05.046
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Title: Journal of Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 340 (5) Sequence Number: - Start / End Page: 965 - 979 Identifier: -