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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Callaghan AJ,Aurikko JP,Ilag LL,Günter Grossmann J,Chandran V,Kühnel K,Poljak L,Carpousis AJ,Robinson CV,Symmons MF,Luisi BFdoi
10.1016/j.jmb.2004.05.046keywords:
subject
Has Abstractpub_date
2004-07-23 00:00:00pages
965-79issue
5eissn
0022-2836issn
1089-8638pii
S0022283604006163journal_volume
340pub_type
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