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Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain.

Abstract:

RNase E is an essential endoribonuclease that plays a central role in the processing and degradation of RNA in Escherichia coli and other bacteria. Most endoribonucleases have been shown to act distributively; however, Feng et al. [(2002) Proc. Natl. Acad. Sci. U.S.A. 99, 14746-14751] have recently found that RNase E acts via a scanning mechanism. A structural explanation for the processivity of RNase E is provided here, with our finding that the conserved catalytic domain of E. coli RNase E ...

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Publication status:
Published

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Publisher copy:
10.1021/bi0351099

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Journal:
Biochemistry
Volume:
42
Issue:
47
Pages:
13848-13855
Publication date:
2003-12-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:747738fb-fe5c-4a5d-a2af-aa0733f9259a
Source identifiers:
59252
Local pid:
pubs:59252

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