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"Zn-link": a metal-sharing interface that organizes the quaternary structure and catalytic site of the endoribonuclease, RNase E.

Abstract:

Ribonuclease E is an essential hydrolytic endonuclease in Escherichia coli, and it plays a central role in maintaining the balance and composition of the messenger RNA population. The enzyme is also required for rRNA and tRNA processing. We have shown earlier that the highly conserved catalytic domain of E. coli RNase E is a homotetramer [Callaghan, A. J. et al. (2003) Biochemistry 42, 13848-13855]. Here, we report that this quaternary organization requires zinc. Two protomers share a single ...

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Publication status:
Published

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Publisher copy:
10.1021/bi0478244

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Journal:
Biochemistry More from this journal
Volume:
44
Issue:
12
Pages:
4667-4675
Publication date:
2005-03-01
DOI:
EISSN:
1520-4995
ISSN:
0006-2960

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