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Molecular recognition of RhlB and RNase D in the Caulobacter crescentus RNA degradosome.

Abstract：

:The endoribonuclease RNase E is a key enzyme in RNA metabolism for many bacterial species. In Escherichia coli, RNase E contributes to the majority of RNA turnover and processing events, and the enzyme has been extensively characterized as the central component of the RNA degradosome assembly. A similar RNA degradosome assembly has been described in the α-proteobacterium Caulobacter crescentus, with the interacting partners of RNase E identified as the Kreb's cycle enzyme aconitase, a DEAD-box RNA helicase RhlB and the exoribonuclease polynucleotide phosphorylase. Here we report that an additional degradosome component is the essential exoribonuclease RNase D, and its recognition site within RNase E is identified. We show that, unlike its E. coli counterpart, C. crescentus RhlB interacts directly with a segment of the N-terminal catalytic domain of RNase E. The crystal structure of a portion of C. crescentus RNase E encompassing the helicase-binding region is reported. This structure reveals that an inserted segment in the S1 domain adopts an α-helical conformation, despite being predicted to be natively unstructured. We discuss the implications of these findings for the organization and mechanisms of the RNA degradosome.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Voss JE,Luisi BF,Hardwick SW

doi

10.1093/nar/gku1134

subject

Has Abstract

pub_date

2014-12-01 00:00:00

pages

13294-305

issue

21

eissn

0305-1048

issn

1362-4962

pii

gku1134

journal_volume

42

pub_type

杂志文章

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