Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli

Pamela G. Jones, Masanori Mitta, Youngho Kim, Weining Jiang, Masayori Inouye

Research output: Contribution to journalArticlepeer-review

266 Scopus citations

Abstract

A 70-kDa protein was specifically induced in Escherichia coli when the culture temperature was shifted from 37 to 15°C. The protein was identified to be the product of the deaD gene (reassigned csdA) encoding a DEAD-box protein. Furthermore, after the shift from 37 to 15°C, CsdA was exclusively localized in the ribosomal fraction and became a major ribosomal-associated protein in cells grown at 15°C. The csdA deletion significantly impaired cell growth and the synthesis of a number of proteins, specifically the derepression of heat-shock proteins, at low temperature. Purified CsdA was found to unwind double-stranded RNA in the absence of ATP. Therefore, the requirement for CsdA in derepression of heat-shock protein synthesis is a cold shock-induced function possibly mediated by destabilization of secondary structures previously identified in the rpoH mRNA.

Original languageEnglish (US)
Pages (from-to)76-80
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume93
Issue number1
DOIs
StatePublished - Jan 9 1996

ASJC Scopus subject areas

  • General

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