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PMID: 17437059 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Structure and function of bacterial cold shock proteins.

Cellular and molecular life sciences : CMLS ·Vol. 64 ·No. 12 ·2007-06-00 ·Pages 1457-70

Horn G, Hofweber R, Kremer W, Kalbitzer HR

Abstract

Cold shock proteins (Csps) comprise a family of small proteins that are structurally highly conserved and bind to single-stranded nucleic acids via their nucleic acid binding motifs RNP1 and RNP2. Bacterial Csps are mainly induced after a rapid temperature downshift to regulate the adaptation to cold stress, but are also present under normal conditions to regulate other biological functions. The structural unit characteristic for Csps occurs also as a cold shock domain (CSD) in other proteins and can be found in wide variety of organisms from bacteria to vertebrates. Important examples are the Y-box proteins that are known to be involved in regulation of several transcription and translation processes. This review describes the role of Csps in protein expression during cold shock with special emphasis on structural aspects of Csps.

MeSH Terms
Amino Acid Motifs Bacterial Proteins/chemistry,metabolism Cold Temperature DNA/metabolism Protein Biosynthesis Protein Conformation
Chemicals
Bacterial Proteins DNA
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Horn G
Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Universitätsstrasse 31, Regensburg, Germany.
Hofweber R
Kremer W
Kalbitzer H R
Article Info
Journal
Cellular and molecular life sciences : CMLS
Abbr.
Cell Mol Life Sci
ISSN
1420-682X
Published
2007-06-00
Pages
1457-70
Language
English
Region
Switzerland
NLM ID
9705402
Subset
IM
Corrections
ErratumIn
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