Chapter 4 The role of cold-shock proteins in low-temperature adaptation

Jeroen A. Wouters*, Frank M. Rombouts, Oscar P. Kuipers, Willem M. de Vos, T. Abee

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

5 Citations (Scopus)

Abstract

This chapter discusses the role of cold-shock proteins in low-temperature adaptation. Research on cold adaptation has mainly focused on the synthesis of so-called “cold-shock proteins” (CSPs), a specific response that is shared by nearly all bacteria. These small (7 kDa) proteins are involved in gene expression, mRNA folding, transcriptional initiation and regulation and/or freeze-protection. Using primarily electrophoresis techniques other (non-7 kDa) low-temperature induced proteins are also identified, which will be referred to as “cold-induced proteins” (CIPs). Such proteins are involved in a variety of cellular processes. The chapter discusses novel aspects concerning the structure, function, and control of CSPs and CIPs, including a model for bacterial cold adaptation and possible mechanisms for low-temperature sensing. The chapter discusses the way bacteria sense low-temperature signals. The putative cellular thermosensors that have been proposed correlate to the major biochemical changes upon low-temperature exposure in bacterial cells, such as DNA topology, ribosomal structure and membrane composition. The sensing of heat shock interlinks with a number of two-component regulatory systems within the bacterial cell.
Original languageEnglish
Title of host publicationProtein Adaptations and Signal Transduction
EditorsK.B. Storey, J.M. Storey
PublisherElsevier
Chapter4
Pages43-56
Number of pages14
Volume2
DOIs
Publication statusPublished - 2001

Publication series

NameCell and Molecular Response to Stress
Volume2
ISSN (Print)1568-1254

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