Horn, G. and Hofweber, R. and Kremer, W. and Kalbitzer, H. R. (2007) Structure and function of bacterial cold shock proteins. CELLULAR AND MOLECULAR LIFE SCIENCES, 64 (12). pp. 1457-1470. ISSN 1420-682X, 1420-9071
Full text not available from this repository. (Request a copy)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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SINGLE-STRANDED-DNA; SOLUTION NMR STRUCTURE; MESSENGER-RNA STABILITY; GENERAL STRESS-RESPONSE; ACID MELTING ACTIVITY; DEAD-BOX PROTEINS; ESCHERICHIA-COLI; BACILLUS-SUBTILIS; CSPA-FAMILY; LOW-TEMPERATURE; cold shock protein; cold shock domain; RNA chaperone; nucleic acid binding; cold adaptation; transcription |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Petra Gürster |
| Date Deposited: | 30 Oct 2020 07:43 |
| Last Modified: | 30 Oct 2020 07:43 |
| URI: | https://pred.uni-regensburg.de/id/eprint/32640 |
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