Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity.
Open Access
- 1 December 1993
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 268 (34), 25425-25431
- https://doi.org/10.1016/s0021-9258(19)74409-3
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- The Escherichia coli chaperones involved in DNA replicadonPhilosophical Transactions Of The Royal Society B-Biological Sciences, 1993
- The translation machinery and 70 kd heat shock protein cooperate in protein synthesisCell, 1992
- Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein foldingNature, 1992
- Protein folding in the cellNature, 1992
- Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of .alpha.-glucosidase from yeastBiochemistry, 1991
- The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent mannerCell, 1990
- THE HEAT-SHOCK PROTEINSAnnual Review of Genetics, 1988
- Speculations on the functions of the major heat shock and glucose-regulated proteinsCell, 1986
- Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptidesJournal of Cellular Physiology, 1980
- Procedure for the rapid, large-scale purification of Escherichia coli DNA-dependent RNA polymerase involving polymin P precipitation and DNA-cellulose chromatographyBiochemistry, 1975