期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 535, 期 -, 页码 66-72出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2020.12.015
关键词
Bacterial adaptation; DnaK chaperone system; J-domain proteins (JDP); RNA polymerase; Cold stress; Stress response
资金
- Centre National de la Recherche Scientifique
- Aix Marseille Universite
- Agence Nationale de la Recherche [ANR-16-CE11-0002-01]
- MESR fellowship
- Agence Nationale de la Recherche (ANR) [ANR-16-CE11-0002] Funding Source: Agence Nationale de la Recherche (ANR)
Bacteria use molecular pathways and protein networks to adapt to changing environments and stress conditions, with one pathway involving the essential co-chaperone AtcJ in the DnaK/Hsp70 system for cold adaptation. AtcJ is part of the atcJABC operon, and it interacts with RNA polymerase to maintain life at low temperatures.
Bacteria possess several molecular pathways to adapt to changing environments and to stress conditions. One of these pathways involves a complex network of chaperone proteins that together control proteostasis. In the aquatic bacterium Shewanella oneidensis, we have recently identified a previously unknown co-chaperone of the DnaK/Hsp70 chaperone system, AtcJ, that is essential for adaptation to low temperatures. AtcJ is encoded in the atcJABC operon, whose products, together with DnaK, form a protein network allowing growth at low temperature. However, how these proteins allow cold adaptation is unknown. Here, we found that AtcB directly interacts with the RNA polymerase and decreases its activity. In addition, AtcB overproduction prevents bacterial growth due to RNA polymerase inhibition. Together, these results suggest that the Atc proteins could direct the DnaK chaperone to the RNA polymerase to sustain life at low temperatures. (C) 2020 Elsevier Inc. All rights reserved.
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