Major E. coli heat-stress protein do not translocate: implications for cell survival.
When Escherichia coli are exposed to heat stress, the majority of proteins in the process of synthesis at the time of heat stress are rapidly translocated to the outer membrane of the bacterium. The synthesis of most of these proteins appears to take place on membrane-bound polyribosomes. With the temperature shift, overall protein synthesis is inhibited while the synthesis of a small group of proteins is initiated. These proteins are not translocated, but remain in the cytosolic compartment, and they are identifiable as heat-stress proteins. Both the translocation phenomenon and the retention of heat-stress proteins in the cytosolic compartment in proximity to the nucleoid could counteract the effects of heat stress. The translocated proteins may operate by stabilizing the outer membrane prior to the induction of heat-stress proteins and the latter, which are confined to the cytoplasmic compartment, may serve to protect the integrity of the nucleoid structures.
Yatvin
M B
MB
Department of Human Oncology, University of Wisconsin, Madison 53706.
Clark
A W
AW
Siegel
F L
FL
D001426:Bacterial Proteins / Q000378:metabolism*; D002451:Cell Compartmentation; D002462:Cell Membrane / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D004926:Escherichia coli / Q000502:physiology*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006358:Hot Temperature; D007526:Isoelectric Point; D008563:Membrane Lipids / Q000502:physiology; D008970:Molecular Weight
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D008563:Membrane Lipids