Abstract
Synthesis of several protein chains of Escherichia coli is markedly, though transiently, induced upon shift-up of a log-phase culture to or above the critical temperature (about 34 degrees C). Such induction occurs coordinately for at least three protein chains (76K, 73K, and 64K) examined. Studies of initial kinetics of induction using a specific inhibitor of transcription (rifampin) revealed that induction occurs at the level of transcription with very little lag, though actual synthesis of messenger ribonucleic acids and proteins requires about 1 min when temperature is shifted up from 30 to 42 degrees C. Evidence suggests that E. coli cells somehow "recognize" the temperature change and activate transcription of several distinct operons, one of which contains the mop (morphogenesis of phages; groE) gene.
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- Ashburner M., Bonner J. J. The induction of gene activity in drosophilia by heat shock. Cell. 1979 Jun;17(2):241–254. doi: 10.1016/0092-8674(79)90150-8. [DOI] [PubMed] [Google Scholar]
- Hendrix R. W. Purification and properties of groE, a host protein involved in bacteriophage assembly. J Mol Biol. 1979 Apr 15;129(3):375–392. doi: 10.1016/0022-2836(79)90502-3. [DOI] [PubMed] [Google Scholar]
- Herendeen S. L., VanBogelen R. A., Neidhardt F. C. Levels of major proteins of Escherichia coli during growth at different temperatures. J Bacteriol. 1979 Jul;139(1):185–194. doi: 10.1128/jb.139.1.185-194.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hohn T., Hohn B., Engel A., Wurtz M., Smith P. R. Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly. J Mol Biol. 1979 Apr 15;129(3):359–373. doi: 10.1016/0022-2836(79)90501-1. [DOI] [PubMed] [Google Scholar]
- Ishihama A., Ikeuchi T., Yura T. A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. I. Copurification and separation. J Biochem. 1976 May;79(5):917–925. doi: 10.1093/oxfordjournals.jbchem.a131159. [DOI] [PubMed] [Google Scholar]
- Ito K., Sato T., Yura T. Synthesis and assembly of the membrane proteins in E. coli. Cell. 1977 Jul;11(3):551–559. doi: 10.1016/0092-8674(77)90073-3. [DOI] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Laskey R. A., Mills A. D. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur J Biochem. 1975 Aug 15;56(2):335–341. doi: 10.1111/j.1432-1033.1975.tb02238.x. [DOI] [PubMed] [Google Scholar]
- Lemaux P. G., Herendeen S. L., Bloch P. L., Neidhardt F. C. Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts. Cell. 1978 Mar;13(3):427–434. doi: 10.1016/0092-8674(78)90317-3. [DOI] [PubMed] [Google Scholar]
- O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
- Sato T., Ohki M., Yura T., Ito K. Genetic studies of an Escherichia coli K-12 temperature-sensitive mutant defective in membrane protein synthesis. J Bacteriol. 1979 May;138(2):305–313. doi: 10.1128/jb.138.2.305-313.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sekiguchi M., Iida S. Mutants of Escherichia coli permeable to actinomycin. Proc Natl Acad Sci U S A. 1967 Dec;58(6):2315–2320. doi: 10.1073/pnas.58.6.2315. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sippel A., Hartmann G. Mode of action of rafamycin on the RNA polymerase reaction. Biochim Biophys Acta. 1968 Mar 18;157(1):218–219. doi: 10.1016/0005-2787(68)90286-4. [DOI] [PubMed] [Google Scholar]
- Sternberg N. Properties of a mutant of Escherichia coli defective in bacteriophage lambda head formation (groE). I. Initial characterization. J Mol Biol. 1973 May 5;76(1):1–23. doi: 10.1016/0022-2836(73)90078-8. [DOI] [PubMed] [Google Scholar]
- VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
- Wehrli W., Staehelin M. Actions of the rifamycins. Bacteriol Rev. 1971 Sep;35(3):290–309. doi: 10.1128/br.35.3.290-309.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yamamori T., Ito K., Nakamura Y., Yura T. Transient regulation of protein synthesis in Escherichia coli upon shift-up of growth temperature. J Bacteriol. 1978 Jun;134(3):1133–1140. doi: 10.1128/jb.134.3.1133-1140.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]