Abstract
We examined the synthesis of individual proteins following depletion of 4.5S RNA by using a strain deficient in the induction of heat shock proteins. We found that initially the synthesis of all proteins was equally affected, and the peptide elongation rate was reduced by approximately 10%. For up to 1 generation time after the onset of inhibition of total protein synthesis, the processing of secreted proteins was unaffected. After further depletion of 4.5S RNA, accumulation of precursors of secreted proteins was observed under some growth conditions.
Full text
PDF




Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bourgaize D. B., Phillips T. A., VanBogelen R. A., Jones P. G., Neidhardt F. C., Fournier M. J. Loss of 4.5S RNA induces the heat shock response and lambda prophage in Escherichia coli. J Bacteriol. 1990 Feb;172(2):1151–1154. doi: 10.1128/jb.172.2.1151-1154.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brown S. 4.5S RNA: does form predict function? New Biol. 1991 May;3(5):430–438. [PubMed] [Google Scholar]
- Brown S., Fournier M. J. The 4.5 S RNA gene of Escherichia coli is essential for cell growth. J Mol Biol. 1984 Sep 25;178(3):533–550. doi: 10.1016/0022-2836(84)90237-7. [DOI] [PubMed] [Google Scholar]
- Brown S. Time of action of 4.5 S RNA in Escherichia coli translation. J Mol Biol. 1989 Sep 5;209(1):79–90. doi: 10.1016/0022-2836(89)90171-x. [DOI] [PubMed] [Google Scholar]
- Heine H. G., Francis G., Lee K. S., Ferenci T. Genetic analysis of sequences in maltoporin that contribute to binding domains and pore structure. J Bacteriol. 1988 Apr;170(4):1730–1738. doi: 10.1128/jb.170.4.1730-1738.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Luirink J., High S., Wood H., Giner A., Tollervey D., Dobberstein B. Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex. Nature. 1992 Oct 22;359(6397):741–743. doi: 10.1038/359741a0. [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]
- Pedersen S. Escherichia coli ribosomes translate in vivo with variable rate. EMBO J. 1984 Dec 1;3(12):2895–2898. doi: 10.1002/j.1460-2075.1984.tb02227.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Phillips G. J., Silhavy T. J. The E. coli ffh gene is necessary for viability and efficient protein export. Nature. 1992 Oct 22;359(6397):744–746. doi: 10.1038/359744a0. [DOI] [PubMed] [Google Scholar]
- Poritz M. A., Bernstein H. D., Strub K., Zopf D., Wilhelm H., Walter P. An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle. Science. 1990 Nov 23;250(4984):1111–1117. doi: 10.1126/science.1701272. [DOI] [PubMed] [Google Scholar]
- Poritz M. A., Strub K., Walter P. Human SRP RNA and E. coli 4.5S RNA contain a highly homologous structural domain. Cell. 1988 Oct 7;55(1):4–6. doi: 10.1016/0092-8674(88)90003-7. [DOI] [PubMed] [Google Scholar]
- Ribes V., Römisch K., Giner A., Dobberstein B., Tollervey D. E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle. Cell. 1990 Nov 2;63(3):591–600. doi: 10.1016/0092-8674(90)90454-m. [DOI] [PubMed] [Google Scholar]
- Sørensen M. A., Kurland C. G., Pedersen S. Codon usage determines translation rate in Escherichia coli. J Mol Biol. 1989 May 20;207(2):365–377. doi: 10.1016/0022-2836(89)90260-x. [DOI] [PubMed] [Google Scholar]
- Walter P., Blobel G. Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes. J Cell Biol. 1981 Nov;91(2 Pt 1):557–561. doi: 10.1083/jcb.91.2.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wood H., Luirink J., Tollervey D. Evolutionary conserved nucleotides within the E.coli 4.5S RNA are required for association with P48 in vitro and for optimal function in vivo. Nucleic Acids Res. 1992 Nov 25;20(22):5919–5925. doi: 10.1093/nar/20.22.5919. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zhou Y. N., Kusukawa N., Erickson J. W., Gross C. A., Yura T. Isolation and characterization of Escherichia coli mutants that lack the heat shock sigma factor sigma 32. J Bacteriol. 1988 Aug;170(8):3640–3649. doi: 10.1128/jb.170.8.3640-3649.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]