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. 1984 Dec;81(24):7737–7741. doi: 10.1073/pnas.81.24.7737

Protein export in Escherichia coli requires a soluble activity.

M Müller, G Blobel
PMCID: PMC392227  PMID: 6083561

Abstract

By using a reconstituted cell-free system we have demonstrated the existence of a soluble activity that is required for the export of proteins in Escherichia coli. This export factor sediments at about 12 S. It has been partially purified by passage through an omega-NH2-butylagarose column and by salt elution off a DEAE matrix. The export factor does not contain 6S RNA.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson D. J., Mostov K. E., Blobel G. Mechanisms of integration of de novo-synthesized polypeptides into membranes: signal-recognition particle is required for integration into microsomal membranes of calcium ATPase and of lens MP26 but not of cytochrome b5. Proc Natl Acad Sci U S A. 1983 Dec;80(23):7249–7253. doi: 10.1073/pnas.80.23.7249. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brickman E. R., Oliver D. B., Garwin J. L., Kumamoto C., Beckwith J. The use of extragenic suppressors to define genes involved in protein export in Escherichia coli. Mol Gen Genet. 1984;196(1):24–27. doi: 10.1007/BF00334087. [DOI] [PubMed] [Google Scholar]
  3. Brownlee G. G. Sequence of 6S RNA of E. coli. Nat New Biol. 1971 Feb 3;229(5):147–149. doi: 10.1038/newbio229147a0. [DOI] [PubMed] [Google Scholar]
  4. Burgess R. R. A new method for the large scale purification of Escherichia coli deoxyribonucleic acid-dependent ribonucleic acid polymerase. J Biol Chem. 1969 Nov 25;244(22):6160–6167. [PubMed] [Google Scholar]
  5. Drahos D. J., Hendrix R. W. Effect of bacteriophage lambda infection on synthesis of groE protein and other Escherichia coli proteins. J Bacteriol. 1982 Mar;149(3):1050–1063. doi: 10.1128/jb.149.3.1050-1063.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ferro-Novick S., Honma M., Beckwith J. The product of gene secC is involved in the synthesis of exported proteins in E. coli. Cell. 1984 Aug;38(1):211–217. doi: 10.1016/0092-8674(84)90542-7. [DOI] [PubMed] [Google Scholar]
  7. Hershey J. W., Yanov J., Johnston K., Fakunding J. L. Purification and characterization of protein synthesis initiation factors IF1, IF2, and IF3 from Escherichia coli. Arch Biochem Biophys. 1977 Aug;182(2):626–638. doi: 10.1016/0003-9861(77)90543-4. [DOI] [PubMed] [Google Scholar]
  8. Kung H. F., Fox J. E., Spears C., Brot N., Weissbach H. Studies on the role of ribosomal proteins L 7 and L 12 in the in vitro synthesis of -galactosidase. J Biol Chem. 1973 Jul 25;248(14):5012–5015. [PubMed] [Google Scholar]
  9. Kung H. F., Spears C., Schulz T., Weissbach H. Studies on the in vitro synthesis of beta-galactosidase: necessary components in the ribosomal wash. Arch Biochem Biophys. 1974 Jun;162(2):578–584. doi: 10.1016/0003-9861(74)90218-5. [DOI] [PubMed] [Google Scholar]
  10. Lee S. Y., Bailey S. C., Apirion D. Small stable RNAs from Escherichia coli: evidence for the existence of new molecules and for a new ribonucleoprotein particle containing 6S RNA. J Bacteriol. 1978 Feb;133(2):1015–1023. doi: 10.1128/jb.133.2.1015-1023.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Michaelis S., Beckwith J. Mechanism of incorporation of cell envelope proteins in Escherichia coli. Annu Rev Microbiol. 1982;36:435–465. doi: 10.1146/annurev.mi.36.100182.002251. [DOI] [PubMed] [Google Scholar]
  12. Müller M., Blobel G. In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli. Proc Natl Acad Sci U S A. 1984 Dec;81(23):7421–7425. doi: 10.1073/pnas.81.23.7421. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Müller M., Ibrahimi I., Chang C. N., Walter P., Blobel G. A bacterial secretory protein requires signal recognition particle for translocation across mammalian endoplasmic reticulum. J Biol Chem. 1982 Oct 25;257(20):11860–11863. [PubMed] [Google Scholar]
  14. Oliver D. B., Beckwith J. Regulation of a membrane component required for protein secretion in Escherichia coli. Cell. 1982 Aug;30(1):311–319. doi: 10.1016/0092-8674(82)90037-x. [DOI] [PubMed] [Google Scholar]
  15. Randall-Hazelbauer L., Schwartz M. Isolation of the bacteriophage lambda receptor from Escherichia coli. J Bacteriol. 1973 Dec;116(3):1436–1446. doi: 10.1128/jb.116.3.1436-1446.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Rossi J. J., Soberon X., Marumoto Y., McMahon J., Itakura K. Biological expression of an Escherichia coli consensus sequence promoter and some mutant derivatives. Proc Natl Acad Sci U S A. 1983 Jun;80(11):3203–3207. doi: 10.1073/pnas.80.11.3203. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Schwartz M. Phage lambda receptor (lamB protein) in Escherichia coli. Methods Enzymol. 1983;97:100–112. doi: 10.1016/0076-6879(83)97123-9. [DOI] [PubMed] [Google Scholar]
  18. Silhavy T. J., Benson S. A., Emr S. D. Mechanisms of protein localization. Microbiol Rev. 1983 Sep;47(3):313–344. doi: 10.1128/mr.47.3.313-344.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Walter P., Blobel G. Disassembly and reconstitution of signal recognition particle. Cell. 1983 Sep;34(2):525–533. doi: 10.1016/0092-8674(83)90385-9. [DOI] [PubMed] [Google Scholar]
  20. Walter P., Blobel G. Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum. Nature. 1982 Oct 21;299(5885):691–698. doi: 10.1038/299691a0. [DOI] [PubMed] [Google Scholar]
  21. Walter P., Blobel G. Signal recognition particle: a ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties. Methods Enzymol. 1983;96:682–691. doi: 10.1016/s0076-6879(83)96057-3. [DOI] [PubMed] [Google Scholar]
  22. Walter P., Blobel G. Subcellular distribution of signal recognition particle and 7SL-RNA determined with polypeptide-specific antibodies and complementary DNA probe. J Cell Biol. 1983 Dec;97(6):1693–1699. doi: 10.1083/jcb.97.6.1693. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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]
  24. Walter P., Blobel G. Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein. J Cell Biol. 1981 Nov;91(2 Pt 1):551–556. doi: 10.1083/jcb.91.2.551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Walter P., Ibrahimi I., Blobel G. Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein. J Cell Biol. 1981 Nov;91(2 Pt 1):545–550. doi: 10.1083/jcb.91.2.545. [DOI] [PMC free article] [PubMed] [Google Scholar]

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