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Literature DB >> 8985168

Assembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle.

J W de Gier¹, P Mansournia, Q A Valent, G J Phillips, J Luirink, G von Heijne.

Abstract

Targeting of the cytoplasmic membrane protein leader peptidase (Lep) and a Lep mutant (Lep-inv) that inserts with an inverted topology compared to the wild-type protein was studied in Escherichia coli strains that are conditional for the expression of either Ffh or 4.5S RNA, the two components of the E. coli SRP. Depletion of either component strongly affected the insertion of both Lep and Lep-inv into the cytoplasmic membrane. This indicates that SRP is required for the assembly of cytoplasmic membrane proteins in E. coli.

Entities: Gene Species

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Year: 1996 PMID： 8985168 DOI： 10.1016/s0014-5793(96)01354-3

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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Cited

53 in total

1. The structure of multiple polypeptide domains determines the signal recognition particle targeting requirement of Escherichia coli inner membrane proteins.

Authors: J A Newitt; N D Ulbrandt; H D Bernstein
Journal: J Bacteriol Date: 1999-08 Impact factor: 3.490

2. A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery.

Authors: H Tian; D Boyd; J Beckwith
Journal: Proc Natl Acad Sci U S A Date: 2000-04-25 Impact factor: 11.205

Review 3. Protein targeting to the bacterial cytoplasmic membrane.

Authors: P Fekkes; A J Driessen
Journal: Microbiol Mol Biol Rev Date: 1999-03 Impact factor: 11.056

4. SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein.

Authors: C Neumann-Haefelin; U Schäfer; M Müller; H G Koch
Journal: EMBO J Date: 2000-12-01 Impact factor: 11.598

Assembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle.

1. The structure of multiple polypeptide domains determines the signal recognition particle targeting requirement of Escherichia coli inner membrane proteins.

2. A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery.

Review 3. Protein targeting to the bacterial cytoplasmic membrane.

4. SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein.

5. Competition between Sec- and TAT-dependent protein translocation in Escherichia coli.

6. Consequences of depletion of the signal recognition particle in Escherichia coli.

7. Role for both DNA and RNA in GTP hydrolysis by the Neisseria gonorrhoeae signal recognition particle receptor.

Review 8. The archaeal signal recognition particle: steps toward membrane binding.

9. Novel proteomic tools reveal essential roles of SRP and importance of proper membrane protein biogenesis.

10. Identification of ZipA, a signal recognition particle-dependent protein from Neisseria gonorrhoeae.