Literature DB >> 1331806

The E. coli ffh gene is necessary for viability and efficient protein export.

G J Phillips1, T J Silhavy.   

Abstract

Homologues of the gene encoding the 54K (M(r) 54,000) subunit of the mammalian signal recognition particle have been identified in different organisms. The Escherichia coli homologue, termed ffh (for fifty-four homologue), specifies a protein (Ffh) that shares many properties with its eukaryotic counterpart, including association with mammalian 7S RNA and the ability to bind signal sequences specifically. Ffh also associates with E. coli 4.5S RNA, showing that it can form a ribonucleoprotein complex in prokaryotes. These results are intriguing because extensive genetic and biochemical characterization of E. coli failed to identify a signal recognition particle-like mechanism for protein export. Here we address this issue directly by construction of a strain in which ffh expression is arabinose-dependent. Results of depletion experiments indicate that Ffh is important in protein translocation.

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Year:  1992        PMID: 1331806     DOI: 10.1038/359744a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  104 in total

1.  The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus.

Authors:  S Kawaguchi; J Müller; D Linde; S Kuramitsu; T Shibata; Y Inoue; D G Vassylyev; S Yokoyama
Journal:  EMBO J       Date:  2001-02-01       Impact factor: 11.598

2.  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

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

Review 4.  Sec-dependent protein export and the involvement of the molecular chaperone SecB.

Authors:  J Kim; D A Kendall
Journal:  Cell Stress Chaperones       Date:  2000-10       Impact factor: 3.667

5.  Mapping an interface of SecY (PrlA) and SecE (PrlG) by using synthetic phenotypes and in vivo cross-linking.

Authors:  C R Harris; T J Silhavy
Journal:  J Bacteriol       Date:  1999-06       Impact factor: 3.490

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

Authors:  David Wickström; Samuel Wagner; Louise Baars; A Jimmy Ytterberg; Mirjam Klepsch; Klaas J van Wijk; Joen Luirink; Jan-Willem de Gier
Journal:  J Biol Chem       Date:  2010-10-05       Impact factor: 5.157

7.  Characterization of the sat operon in Streptococcus mutans: evidence for a role of Ffh in acid tolerance.

Authors:  B H Kremer; M van der Kraan; P J Crowley; I R Hamilton; L J Brady; A S Bleiweis
Journal:  J Bacteriol       Date:  2001-04       Impact factor: 3.490

8.  SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

Authors:  Saskia B Neher; Niels Bradshaw; Stephen N Floor; John D Gross; Peter Walter
Journal:  Nat Struct Mol Biol       Date:  2008-09       Impact factor: 15.369

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

Authors:  Ying Du; Cindy Grove Arvidson
Journal:  J Bacteriol       Date:  2003-04       Impact factor: 3.490

10.  The Srp54 GTPase is essential for protein export in the fission yeast Schizosaccharomyces pombe.

Authors:  S M Althoff; S W Stevens; J A Wise
Journal:  Mol Cell Biol       Date:  1994-12       Impact factor: 4.272

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