Literature DB >> 2656409

Characterization of the Escherichia coli protein-export gene secB.

C A Kumamoto1, A K Nault.   

Abstract

The Escherichia coli secB gene product is required for normal export of envelope proteins out of the cell cytoplasm. In this report, we present the identification and nucleotide sequence of the secB coding sequence. The secB structural gene overlaps almost completely with a predicted open reading frame (ORF) that is encoded on the opposite strand. To establish the identity of the secB ORF, we characterized a secB mutation that caused total loss of secB function, based upon its phenotype. This mutation resulted from a nucleotide change that caused an ochre mutation in one ORF (the secB gene) and a silent (no amino acid change) codon change in the opposite ORF.

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Year:  1989        PMID: 2656409     DOI: 10.1016/0378-1119(89)90393-4

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  27 in total

Review 1.  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 2.  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

Review 3.  The sec and prl genes of Escherichia coli.

Authors:  K L Bieker; G J Phillips; T J Silhavy
Journal:  J Bioenerg Biomembr       Date:  1990-06       Impact factor: 2.945

4.  Escherichia coli SecB protein associates with exported protein precursors in vivo.

Authors:  C A Kumamoto
Journal:  Proc Natl Acad Sci U S A       Date:  1989-07       Impact factor: 11.205

5.  Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits.

Authors:  A P Vogler; M Homma; V M Irikura; R M Macnab
Journal:  J Bacteriol       Date:  1991-06       Impact factor: 3.490

6.  Requirement of the SecB chaperone for export of a non-secretory polypeptide in Escherichia coli.

Authors:  S MacIntyre; B Mutschler; U Henning
Journal:  Mol Gen Genet       Date:  1991-06

7.  The SecB chaperone is bifunctional in Serratia marcescens: SecB is involved in the Sec pathway and required for HasA secretion by the ABC transporter.

Authors:  Guillaume Sapriel; Cécile Wandersman; Philippe Delepelaire
Journal:  J Bacteriol       Date:  2003-01       Impact factor: 3.490

8.  SecY, a multispanning integral membrane protein, contains a potential leader peptidase cleavage site.

Authors:  Y Akiyama; T Inada; Y Nakamura; K Ito
Journal:  J Bacteriol       Date:  1990-06       Impact factor: 3.490

9.  Electrospray mass spectrometric investigation of the chaperone SecB.

Authors:  V F Smith; B L Schwartz; L L Randall; R D Smith
Journal:  Protein Sci       Date:  1996-03       Impact factor: 6.725

10.  The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter.

Authors:  P Delepelaire; C Wandersman
Journal:  EMBO J       Date:  1998-02-16       Impact factor: 11.598

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