Literature DB >> 17935998

Are bacterial 'autotransporters' really transporters?

Harris D Bernstein1.   

Abstract

Autotransporters are bacterial outer membrane proteins that consist of a large N-terminal extracellular domain ('passenger domain') and a C-terminal beta-barrel domain ('beta domain'). The beta domain was originally proposed to function as a channel that transports its own passenger domain across the outer membrane. Results of recent structural, biochemical and molecular genetic studies, however, have challenged this idea. Here I describe an alternative model in which translocation of the passenger domain is mediated by an exogenous factor (possibly a newly identified factor necessary for assembly of outer membrane proteins called 'Omp85/YaeT'), whereas the beta domain only targets the protein to the outer membrane and serves as a membrane anchor.

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Year:  2007        PMID: 17935998     DOI: 10.1016/j.tim.2007.09.007

Source DB:  PubMed          Journal:  Trends Microbiol        ISSN: 0966-842X            Impact factor:   17.079


  26 in total

1.  Comparative analysis of the biochemical and functional properties of C-terminal domains of autotransporters.

Authors:  Elvira Marín; Gustavo Bodelón; Luis Ángel Fernández
Journal:  J Bacteriol       Date:  2010-08-27       Impact factor: 3.490

2.  A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocation.

Authors:  Zora Soprova; Ana Sauri; Peter van Ulsen; Jeremy R H Tame; Tanneke den Blaauwen; Wouter S P Jong; Joen Luirink
Journal:  J Biol Chem       Date:  2010-10-05       Impact factor: 5.157

Review 3.  Adhesins Involved in Attachment to Abiotic Surfaces by Gram-Negative Bacteria.

Authors:  Cécile Berne; Adrien Ducret; Gail G Hardy; Yves V Brun
Journal:  Microbiol Spectr       Date:  2015-08

4.  Purification, crystallization and preliminary X-ray crystallographic analysis of the transport unit of the monomeric autotransporter AIDA-I from Escherichia coli.

Authors:  Iris Gawarzewski; Britta Tschapek; Astrid Hoeppner; Joachim Jose; Sander H J Smits; Lutz Schmitt
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-09-28

5.  The structural basis of autotransporter translocation by TamA.

Authors:  Fabian Gruss; Franziska Zähringer; Roman P Jakob; Björn M Burmann; Sebastian Hiller; Timm Maier
Journal:  Nat Struct Mol Biol       Date:  2013-09-22       Impact factor: 15.369

6.  Role of periplasmic chaperones and BamA (YaeT/Omp85) in folding and secretion of intimin from enteropathogenic Escherichia coli strains.

Authors:  Gustavo Bodelón; Elvira Marín; Luis Angel Fernández
Journal:  J Bacteriol       Date:  2009-06-12       Impact factor: 3.490

7.  Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane.

Authors:  Raffaele Ieva; Harris D Bernstein
Journal:  Proc Natl Acad Sci U S A       Date:  2009-10-22       Impact factor: 11.205

8.  Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain.

Authors:  Raffaele Ieva; Pu Tian; Janine H Peterson; Harris D Bernstein
Journal:  Proc Natl Acad Sci U S A       Date:  2011-06-06       Impact factor: 11.205

9.  Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.

Authors:  Fernando Ruiz-Perez; Ian R Henderson; Denisse L Leyton; Amanda E Rossiter; Yinghua Zhang; James P Nataro
Journal:  J Bacteriol       Date:  2009-09-04       Impact factor: 3.490

Review 10.  Protein secretion systems in bacterial-host associations, and their description in the Gene Ontology.

Authors:  Tsai-Tien Tseng; Brett M Tyler; João C Setubal
Journal:  BMC Microbiol       Date:  2009-02-19       Impact factor: 3.605

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