Literature DB >> 24333859

Structure and mechanism of Escherichia coli type I signal peptidase.

Mark Paetzel1.   

Abstract

Type I signal peptidase is the enzyme responsible for cleaving off the amino-terminal signal peptide from proteins that are secreted across the bacterial cytoplasmic membrane. It is an essential membrane bound enzyme whose serine/lysine catalytic dyad resides on the exo-cytoplasmic surface of the bacterial membrane. This review discusses the progress that has been made in the structural and mechanistic characterization of Escherichia coli type I signal peptidase (SPase I) as well as efforts to develop a novel class of antibiotics based on SPase I inhibition. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey.
Copyright © 2013 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Leader peptidase; Leader peptide; Preprotein processing; Protein secretion; Signal peptidase; Signal peptide

Mesh:

Substances:

Year:  2013        PMID: 24333859     DOI: 10.1016/j.bbamcr.2013.12.003

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  26 in total

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Journal:  J Biol Chem       Date:  2015-10-07       Impact factor: 5.157

2.  Membrane Chaperoning of a Thylakoid Protease Whose Structural Stability Is Modified by the Protonmotive Force.

Authors:  Lucas J McKinnon; Jeremy Fukushima; Joshua K Endow; Kentaro Inoue; Steven M Theg
Journal:  Plant Cell       Date:  2020-03-13       Impact factor: 11.277

Review 3.  Protein Transport Across the Bacterial Plasma Membrane by the Sec Pathway.

Authors:  Dries Smets; Maria S Loos; Spyridoula Karamanou; Anastassios Economou
Journal:  Protein J       Date:  2019-06       Impact factor: 2.371

4.  A putative cro-like repressor contributes to arylomycin resistance in Staphylococcus aureus.

Authors:  Arryn Craney; Floyd E Romesberg
Journal:  Antimicrob Agents Chemother       Date:  2015-03-09       Impact factor: 5.191

5.  Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.

Authors:  Jozefien De Geyter; Athina G Portaliou; Bindu Srinivasu; Srinath Krishnamurthy; Anastassios Economou; Spyridoula Karamanou
Journal:  EMBO Rep       Date:  2020-04-19       Impact factor: 8.807

6.  Chloroplast Chaperonin-Mediated Targeting of a Thylakoid Membrane Protein.

Authors:  Laura Klasek; Kentaro Inoue; Steven M Theg
Journal:  Plant Cell       Date:  2020-10-22       Impact factor: 11.277

Review 7.  The Sec System: Protein Export in Escherichia coli.

Authors:  Jennine M Crane; Linda L Randall
Journal:  EcoSal Plus       Date:  2017-11

8.  Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.

Authors:  Julie A Maupin-Furlow
Journal:  Emerg Top Life Sci       Date:  2018-11-14

9.  Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

Authors:  Joshua K Endow; Rajneesh Singhal; Donna E Fernandez; Kentaro Inoue
Journal:  J Biol Chem       Date:  2015-10-07       Impact factor: 5.157

10.  A Type I Signal Peptidase Is Required for Pilus Assembly in the Gram-Positive, Biofilm-Forming Bacterium Actinomyces oris.

Authors:  Sara D Siegel; Chenggang Wu; Hung Ton-That
Journal:  J Bacteriol       Date:  2016-07-13       Impact factor: 3.490

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