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Literature DB >> 23818593

Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species.

Chunfeng Mao¹, Carl E Cheadle, Simon J S Hardy, Angela A Lilly, Yuying Suo, Raghavendar Reddy Sanganna Gari, Gavin M King, Linda L Randall.

Abstract

We have established a reconstitution system for the translocon SecYEG in proteoliposomes in which 55% of the accessible translocons are active. This level corresponds to the fraction of translocons that are active in vitro when assessed in their native environment of cytoplasmic membrane vesicles. Assays using these robust reconstituted proteoliposomes and cytoplasmic membrane vesicles have revealed that the number of SecYEG units involved in an active translocase depends on the precursor undergoing transfer. The active translocase for the precursor of periplasmic galactose-binding protein contains twice the number of heterotrimeric units of SecYEG as does that for the precursor of outer membrane protein A.

Entities: Gene Species

Keywords: SecA; SecB; export; secretion

Mesh：

Substances：

Year: 2013 PMID： 23818593 PMCID： PMC3718118 DOI： 10.1073/pnas.1303289110

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

44 in total

1. Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coli.

Authors: S Matsuyama; Y Fujita; K Sagara; S Mizushima
Journal: Biochim Biophys Acta Date: 1992-07-13

2. Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli.

Authors: R J Cabelli; K M Dolan; L P Qian; D B Oliver
Journal: J Biol Chem Date: 1991-12-25 Impact factor: 5.157

3. The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.

Authors: L Brundage; J P Hendrick; E Schiebel; A J Driessen; W Wickner
Journal: Cell Date: 1990-08-24 Impact factor: 41.582

4. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins.

Authors: R Lill; W Dowhan; W Wickner
Journal: Cell Date: 1990-01-26 Impact factor: 41.582

5. SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm.

Authors: C van der Does; T den Blaauwen; J G de Wit; E H Manting; N A Groot; P Fekkes; A J Driessen
Journal: Mol Microbiol Date: 1996-11 Impact factor: 3.501

6. A significant fraction of functional SecA is permanently embedded in the membrane. SecA cycling on and off the membrane is not essential during protein translocation.

Authors: X Chen; H Xu; P C Tai
Journal: J Biol Chem Date: 1996-11-22 Impact factor: 5.157

7. Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli.

Authors: L L Randall; S J Hardy
Journal: Cell Date: 1986-09-12 Impact factor: 41.582

8. Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli.

Authors: K Uchida; H Mori; S Mizushima
Journal: J Biol Chem Date: 1995-12-29 Impact factor: 5.157

9. Export of periplasmic galactose-binding protein in Escherichia coli depends on the chaperone SecB.

Authors: E L Powers; L L Randall
Journal: J Bacteriol Date: 1995-04 Impact factor: 3.490

10. SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study.

Authors: E Breukink; R A Demel; G de Korte-Kool; B de Kruijff
Journal: Biochemistry Date: 1992-02-04 Impact factor: 3.162

23 in total

1. Determination of the Oligomeric State of SecYEG Protein Secretion Channel Complex Using in Vivo Photo- and Disulfide Cross-linking.

Authors: Zeliang Zheng; Amy Blum; Tithi Banerjee; Qianyu Wang; Virginia Dantis; Donald Oliver
Journal: J Biol Chem Date: 2016-01-08 Impact factor: 5.157

2. Refined measurement of SecA-driven protein secretion reveals that translocation is indirectly coupled to ATP turnover.

Authors: William J Allen; Daniel W Watkins; Mark S Dillingham; Ian Collinson
Journal: Proc Natl Acad Sci U S A Date: 2020-11-30 Impact factor: 11.205

Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species.

1. Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coli.

2. Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli.

3. The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.

4. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins.

5. SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm.

6. A significant fraction of functional SecA is permanently embedded in the membrane. SecA cycling on and off the membrane is not essential during protein translocation.

7. Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli.

8. Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli.

9. Export of periplasmic galactose-binding protein in Escherichia coli depends on the chaperone SecB.

10. SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study.

1. Determination of the Oligomeric State of SecYEG Protein Secretion Channel Complex Using in Vivo Photo- and Disulfide Cross-linking.

2. Refined measurement of SecA-driven protein secretion reveals that translocation is indirectly coupled to ATP turnover.

3. Atomic Force Microscopy Reveals Membrane Protein Activity at the Single Molecule Level.

4. Substrate Proteins Take Shape at an Improved Bacterial Translocon.

5. Coassembly of SecYEG and SecA Fully Restores the Properties of the Native Translocon.

6. Investigating the stability of the SecA-SecYEG complex during protein translocation across the bacterial membrane.

7. Capturing the bacterial holo-complex.

8. Comparison of Single and Multiple Turnovers of SecYEG in Escherichia coli.

9. Membrane chaperone SecDF plays a role in the secretion of Listeria monocytogenes major virulence factors.

Review 10. The Sec System: Protein Export in Escherichia coli.