Regulation of Escherichia coli secA by cellular protein secretion proficiency requires an intact gene X signal sequence and an active translocon (Q33737540)

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English	Regulation of Escherichia coli secA by cellular protein secretion proficiency requires an intact gene X signal sequence and an active translocon	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

Regulation of Escherichia coli secA by cellular protein secretion proficiency requires an intact gene X signal sequence and an active translocon (English)

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

Escherichia coli

1 reference

based on heuristic

inferred from title

author name string

D Oliver

1

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

J Norman

2

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Europe PubMed Central

PubMed publication ID

29 July 2017

S Sarker

3

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Europe PubMed Central

PubMed publication ID

29 July 2017

language of work or name

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publication date

1 October 1998

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Europe PubMed Central

PubMed publication ID

29 July 2017

Journal of Bacteriology

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Europe PubMed Central

PubMed publication ID

29 July 2017

180

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

19

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

5240-5242

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

Protein translocation in the three domains of life: variations on a theme

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

Dual regulation of Escherichia coli secA translation by distinct upstream elements

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

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.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

Escherichia coli preprotein translocase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

Integration of SecA protein into the Escherichia coli inner membrane is regulated by its amino-terminal ATP-binding domain

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

A signal sequence is not required for protein export in prlA mutants of Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

SecA protein: autoregulated ATPase catalysing preprotein insertion and translocation across the Escherichia coli inner membrane

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

Suppressor mutations that restore export of a protein with a defective signal sequence

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

Intragenic suppressor mutations that restore export of maltose binding protein with a truncated signal peptide

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

secD, a new gene involved in protein export in Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

The first gene in the Escherichia coli secA operon, gene X, encodes a nonessential secretory protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

21 June 2018

Identification of elements on GeneX-secA RNA of Escherichia coli required for SecA binding and secA auto-regulation.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

30 October 2018

SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

30 October 2018

SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

30 October 2018

Competition between ribosome and SecA binding promotes Escherichia coli secA translational regulation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107564

30 October 2018

Regulation of a membrane component required for protein secretion in Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/9748461

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/9748461

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation

1 reference

https://pubmed.ncbi.nlm.nih.gov/9748461

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

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