Nucleotide binding activity of SecA homodimer is conformationally regulated by temperature and altered by prlD and azi mutations (Q73626344)

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5 November 2019

title

Nucleotide binding activity of SecA homodimer is conformationally regulated by temperature and altered by prlD and azi mutations (English)

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5 November 2019

author name string

M Schmidt

1

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5 November 2019

H Ding

2

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5 November 2019

V Ramamurthy

3

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5 November 2019

I Mukerji

4

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5 November 2019

D Oliver

5

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5 November 2019

language of work or name

English

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publication date

1 May 2000

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Journal of Biological Chemistry

5 November 2019

published in

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5 November 2019

volume

275

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5 November 2019

issue

20

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5 November 2019

page(s)

15440-15448

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Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli

5 November 2019

cites work

1 reference

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21 January 2018

1 reference

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Preprotein transfer to the Escherichia coli translocase requires the co‐operative binding of SecB and the signal sequence to SecA

21 January 2018

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SecA is required for the insertion of inner membrane proteins targeted by the Escherichia coli signal recognition particle

21 January 2018

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The Escherichia coli SRP and SecB targeting pathways converge at the translocon

21 January 2018

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

21 January 2018

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

21 January 2018

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The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex

21 January 2018

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

21 January 2018

1 reference

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

21 January 2018

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Roles of SecG in ATP- and SecA-dependent protein translocation.

21 January 2018

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Coupled structure changes of SecA and SecG revealed by the synthetic lethality of the secAcsR11 and delta secG::kan double mutant

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding.

21 January 2018

1 reference

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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.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M000605200

SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer.

21 January 2018

1 reference

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Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase

21 January 2018

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

21 January 2018

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Domain interactions of the peripheral preprotein Translocase subunit SecA.

21 January 2018

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Novel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptide

21 January 2018

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Mutations conferring resistance to azide in Escherichia coli occur primarily in the secA gene

21 January 2018

1 reference

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Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery

21 January 2018

1 reference

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Suppression of signal sequence defects and azide resistance in Escherichia coli commonly result from the same mutations in secA

21 January 2018

1 reference

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Differential effect of precursor ribose binding protein of Escherichia coli and its signal peptide on the SecA penetration of lipid bilayer.

21 January 2018

1 reference

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

21 January 2018

1 reference

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Endogenous SecA catalyzes preprotein translocation at SecYEG.

21 January 2018

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Specific recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli

21 January 2018

1 reference

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Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein

21 January 2018

1 reference

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RNA helicase activity of Escherichia coli SecA protein.

21 January 2018

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Staying on track: common features of DNA helicases and microtubule motors.

21 January 2018

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Helicase motifs: the engine that powers DNA unwinding

21 January 2018

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SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M000605200

PrlA and PrlG suppressors reduce the requirement for signal sequence recognition

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M000605200

PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M000605200

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

21 January 2018

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SecA protein is required for secretory protein translocation into E. coli membrane vesicles.

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M000605200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10747939%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

1 reference