(Q54529600)

31 May 2018

title

Identification of key regions within the Escherichia coli TatAB subunits. (English)

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31 May 2018

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Claire M L Barrett

1

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31 May 2018

Joanne E Mathers

series ordinal

2

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31 May 2018

Colin Robinson

series ordinal

3

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31 May 2018

language of work or name

English

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publication date

1 February 2003

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31 May 2018

number of pages

5

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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31 May 2018

volume

537

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31 May 2018

issue

1-3

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31 May 2018

page(s)

42-46

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31 May 2018

Protein targeting by the twin-arginine translocation pathway

cites work

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A common export pathway for proteins binding complex redox cofactors?

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A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins

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An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria

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Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein

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Sec-independent protein translocation by the maize Hcf106 protein.

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The maize tha4 gene functions in sec-independent protein transport in chloroplasts and is related to hcf106, tatA, and tatB

21 January 2018

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TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli

21 January 2018

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Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport

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A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid [Delta]pH/Tat translocase

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Essential cytoplasmic domains in the Escherichia coli TatC protein

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Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis

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Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences

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Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli.

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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

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TatD Is a Cytoplasmic Protein with DNase Activity

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The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane

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Subunit interactions in the twin-arginine translocase complex of Escherichia coli

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A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase

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A folded protein can be transported across the chloroplast envelope and thylakoid membranes

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10.1016/S0014-5793(03)00068-1

7 January 2021

Identifiers

DOI

1 reference

31 May 2018

1 reference

31 May 2018