Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in

PpiD SecYEG translocon YidC chaperone protein cross-linking protein secretion protein sorting protein translocation proteomics quantitative affinity purification-mass spectrometry (qAP-MS)

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
13 12 2019
Historique:
received: 16 08 2019
revised: 25 10 2019
pubmed: 9 11 2019
medline: 14 7 2020
entrez: 9 11 2019
Statut: ppublish

Résumé

The SecYEG translocon constitutes the major protein transport channel in bacteria and transfers an enormous variety of different secretory and inner-membrane proteins. The minimal core of the SecYEG translocon consists of three inner-membrane proteins, SecY, SecE, and SecG, which, together with appropriate targeting factors, are sufficient for protein transport

Identifiants

pubmed: 31699901
pii: S0021-9258(20)30829-2
doi: 10.1074/jbc.RA119.010686
pmc: PMC6916481
doi:

Substances chimiques

Escherichia coli Proteins 0
Membrane Transport Proteins 0
SEC Translocation Channels 0
YIDC protein, E coli 0
PpiD protein, E coli EC 5.2.1.-
Peptidylprolyl Isomerase EC 5.2.1.8

Banques de données

PDB
['4V6M', '46VM']

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

19167-19183

Informations de copyright

© 2019 Jauss et al.

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Auteurs

Benjamin Jauss (B)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.

Narcis-Adrian Petriman (NA)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.
Faculty of Biology, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.

Friedel Drepper (F)

Faculty of Biology, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.
Institute of Biology II, Biochemistry and Functional Proteomics, Faculty of Biology, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.
Signalling Research Centres BIOSS and CIBSS, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.

Lisa Franz (L)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.

Ilie Sachelaru (I)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.

Thomas Welte (T)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.

Ruth Steinberg (R)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.

Bettina Warscheid (B)

Faculty of Biology, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.
Institute of Biology II, Biochemistry and Functional Proteomics, Faculty of Biology, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.
Signalling Research Centres BIOSS and CIBSS, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.

Hans-Georg Koch (HG)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany Hans-Georg.Koch@biochemie.uni-freiburg.de.

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