Trigger factor interacts with the signal peptide of nascent Tat substrates but does not play a critical role in tat-mediated export.

W.S. Jong, C.M. ten Hagen-Jongman ten, P. Genevaux, J Brunner, B. Oudega, S. Luirink

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Twin-arginine translocation (Tat)-mediated protein transport across the bacterial cytoplasmic membrane occurs only after synthesis and folding of the substrate protein that contains a signal peptide with a characteristic twin-arginine motif. This implies that premature contact between the Tat signal peptide and the Tat translocon in the membrane must be prevented. We used site-specific photo-crosslinking to demonstrate that the signal peptide of nascent Tat proteins is in close proximity to the chaperone and peptidyl-prolyl isomerase trigger factor (TF). The contact with TF was strictly dependent on the context of the translating ribosome, started early in biogenesis when the nascent chain left the ribosome near L23, and persisted until the chain reached its full length. Despite this exclusive and prolonged contact, depletion or overexpression of TF had little effect on the kinetics and efficiency of the Tat export process.
Original languageEnglish
Pages (from-to)4779-4787
Number of pages9
JournalEuropean Journal of Biochemistry
Volume271
DOIs
Publication statusPublished - 2004

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Protein Sorting Signals
Arginine
Substrates
Protein Transport
Ribosomes
Peptidylprolyl Isomerase
Membranes
Proteins
Protein Folding
Crosslinking
Cell Membrane
Kinetics

Cite this

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title = "Trigger factor interacts with the signal peptide of nascent Tat substrates but does not play a critical role in tat-mediated export.",
abstract = "Twin-arginine translocation (Tat)-mediated protein transport across the bacterial cytoplasmic membrane occurs only after synthesis and folding of the substrate protein that contains a signal peptide with a characteristic twin-arginine motif. This implies that premature contact between the Tat signal peptide and the Tat translocon in the membrane must be prevented. We used site-specific photo-crosslinking to demonstrate that the signal peptide of nascent Tat proteins is in close proximity to the chaperone and peptidyl-prolyl isomerase trigger factor (TF). The contact with TF was strictly dependent on the context of the translating ribosome, started early in biogenesis when the nascent chain left the ribosome near L23, and persisted until the chain reached its full length. Despite this exclusive and prolonged contact, depletion or overexpression of TF had little effect on the kinetics and efficiency of the Tat export process.",
author = "W.S. Jong and {ten Hagen-Jongman ten}, C.M. and P. Genevaux and J Brunner and B. Oudega and S. Luirink",
year = "2004",
doi = "10.1111/j.1432-1033.2004.04442.x",
language = "English",
volume = "271",
pages = "4779--4787",
journal = "European Journal of Biochemistry",
issn = "0014-2956",
publisher = "Wiley-Blackwell",

}

Trigger factor interacts with the signal peptide of nascent Tat substrates but does not play a critical role in tat-mediated export. / Jong, W.S.; ten Hagen-Jongman ten, C.M.; Genevaux, P.; Brunner, J; Oudega, B.; Luirink, S.

In: European Journal of Biochemistry, Vol. 271, 2004, p. 4779-4787.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - Trigger factor interacts with the signal peptide of nascent Tat substrates but does not play a critical role in tat-mediated export.

AU - Jong, W.S.

AU - ten Hagen-Jongman ten, C.M.

AU - Genevaux, P.

AU - Brunner, J

AU - Oudega, B.

AU - Luirink, S.

PY - 2004

Y1 - 2004

N2 - Twin-arginine translocation (Tat)-mediated protein transport across the bacterial cytoplasmic membrane occurs only after synthesis and folding of the substrate protein that contains a signal peptide with a characteristic twin-arginine motif. This implies that premature contact between the Tat signal peptide and the Tat translocon in the membrane must be prevented. We used site-specific photo-crosslinking to demonstrate that the signal peptide of nascent Tat proteins is in close proximity to the chaperone and peptidyl-prolyl isomerase trigger factor (TF). The contact with TF was strictly dependent on the context of the translating ribosome, started early in biogenesis when the nascent chain left the ribosome near L23, and persisted until the chain reached its full length. Despite this exclusive and prolonged contact, depletion or overexpression of TF had little effect on the kinetics and efficiency of the Tat export process.

AB - Twin-arginine translocation (Tat)-mediated protein transport across the bacterial cytoplasmic membrane occurs only after synthesis and folding of the substrate protein that contains a signal peptide with a characteristic twin-arginine motif. This implies that premature contact between the Tat signal peptide and the Tat translocon in the membrane must be prevented. We used site-specific photo-crosslinking to demonstrate that the signal peptide of nascent Tat proteins is in close proximity to the chaperone and peptidyl-prolyl isomerase trigger factor (TF). The contact with TF was strictly dependent on the context of the translating ribosome, started early in biogenesis when the nascent chain left the ribosome near L23, and persisted until the chain reached its full length. Despite this exclusive and prolonged contact, depletion or overexpression of TF had little effect on the kinetics and efficiency of the Tat export process.

U2 - 10.1111/j.1432-1033.2004.04442.x

DO - 10.1111/j.1432-1033.2004.04442.x

M3 - Article

VL - 271

SP - 4779

EP - 4787

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

SN - 0014-2956

ER -