Chaperone binding at the ribosomal exit tunnel

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Chaperone binding at the ribosomal exit tunnel. / Kristensen, Ole; Gajhede, Michael.

In: Structure, Vol. 11, No. 12, 2003, p. 1547-56.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Kristensen, O & Gajhede, M 2003, 'Chaperone binding at the ribosomal exit tunnel', Structure, vol. 11, no. 12, pp. 1547-56.

APA

Kristensen, O., & Gajhede, M. (2003). Chaperone binding at the ribosomal exit tunnel. Structure, 11(12), 1547-56.

Vancouver

Kristensen O, Gajhede M. Chaperone binding at the ribosomal exit tunnel. Structure. 2003;11(12):1547-56.

Author

Kristensen, Ole ; Gajhede, Michael. / Chaperone binding at the ribosomal exit tunnel. In: Structure. 2003 ; Vol. 11, No. 12. pp. 1547-56.

Bibtex

@article{abe975bdacc7431a90d59e65e2948a58,
title = "Chaperone binding at the ribosomal exit tunnel",
abstract = "The exit tunnel region of the ribosome is well established as a focal point for interaction between the components that guide the fate of nascent polypeptides. One of these, the chaperone trigger factor (TF), associates with the 50S ribosomal subunit through its N-terminal domain. Targeting of TF to ribosomes is crucial to achieve its remarkable efficiency in protein folding. A similar tight coupling to translation is found in signal recognition particle (SRP)-dependent protein translocation. Here, we report crystal structures of the E. coli TF ribosome binding domain. TF is structurally related to the Hsp33 chaperone but has a prominent ribosome anchor located as a tip of the molecule. This tip includes the previously established unique TF signature motif. Comparison reveals that this feature is not found in SRP structures. We identify a conserved helical kink as a hallmark of the TF structure that is most likely critical to ensure ribosome association.",
keywords = "Amino Acid Motifs, Amino Acid Sequence, Crystallography, X-Ray, Dimerization, Escherichia coli, Escherichia coli Proteins, Models, Molecular, Molecular Sequence Data, Peptidylprolyl Isomerase, Protein Binding, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Transport, Ribosomes, Sequence Homology, Amino Acid, Signal Recognition Particle",
author = "Ole Kristensen and Michael Gajhede",
year = "2003",
language = "English",
volume = "11",
pages = "1547--56",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "12",

}

RIS

TY - JOUR

T1 - Chaperone binding at the ribosomal exit tunnel

AU - Kristensen, Ole

AU - Gajhede, Michael

PY - 2003

Y1 - 2003

N2 - The exit tunnel region of the ribosome is well established as a focal point for interaction between the components that guide the fate of nascent polypeptides. One of these, the chaperone trigger factor (TF), associates with the 50S ribosomal subunit through its N-terminal domain. Targeting of TF to ribosomes is crucial to achieve its remarkable efficiency in protein folding. A similar tight coupling to translation is found in signal recognition particle (SRP)-dependent protein translocation. Here, we report crystal structures of the E. coli TF ribosome binding domain. TF is structurally related to the Hsp33 chaperone but has a prominent ribosome anchor located as a tip of the molecule. This tip includes the previously established unique TF signature motif. Comparison reveals that this feature is not found in SRP structures. We identify a conserved helical kink as a hallmark of the TF structure that is most likely critical to ensure ribosome association.

AB - The exit tunnel region of the ribosome is well established as a focal point for interaction between the components that guide the fate of nascent polypeptides. One of these, the chaperone trigger factor (TF), associates with the 50S ribosomal subunit through its N-terminal domain. Targeting of TF to ribosomes is crucial to achieve its remarkable efficiency in protein folding. A similar tight coupling to translation is found in signal recognition particle (SRP)-dependent protein translocation. Here, we report crystal structures of the E. coli TF ribosome binding domain. TF is structurally related to the Hsp33 chaperone but has a prominent ribosome anchor located as a tip of the molecule. This tip includes the previously established unique TF signature motif. Comparison reveals that this feature is not found in SRP structures. We identify a conserved helical kink as a hallmark of the TF structure that is most likely critical to ensure ribosome association.

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Crystallography, X-Ray

KW - Dimerization

KW - Escherichia coli

KW - Escherichia coli Proteins

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Peptidylprolyl Isomerase

KW - Protein Binding

KW - Protein Conformation

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - Protein Transport

KW - Ribosomes

KW - Sequence Homology, Amino Acid

KW - Signal Recognition Particle

M3 - Journal article

C2 - 14656439

VL - 11

SP - 1547

EP - 1556

JO - Structure

JF - Structure

SN - 0969-2126

IS - 12

ER -

ID: 40318630