The signal recognition particle

R. J. Keenan; D. M. Freymann; R. M. Stroud; P. Walter

doi:10.1146/annurev.biochem.70.1.755

The signal recognition particle

R. J. Keenan^*, D. M. Freymann, R. M. Stroud, P. Walter

^*Corresponding author for this work

Biochemistry and Molecular Genetics

Research output: Contribution to journal › Review article › peer-review

496 Scopus citations

Abstract

The signal recognition panicle (SRP) and its membrane-associated receptor (SR) catalyze targeting of nascent secretory and membrane proteins to the protein translocation apparatus of the cell. Components of the SRP pathway and salient features of the molecular mechanism of SRP-dependent protein targeting are conserved in all three kingdoms of life, Recent advances in the structure determination of a number of key components in the eukaryotic and prokaryotic SRP pathway provide new insight into the molecular basis of SRP function, and they set the stage for future work toward an integrated picture that takes into account the dynamic and contextual properties of this remarkable cellular machine.

Original language	English (US)
Pages (from-to)	755-775
Number of pages	21
Journal	Annual review of biochemistry
Volume	70
DOIs	https://doi.org/10.1146/annurev.biochem.70.1.755
State	Published - 2001

Keywords

Alu domain
Ffh
FtsY
GTPase
SRP
SRP RNA
SRP receptor
SRP54
SRP9/14
Signal sequence

ASJC Scopus subject areas

Biochemistry

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10.1146/annurev.biochem.70.1.755

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title = "The signal recognition particle",

abstract = "The signal recognition panicle (SRP) and its membrane-associated receptor (SR) catalyze targeting of nascent secretory and membrane proteins to the protein translocation apparatus of the cell. Components of the SRP pathway and salient features of the molecular mechanism of SRP-dependent protein targeting are conserved in all three kingdoms of life, Recent advances in the structure determination of a number of key components in the eukaryotic and prokaryotic SRP pathway provide new insight into the molecular basis of SRP function, and they set the stage for future work toward an integrated picture that takes into account the dynamic and contextual properties of this remarkable cellular machine.",

keywords = "Alu domain, Ffh, FtsY, GTPase, SRP, SRP RNA, SRP receptor, SRP54, SRP9/14, Signal sequence",

author = "Keenan, {R. J.} and Freymann, {D. M.} and Stroud, {R. M.} and P. Walter",

year = "2001",

doi = "10.1146/annurev.biochem.70.1.755",

language = "English (US)",

volume = "70",

pages = "755--775",

journal = "Annual review of biochemistry",

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T1 - The signal recognition particle

AU - Keenan, R. J.

AU - Freymann, D. M.

AU - Stroud, R. M.

AU - Walter, P.

PY - 2001

Y1 - 2001

N2 - The signal recognition panicle (SRP) and its membrane-associated receptor (SR) catalyze targeting of nascent secretory and membrane proteins to the protein translocation apparatus of the cell. Components of the SRP pathway and salient features of the molecular mechanism of SRP-dependent protein targeting are conserved in all three kingdoms of life, Recent advances in the structure determination of a number of key components in the eukaryotic and prokaryotic SRP pathway provide new insight into the molecular basis of SRP function, and they set the stage for future work toward an integrated picture that takes into account the dynamic and contextual properties of this remarkable cellular machine.

AB - The signal recognition panicle (SRP) and its membrane-associated receptor (SR) catalyze targeting of nascent secretory and membrane proteins to the protein translocation apparatus of the cell. Components of the SRP pathway and salient features of the molecular mechanism of SRP-dependent protein targeting are conserved in all three kingdoms of life, Recent advances in the structure determination of a number of key components in the eukaryotic and prokaryotic SRP pathway provide new insight into the molecular basis of SRP function, and they set the stage for future work toward an integrated picture that takes into account the dynamic and contextual properties of this remarkable cellular machine.

KW - Alu domain

KW - Ffh

KW - FtsY

KW - GTPase

KW - SRP

KW - SRP RNA

KW - SRP receptor

KW - SRP54

KW - SRP9/14

KW - Signal sequence

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U2 - 10.1146/annurev.biochem.70.1.755

DO - 10.1146/annurev.biochem.70.1.755

M3 - Review article

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AN - SCOPUS:0034923677

SN - 0066-4154

VL - 70

SP - 755

EP - 775

JO - Annual review of biochemistry

JF - Annual review of biochemistry

ER -

The signal recognition particle

Abstract

Keywords

ASJC Scopus subject areas

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