The 68 kDa protein of signal recognition particle contains a glycine-rich region also found in certain RNA-binding proteins

Joachim Herz; Nicholas Flint; Keith Stanley; Rainer Frank; Bernhard Dobberstein

doi:10.1016/0014-5793(90)80518-N

The 68 kDa protein of signal recognition particle contains a glycine-rich region also found in certain RNA-binding proteins

Joachim Herz, Nicholas Flint, Keith Stanley, Rainer Frank, Bernhard Dobberstein

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

Abstract

Signal recognition particle (SRP) interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the endoplasmic reticulum. Membrane targeting is mediated by the 68 and the 72 kDa proteins of SRP. We have cloned and sequenced cDNA encoding the 68 kDa protein of canine signal recognition particle (SRP68). SRP68 is a basic protein comprised of 622 amino acid residues. Close to the amino terminus there is a glycine-rich region which SRP68 has in common with some RNA-binding proteins. SRP68 shares no detectable similarity to any of the proteins in data libraries.

Original language	English (US)
Pages (from-to)	103-107
Number of pages	5
Journal	FEBS Letters
Volume	276
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(90)80518-N
State	Published - Dec 10 1990

Keywords

Glycine-rich
Ribonucleoprotein particle
Signal recognition particle
Translocation

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(90)80518-N

Cite this

@article{986c969ab36b4272b47e95388dead680,

title = "The 68 kDa protein of signal recognition particle contains a glycine-rich region also found in certain RNA-binding proteins",

abstract = "Signal recognition particle (SRP) interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the endoplasmic reticulum. Membrane targeting is mediated by the 68 and the 72 kDa proteins of SRP. We have cloned and sequenced cDNA encoding the 68 kDa protein of canine signal recognition particle (SRP68). SRP68 is a basic protein comprised of 622 amino acid residues. Close to the amino terminus there is a glycine-rich region which SRP68 has in common with some RNA-binding proteins. SRP68 shares no detectable similarity to any of the proteins in data libraries.",

keywords = "Glycine-rich, Ribonucleoprotein particle, Signal recognition particle, Translocation",

author = "Joachim Herz and Nicholas Flint and Keith Stanley and Rainer Frank and Bernhard Dobberstein",

year = "1990",

month = dec,

day = "10",

doi = "10.1016/0014-5793(90)80518-N",

language = "English (US)",

volume = "276",

pages = "103--107",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1-2",

}

TY - JOUR

T1 - The 68 kDa protein of signal recognition particle contains a glycine-rich region also found in certain RNA-binding proteins

AU - Herz, Joachim

AU - Flint, Nicholas

AU - Stanley, Keith

AU - Frank, Rainer

AU - Dobberstein, Bernhard

PY - 1990/12/10

Y1 - 1990/12/10

N2 - Signal recognition particle (SRP) interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the endoplasmic reticulum. Membrane targeting is mediated by the 68 and the 72 kDa proteins of SRP. We have cloned and sequenced cDNA encoding the 68 kDa protein of canine signal recognition particle (SRP68). SRP68 is a basic protein comprised of 622 amino acid residues. Close to the amino terminus there is a glycine-rich region which SRP68 has in common with some RNA-binding proteins. SRP68 shares no detectable similarity to any of the proteins in data libraries.

AB - Signal recognition particle (SRP) interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the endoplasmic reticulum. Membrane targeting is mediated by the 68 and the 72 kDa proteins of SRP. We have cloned and sequenced cDNA encoding the 68 kDa protein of canine signal recognition particle (SRP68). SRP68 is a basic protein comprised of 622 amino acid residues. Close to the amino terminus there is a glycine-rich region which SRP68 has in common with some RNA-binding proteins. SRP68 shares no detectable similarity to any of the proteins in data libraries.

KW - Glycine-rich

KW - Ribonucleoprotein particle

KW - Signal recognition particle

KW - Translocation

UR - http://www.scopus.com/inward/record.url?scp=0025630660&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025630660&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(90)80518-N

DO - 10.1016/0014-5793(90)80518-N

M3 - Article

C2 - 1702390

AN - SCOPUS:0025630660

SN - 0014-5793

VL - 276

SP - 103

EP - 107

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

The 68 kDa protein of signal recognition particle contains a glycine-rich region also found in certain RNA-binding proteins

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this