Signal recognition particle

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signal recognition particle 9kDa
Identifiers
Symbol(s) SRP9
Entrez 6726
OMIM 600707
RefSeq NM_003133
UniProt P49458
Other data
Locus Chr. 1 q42.12
signal recognition particle 14kDa
Identifiers
Symbol(s) SRP14
Entrez 6727
OMIM 600708
RefSeq NM_003134
UniProt P37108
Other data
Locus Chr. 15 q22
signal recognition particle 19kDa
Identifiers
Symbol(s) SRP19
Entrez 6728
OMIM 182175
RefSeq NM_003135
UniProt P09132
Other data
Locus Chr. 5 q21-q22
signal recognition particle 54kDa
Identifiers
Symbol(s) SRP54
Entrez 6729
OMIM 604857
RefSeq NM_003136
UniProt P61011
Other data
Locus Chr. 14 q13.2
signal recognition particle 68kDa
Identifiers
Symbol(s) SRP68
Entrez 6730
OMIM 604858
RefSeq NM_014230
UniProt Q9UHB9
Other data
Locus Chr. 17 q25.1
signal recognition particle 72kDa
Identifiers
Symbol(s) SRP72
Entrez 6731
OMIM 602122
RefSeq NM_006947
UniProt O76094
Other data
Locus Chr. 4 q11

The signal recognition particle (SRP) is a protein-RNA complex that recognizes and transports specific proteins to the endoplasmic reticulum in eukaryotes and the plasma membrane in prokaryotes. The eukaryotic SRP is composed of six distinct polypeptides bound to an RNA molecule, with GTPase activity. In the GTP-bound state, it recognizes an endoplasmic reticulum signal sequence of eight or more nonpolar amino acid residues at its center.[1] It transiently binds to the endoplasmic reticulum signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor. The core of the SRP is universal, being conserved in all three kingdoms.

The SRP is found in the cytosol. In eukaryotes, it binds to the endoplasmic reticulum signal sequence found in an emerging secretory protein and subsequently delivers the protein along with the ribosome creating it to the endoplasmic reticulum membrane. When SRP binds the endoplasmic reticulum signal sequence, it also binds the ribosome and thereby pauses translation until the entire SRP-bound translation complex is transported to the endoplasmic reticulum, where translation resumes.[2]

SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum membrane. Once the chain reaches the translocon, SRP and its receptor both hydrolyze their bound GTP to GDP, then dislocate allowing translation to restart.

[edit] Components

  • P9
  • P14
  • P19
  • P54
  • P68
  • P72
  • SRP RNA

[edit] History

SRP was identified and characterized by Peter Walter when he was a graduate student in the laboratory of Günter Blobel. [3]