TY - JOUR
T1 - Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
AU - Römisch, Karin
AU - Webb, Jane
AU - Herz, Joachim
AU - Prehn, Siegfried
AU - Frank, Rainer
AU - Vingron, Martin
AU - Dobberstein, Bernhard
PY - 1989
Y1 - 1989
N2 - MOST proteins exported from mammalian cells contain a signal sequence which mediates targeting to and insertion into the mem-brane of the endoplasmic reticulum (ER). Involved in this process are the signal-recognition particle (SRP) and docking protein (DP), the receptor for SRP in the ER membrane. SRP interacts with the signal sequence on nascent polypeptide chains and retards their further elongation, which resumes only after interaction of the arrested ribosomal complex with the docking protein. SRP is a ribonucleoprotein particle comprising a 7S RNA and six polypeptides with relative molecular masses (Mr) of 9,000 (9K) 14K, 19K, 54K, 68K and 72K (ref. 1). The 9K and 14K proteins are essential for elongation arrest and the 68K-72K heterodimer is required for docking to the ER membrane. The 54K protein binds to the signal sequence when it emerges from the ribosome. Docking protein consists of two polypeptides, a 72K α-summit (DPα) and a 30K β-subunit (DPβ). No components structurally homologous to SRP and docking protein have yet been found in yeast or Escherichia coli. To understand the molecular nature of the interaction between the signal sequence and its receptor(s) we have characterized a complementary DNA coding for the 54K protein of SRP. Significant sequence homology was found to part of DPα and two E. coli proteins of unknown function. The homologous region includes a putative GTP#150;binding domain.
AB - MOST proteins exported from mammalian cells contain a signal sequence which mediates targeting to and insertion into the mem-brane of the endoplasmic reticulum (ER). Involved in this process are the signal-recognition particle (SRP) and docking protein (DP), the receptor for SRP in the ER membrane. SRP interacts with the signal sequence on nascent polypeptide chains and retards their further elongation, which resumes only after interaction of the arrested ribosomal complex with the docking protein. SRP is a ribonucleoprotein particle comprising a 7S RNA and six polypeptides with relative molecular masses (Mr) of 9,000 (9K) 14K, 19K, 54K, 68K and 72K (ref. 1). The 9K and 14K proteins are essential for elongation arrest and the 68K-72K heterodimer is required for docking to the ER membrane. The 54K protein binds to the signal sequence when it emerges from the ribosome. Docking protein consists of two polypeptides, a 72K α-summit (DPα) and a 30K β-subunit (DPβ). No components structurally homologous to SRP and docking protein have yet been found in yeast or Escherichia coli. To understand the molecular nature of the interaction between the signal sequence and its receptor(s) we have characterized a complementary DNA coding for the 54K protein of SRP. Significant sequence homology was found to part of DPα and two E. coli proteins of unknown function. The homologous region includes a putative GTP#150;binding domain.
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U2 - 10.1038/340478a0
DO - 10.1038/340478a0
M3 - Article
C2 - 2502717
AN - SCOPUS:0024400708
SN - 0028-0836
VL - 340
SP - 478
EP - 482
JO - Nature
JF - Nature
IS - 6233
ER -