Topology of signal recognition particle receptor in endoplasmic reticulum membrane
- 1 November 1985
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 318 (6044), 334-338
- https://doi.org/10.1038/318334a0
Abstract
The signal recognition particle (SRP) receptor is an integral membrane protein of the endoplasmic reticulum which, in conjunction with SRP, ensures the correct targeting of nascent secretory proteins to this membrane system. From the complementary DNA sequence we have deduced the complete primary structure of the SRP receptor and established that its amino-terminal region is anchored in the membrane. The anchor fragment and the cytoplasmic fragment contribute jointly to a functionally important region which is highly charged and may function in nucleic acid binding.This publication has 31 references indexed in Scilit:
- Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane.The Journal of cell biology, 1985
- Protein translocation across the endoplasmic reticulumCell, 1984
- Transient involvement of signal recognition particle and its receptor in the microsomal membrane prior to protein translocationCell, 1983
- Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor.The Journal of cell biology, 1982
- Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle.The Journal of cell biology, 1982
- Secretory protein translocation across membranes—the role of the ‘docking protein’Nature, 1982
- Codon catalog usage is a genome strategy modulated for gene expressivityNucleic Acids Research, 1981
- A membrane component essential for vectorial translocation of nascent proteins across the endoplasmic reticulum: requirements for its extraction and reassociation with the membrane.The Journal of cell biology, 1980
- Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum.The Journal of cell biology, 1980
- Tryptic dissection and reconstitution of translocation activity for nascent presecretory proteins across microsomal membranes.Proceedings of the National Academy of Sciences, 1979