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Photocrosslinking demonstrates proximity of a 34 kDa membrane protein to different portions of preprolactin during translocation through the endoplasmic reticulum
Author(s) -
Wiedmann Martin,
Goerlich Dirk,
Hartmann Enno,
Kurzchalia Teymuras V.,
Rapoport Tom A.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81549-2
Subject(s) - endoplasmic reticulum , signal peptide , chromosomal translocation , stim1 , transmembrane protein , sec61 , membrane protein , glycoprotein , biochemistry , protein sorting signals , membrane glycoproteins , integral membrane protein , membrane , sequence (biology) , biology , peptide sequence , transmembrane domain , chemistry , translocon , receptor , gene
Photocrosslinking has been used to identify integral proteins of the endoplasmic reticulum membrane that are in proximity to nascent preprolactin during in vitro translocation. A photoreactive lysyl derivative was introduced into truncated preprolactin chains comprising 86 or 115 amino acids. Both with the 86mer, containing the reactive group in the signal sequence, and with the 115mer, containing the probe exclusively in the mature portion of the chain, photocrosslinking occurred to a 3̃5 kDa transmembrane glycoprotein, the signal sequence receptor (SSR). SSR is identical with a previously isolated abundant and ubiquitous 34 kDa membrane protein that appears to be essential for protein translocation.