TY - JOUR
T1 - Photocrosslinking demonstrates proximity of a 34 kDa membrane protein to different portions of preprolactin during translocation through the endoplasmic reticulum
AU - Wiedmann, Martin
AU - Goerlich, Dirk
AU - Hartmann, Enno
AU - Kurzchalia, Teymuras V.
AU - Rapoport, Tom A.
PY - 1989/11/6
Y1 - 1989/11/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0024807163&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(89)81549-2
DO - 10.1016/0014-5793(89)81549-2
M3 - Journal articles
C2 - 2583273
AN - SCOPUS:0024807163
SN - 0014-5793
VL - 257
SP - 263
EP - 268
JO - FEBS Letters
JF - FEBS Letters
IS - 2
ER -
