Photocrosslinking demonstrates proximity of a 34 kDa membrane protein to different portions of preprolactin during translocation through the endoplasmic reticulum

FEBS Letters

Hartmann, Enno¹  Rapoport, Tom A.¹  Wiedmann, Martin¹  Goerlich, Dirk¹  Kurzchalia, Teymuras V.¹ 

[1] Zentralinstitut für Molekularbiologie der Akademie der Wissenschaften der DDR, 1115 Berlin-Buch, Robert-Roessle-Str. 10, GDR

关键词: Signal sequence;    Endoplasmic reticulum;    Protein translocation;    Photocrosslinking;    ER;    endoplasmic reticulum;    SRP;    signal recognition particle;    SSR;    signal sequence receptor;    K-RM;    rough microsomes washed with high salt;   

DOI  :  10.1016/0014-5793(89)81549-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown