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

Martin Wiedmann; Dirk Goerlich; Enno Hartmann; Teymuras V. Kurzchalia; Tom A. Rapoport

doi:10.1016/0014-5793(89)81549-2

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

Martin Wiedmann^*, Dirk Goerlich, Enno Hartmann, Teymuras V. Kurzchalia, Tom A. Rapoport

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Biologie

Akademie der Wissenschaften der DDR

56 Zitate (Scopus)

Abstract

Originalsprache	Englisch
Zeitschrift	FEBS Letters
Jahrgang	257
Ausgabenummer	2
Seiten (von - bis)	263-268
Seitenumfang	6
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(89)81549-2
Publikationsstatus	Veröffentlicht - 06.11.1989

UN SDGs

Dieser Output leistet einen Beitrag zu folgendem(n) Ziel(en) für nachhaltige Entwicklung

SDG 3 – Gesundheit und Wohlergehen

Dokumente

10.1016/0014-5793(89)81549-2

Weitere Links

Link to publication in Scopus

Zitieren

@article{06e3fec9ca5749039bf4b1a7b28cdce5,

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

abstract = "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 {\~3}5 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.",

author = "Martin Wiedmann and Dirk Goerlich and Enno Hartmann and Kurzchalia, \{Teymuras V.\} and Rapoport, \{Tom A.\}",

year = "1989",

month = nov,

day = "6",

doi = "10.1016/0014-5793(89)81549-2",

language = "English",

volume = "257",

pages = "263--268",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc",

number = "2",

}

Photocrosslinking demonstrates proximity of a 34 kDa membrane protein to different portions of preprolactin during translocation through the endoplasmic reticulum. / Wiedmann, Martin; Goerlich, Dirk; Hartmann, Enno et al.
in: FEBS Letters, Jahrgang 257, Nr. 2, 06.11.1989, S. 263-268.

Publikation: Beiträge in Fachzeitschriften › Zeitschriftenaufsätze › Forschung › Begutachtung

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 - https://www.scopus.com/pages/publications/0024807163

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 -

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

Abstract

UN SDGs

Dokumente

Weitere Links

Fingerprint

Zitieren