Directly to content
  1. Publishing |
  2. Search |
  3. Browse |
  4. Recent items rss |
  5. Open Access |
  6. Jur. Issues |
  7. DeutschClear Cookie - decide language by browser settings

The methionine-rich domain of the 54 kDa subunit of signal recognition particle is sufficient for the interaction with signal sequences

Lütcke, Henrich ; High, Stephen ; Römisch, Karin ; Ashford, Anthony J. ; Dobberstein, Bernhard

In: The EMBO Journal, 11 (1992), Nr. 4. pp. 1543-1551

[thumbnail of Luetcke_1992_EMBOJ.pdf]
Preview
PDF, English
Download (2MB) | Terms of use

Citation of documents: Please do not cite the URL that is displayed in your browser location input, instead use the DOI, URN or the persistent URL below, as we can guarantee their long-time accessibility.

Abstract

The signal recognition particle (SRP) binds to signal sequences when they emerge from a translating ribosome and targets the complex of ribosome, nascent chain and SRP to the membrane of the rough endoplasmic reticulum (rER) allowing the co-translational translocation of the nascent chain. By photo-crosslinking it has been shown that the signal sequence of preprolactin(PPL) only interacts with the methionine-rich (NI) domain of the 54 kDa protein subunit (SRP54) of SRP. Here we show that (i) a signal-anchor sequence is likewise crosslinked only to the methionine-rich domain of SRP54,(ii) free SRP54 can interact with signal sequences independently of the other components of SRP, (iii) its M domain suffices to perform this function, and (iv) an essentially intact M domain is required for signal sequence recognition. Alkylation of the N+G domain in intact SRP54 with N-ethyl maleimide (NE), but not after cleavage with V8 protease, prevents the binding of a signal sequence to the M domain. This suggests a proximity between the N+G and M domains of SRP54 and raises the possibility that the role of the N+G domain may be to regulate the binding and/or the release of signal sequences.

Document type: Article
Journal or Publication Title: The EMBO Journal
Volume: 11
Number: 4
Date Deposited: 15 Jul 2008 17:26
Date: 1992
Page Range: pp. 1543-1551
Faculties / Institutes: Service facilities > Center for Molecular Biology Heidelberg
DDC-classification: 570 Life sciences
Uncontrolled Keywords: GTP binding protein , methionine-rich domain of SRP54 , photo-crosslinking , signal sequence binding , signal recognition particle
Series: Works by Bernhard Dobberstein
About | FAQ | Contact | Imprint |
OA-LogoDINI certificate 2013Logo der Open-Archives-Initiative