TY  - JOUR
ID  - heidok8555
AV  - public
KW  - GTP binding protein 
KW  -  methionine-rich domain of SRP54 
KW  -  photo-crosslinking 
KW  -  signal sequence binding 
KW  -  signal recognition particle
JF  - The EMBO Journal
N2  - 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.
VL  - 11
EP  - 1551
IS  - 4
TI  - The methionine-rich domain of the 54 kDa subunit of signal recognition particle is sufficient for the interaction with signal sequences
UR  - https://archiv.ub.uni-heidelberg.de/volltextserver/8555/
Y1  - 1992///
SP  - 1543
A1  - Lütcke, Henrich
A1  - High, Stephen
A1  - Römisch, Karin
A1  - Ashford, Anthony J.
A1  - Dobberstein, Bernhard
ER  -