PROSITE logo

PROSITE documentation PDOC00648
Elongation factor 1 beta/beta'/delta chain signatures


Description

Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes [1]. EF-1 is composed of four subunits: the α chain which binds GTP and aminoacyl-tRNAs, the γ chain that probably plays a role in anchoring the complex to other cellular components and the β and delta (or β') chains. The β and delta chains are highly similar proteins that both stimulate the exchange of GDP bound to the α chain for GTP [2]. The β and delta chains are hydrophilic proteins of around 23 to 31 Kd. Their C-terminal part seems important for the nucleotide exchange activity, while the N-terminal section is probably involved in the interaction with the γ chain.

We have developed two signature patterns for this family of proteins. The first corresponds to an acidic region in the central section; the second, to the C-terminal extremity of these proteins.

Expert(s) to contact by email:

Amons R.

Last update:

April 2006 / Pattern revised.

-------------------------------------------------------------------------------


Technical section

PROSITE methods (with tools and information) covered by this documentation:

EF1BD_1, PS00824; Elongation factor 1 beta/beta'/delta chain signature 1  (PATTERN)

EF1BD_2, PS00825; Elongation factor 1 beta/beta'/delta chain signature 2  (PATTERN)


References

1AuthorsRiis B. Rattan S.I. Clark B.F.C. Merrick W.C.
TitleEukaryotic protein elongation factors.
SourceTrends Biochem. Sci. 15:420-424(1990).
PubMed ID2278101

2Authorsvan Damme H.T.F. Amons R. Karssies R. Timmers C.J. Janssen G.M.C. Moeller W.
SourceBiochim. Biophys. Acta 1050:241-247(1990).



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)