Protein translocation: checkpoint role for SRP GTPase activation

Gert Bange; Klemens Wild; Irmgard Sinning

doi:10.1016/j.cub.2007.09.041

Protein translocation: checkpoint role for SRP GTPase activation

Curr Biol. 2007 Nov 20;17(22):R980-2. doi: 10.1016/j.cub.2007.09.041.

Authors

Gert Bange¹, Klemens Wild, Irmgard Sinning

Affiliation

¹ Heidelberg University Biochemistry Center (BZH), INF328, D-69120 Heidelberg, Germany.

PMID: 18029258
DOI: 10.1016/j.cub.2007.09.041

Abstract

Co-translational protein targeting by the signal recognition particle (SRP) relies on a complex series of structural rearrangements in the SRP and its receptor (SR). In order to precisely coordinate the individual steps, the GTPases of the SRP and the SR form a unique complex in which GTP hydrolysis is activated in a composite active site. A recent study provides new insights on the link between the GTPases and protein translocation.

MeSH terms

Bacterial Proteins / chemistry*
Bacterial Proteins / metabolism*
Bacterial Proteins / physiology
Enzyme Activation / physiology
GTP Phosphohydrolases / chemistry*
GTP Phosphohydrolases / metabolism*
GTP Phosphohydrolases / physiology
Protein Transport / physiology
Signal Recognition Particle / chemistry
Signal Recognition Particle / physiology*
Thermus / enzymology

Substances

Bacterial Proteins
Signal Recognition Particle
GTP Phosphohydrolases