Abstract：
:Small G proteins have key roles in signal transduction pathways. They are switched from the signaling 'on' to the non-signaling 'off' state when GTPase-activating proteins (GAPs) provide a catalytic residue. The ancient signal recognition particle (SRP)-type GTPases form GTP-dependent homo- and heterodimers and deviate from the canonical switch paradigm in that no GAPs have been identified. Here we show that the YlxH protein activates the SRP-GTPase FlhF. The crystal structure of the Bacillus subtilis FlhF-effector complex revealed that the effector does not contribute a catalytic residue but positions the catalytic machinery already present in SRP-GTPases. We provide a general concept that might also apply to the RNA-driven activation of the universally conserved, co-translational protein-targeting machinery comprising the SRP-GTPases Ffh and FtsY. Our study exemplifies the evolutionary transition from RNA- to protein-driven activation in SRP-GTPases and suggests that the current view on SRP-mediated protein targeting is incomplete.
journal_name
Nat Struct Mol Bioljournal_title
Nature structural & molecular biologyauthors
Bange G,Kümmerer N,Grudnik P,Lindner R,Petzold G,Kressler D,Hurt E,Wild K,Sinning Idoi
10.1038/nsmb.2141subject
Has Abstractpub_date
2011-11-06 00:00:00pages
1376-80issue
12eissn
1545-9993issn
1545-9985pii
nsmb.2141journal_volume
18pub_type
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