Structural basis for the molecular evolution of SRP-GTPase activation by protein
- Bange, Gert Heidelberg University Biochemistry Center, Germany
- Kümmerer, Nico Heidelberg University Biochemistry Center, Germany
- Grudnik, Przemyslaw Heidelberg University Biochemistry Center, Germany
- Lindner, Robert Heidelberg University Biochemistry Center, Germany
- Petzold, Georg Heidelberg University Biochemistry Center, Germany - Research Institute of Molecular Pathology, Vienna, Austria
- Kressler, Dieter Heidelberg University Biochemistry Center, Germany - Unit of Biochemistry, University of Fribourg, Switzerland
- Hurt, Ed Heidelberg University Biochemistry Center, Germany
- Wild, Klemens Heidelberg University Biochemistry Center, Germany
- Sinning, Irmgard Heidelberg University Biochemistry Center, Germany
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06.11.2011
Published in:
- Nature Structural & Molecular Biology. - 2011, vol. 18, p. 1376–1380
English
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.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
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- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 28639
- DOI 10.1038/nsmb.2141
- Persistent URL
- https://folia.unifr.ch/unifr/documents/302350
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