期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
卷 1843, 期 8, 页码 1433-1441出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2013.10.013
关键词
Protein targeting; SecYEG; GTPases; Molecular recognition and regulation; Ribosome
资金
- NIH [GM078024]
- Henry and Camille Dreyfus foundation
- Arnold and Mabel Beckman foundation
- David and Lucile Packard foundation
- Betty and Gordon Moore Foundation
Co-translational protein targeting by the Signal Recognition Particle (SRP) is an essential cellular pathway that couples the synthesis of nascent proteins to their proper cellular localization. The bacterial SRP, which contains the minimal ribonucleoprotein core of this universally conserved targeting machine, has served as a paradigm for understanding the molecular basis of protein localization in all cells. In this review, we highlight recent biochemical and structural insights into the molecular mechanisms by which fundamental challenges faced by protein targeting machineries are met in the SRP pathway. Collectively, these studies elucidate how an essential SRP RNA and two regulatory GTPases in the SRP and SRP receptor (SR) enable this targeting machinery to recognize, sense and respond to its biological effectors, i.e. the cargo protein, the target membrane and the translocation machinery, thus driving efficient and faithful co-translational protein targeting. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey. (C) 2013 Elsevier B.V. All rights reserved.
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