共 96 条
Ribosome Structure and Dynamics During Translocation and Termination
被引:67
作者:
Dunkle, Jack A.
[1
]
Cate, Jamie H. D.
[1
,2
,3
]
机构:
[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
[2] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA
[3] Univ Calif Berkeley, Lawrence Berkeley Lab, Phys Biosci Div, Berkeley, CA 94720 USA
来源:
ANNUAL REVIEW OF BIOPHYSICS, VOL 39
|
2010年
/
39卷
关键词:
protein synthesis;
proofreading;
X-ray crystallography;
cryo-electron microscopy;
single-molecule spectroscopy;
STOP CODON RECOGNITION;
PEPTIDE-BOND FORMATION;
TRANSFER-RNA BINDING;
ELONGATION-FACTOR G;
HEAT-SHOCK-PROTEIN;
RELEASE FACTOR;
MESSENGER-RNA;
TRANSLATION TERMINATION;
CRYSTAL-STRUCTURE;
HYBRID STATE;
D O I:
10.1146/annurev.biophys.37.032807.125954
中图分类号:
Q6 [生物物理学];
学科分类号:
071011 ;
摘要:
Protein biosynthesis, or translation, occurs on the ribosome, a large RNA-protein assembly universally conserved in all forms of life. Over the last decade, structures of the small and large ribosomal subunits and of the intact ribosome have begun to reveal the molecular details of how the ribosome works. Both cryo-electron microscopy and X-ray crystallography continue to provide fresh insights into the mechanism of translation. In this review, we describe the most recent structural models of the bacterial ribosome that shed light on the movement of messenger RNA and transfer RNA on the ribosome after each peptide bond is formed, a process termed translocation. We also discuss recent structures that reveal the molecular basis for stop codon recognition during translation termination. Finally, we review recent advances in understanding how bacteria handle errors in both translocation and termination.
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页码:227 / 244
页数:18
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