The structure of the human mitochondrial ribosome

被引：386

作者：

Amunts, Alexey ^{[1
]}

Brown, Alan ^{[1
]}

Toots, Jaan ^{[1
]}

Scheres, Sjors H. W. ^{[1
]}

Ramakrishnan, V. ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England

来源：

SCIENCE | 2015年 / 348卷 / 6230期

基金：

英国惠康基金;

关键词：

MESSENGER-RNA; STRANDED-RNA; PROTEIN S1; SUBUNIT; INITIATION; BINDING; TRANSLOCATION; TRANSLATION; SEQUENCES; COMPLEX;

D O I：

10.1126/science.aaa1193

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The highly divergent ribosomes of human mitochondria (mitoribosomes) synthesize 13 essential proteins of oxidative phosphorylation complexes. We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by means of single-particle electron cryogenic microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three ribosomal RNA molecules. The head domain of the small subunit, particularly the messenger (mRNA) channel, is highly remodeled. Many intersubunit bridges are specific to the mitoribosome, which adopts conformations involving ratcheting or rolling of the small subunit that are distinct from those seen in bacteria or eukaryotes. An intrinsic guanosine triphosphatase mediates a contact between the head and central protuberance. The structure provides a reference for analysis of mutations that cause severe pathologies and for future drug design.

引用

页码：95 / 98

页数：4

共 35 条

[21] Ribosomal protein S1 unwinds double-stranded RNA in multiple steps [J].