High-resolution structures of mitochondrial ribosomes and their functional implications

被引：41

作者：

Bieri, Philipp ^{[1
]}

Greber, Basil J. ^{[2
,3
]}

Ban, Nenad ^{[1
]}

机构：

[1] Swiss Fed Inst Technol, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland

[2] Univ Calif Berkeley, Calif Inst Quantitat Biosci QB3, Berkeley, CA 94720 USA

[3] Lawrence Berkeley Natl Lab, Mol Biophys & Integrat Bioimaging Div, Berkeley, CA 94720 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2018年 / 49卷

基金：

瑞士国家科学基金会;

关键词：

TRANSLATION INITIATION; PROTEIN-SYNTHESIS; EVOLUTION; SUBUNIT; ORGANIZATION; DISEASE; COMPLEX; BINDING; MACHINERY; COMPONENT;

D O I：

10.1016/j.sbi.2017.12.009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Mitochondrial ribosomes (mitoribosomes) almost exclusively synthesize essential components of the oxidative phosphorylation machinery. Dysfunction of mitochondrial protein biosynthesis leads to human diseases and plays an important role in the altered metabolism of cancer cells. Recent developments in cryo-electron microscopy enabled the structural characterization of complete yeast and mammalian mitoribosomes at near-atomic resolution. Despite originating from ancestral bacterial ribosomes, mitoribosomes have diverged in their composition and architecture. Mitoribosomal proteins are larger and more numerous, forming an extended network around the ribosomal RNA, which is expanded in yeast and highly reduced in mammals. Novel protein elements at the entrance or exit of the mRNA channel imply a different mechanism of mRNA recruitment. The polypeptide tunnel is optimized for the synthesis of hydrophobic proteins and their co-translational membrane insertion.

引用

页码：44 / 53

页数：10

共 53 条

[1]

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