Elongational stalling activates mitoribosome-associated quality control

doi:10.1126/science.abc7782

GSTDTAP > 气候变化

DOI	10.1126/science.abc7782
	Elongational stalling activates mitoribosome-associated quality control
	Nirupa Desai; Hanting Yang; Viswanathan Chandrasekaran; Razina Kazi; Michal Minczuk; V. Ramakrishnan
	2020-11-27
发表期刊	Science
出版年	2020
英文摘要	Human mitochondria have their own genome and ribosomes called mitoribosomes that respectively encode and synthesize essential subunits of complexes that use the energy from the oxidation of metabolites to drive the synthesis of adenosine triphosphate (ATP). These complexes are key to the health of the cell. Desai et al. studied a mitoribosome-associated quality control pathway that prevents aberrant translation. They purified mitoribosomes under conditions designed to induce stalling and determined the structures of two intermediates in the rescue pathway. These structures revealed two proteins that eject the unfinished polypeptide chain and peptidyl transfer RNA from the ribosome. Their cryo–electron microscopy dataset also revealed additional states that may correspond to intermediates in the mitochondrial translation elongation cycle. Science , this issue p. [1105][1] The human mitochondrial ribosome (mitoribosome) and associated proteins regulate the synthesis of 13 essential subunits of the oxidative phosphorylation complexes. We report the discovery of a mitoribosome-associated quality control pathway that responds to interruptions during elongation, and we present structures at 3.1- to 3.3-angstrom resolution of mitoribosomal large subunits trapped during ribosome rescue. Release factor homolog C12orf65 (mtRF-R) and RNA binding protein C6orf203 (MTRES1) eject the nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome biogenesis factors to these quality control intermediates suggests additional roles for these factors during mitoribosome rescue. We also report related cryo–electron microscopy structures (3.7 to 4.4 angstrom resolution) of elongating mitoribosomes bound to tRNAs, nascent polypeptides, the guanosine triphosphatase elongation factors mtEF-Tu and mtEF-G1, and the Oxa1L translocase. [1]: /lookup/doi/10.1126/science.abc7782
领域	气候变化 ; 资源环境
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引用统计
文献类型	期刊论文
条目标识符	http://119.78.100.173/C666/handle/2XK7JSWQ/304887
专题	气候变化资源环境科学
推荐引用方式 GB/T 7714	Nirupa Desai,Hanting Yang,Viswanathan Chandrasekaran,et al. Elongational stalling activates mitoribosome-associated quality control[J]. Science,2020.
APA	Nirupa Desai,Hanting Yang,Viswanathan Chandrasekaran,Razina Kazi,Michal Minczuk,&V. Ramakrishnan.(2020).Elongational stalling activates mitoribosome-associated quality control.Science.
MLA	Nirupa Desai,et al."Elongational stalling activates mitoribosome-associated quality control".Science (2020).