The N‐terminal region of yeast mitoribosomal Mrp7/ bL27m protein serves to optimize translation of nascent chains competent for OXPHOS complex assembly
The N‐terminal region of yeast mitoribosomal Mrp7/ bL27m protein serves to optimize translation of nascent chains competent for OXPHOS complex assembly
复制标题
酵母线粒体 Mrp7/bL27m 蛋白的 N 末端区域用于优化能够进行 OXPHOS 复合物组装的新生链的翻译
DOI：
10.1002/1873-3468.14631
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发表时间：
2023
期刊：
影响因子：
3.5
通讯作者：
Stuart, Rosemary A.
中科院分区：
文献类型：
--
作者：
Anderson, Jessica M.;Box, Jodie M.;Stuart, Rosemary A.
线粒体核糖体bL27m蛋白的N端末端残基位于核糖体肽基转移酶中心（PTC）内，并从其细菌祖先中保存下来。酵母Mrp7/bL27m蛋白N端区域的突变或截断不会抑制蛋白质合成，但会显著影响线粒体翻译过程的效率，从而产生能够组装成功能性氧化磷酸化酶的蛋白质。Mrp7/bL27m的N端残基支持正常有丝分裂翻译的需求在呼吸生长过程中更为明显。我们证明Mrp7/bL27m的N端区域影响PTC的环境，并推测bL27m蛋白对新生链的下游命运起到微调和优化线粒体活性的作用。
The extreme N‐terminal residues of the mitochondrial ribosomal bL27m proteins reside within the ribosomal peptidyl transferase center (PTC) and are conserved from their bacterial ancestors. Mutation or truncation of the N‐terminal region of the yeast Mrp7/bL27m protein did not inhibit protein synthesis but significantly impacted the efficacy of the mitochondrial translational process with respect to yielding proteins competent to assemble into functional oxidative phosphorylation enzymes. The requirement for the N‐terminal residues of Mrp7/bL27m to support normal mitotranslation was more apparent under respiratory growth. We demonstrate that the N‐terminal region of Mrp7/bL27m impacts the environment of the PTC and speculate the bL27m proteins serve to fine‐tune and optimize mitoribosomal activity with respect to the downstream fate of the nascent chain.