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首页> 外文期刊>Molecular and Cellular Biology >Physical evidence for cotranslational regulation of beta-tubulin mRNA degradation.
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Physical evidence for cotranslational regulation of beta-tubulin mRNA degradation.

机译：β-微管蛋白mRNA降解共翻译调控的物理证据。

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Tubulin synthesis is controlled by an autoregulatory mechanism through which an increase in the intracellular concentration of tubulin subunits leads to specific degradation of tubulin mRNAs. The sequence necessary and sufficient for the selective degradation of a beta-tubulin mRNA in response to changes in the level of free tubulin subunits resides within the first 13 translated nucleotides that encode the amino-terminal sequence of beta-tubulin, Met-Arg-Glu-Ile (MREI). Previous results have suggested that the sequence responsible for autoregulation resides in the nascent peptide rather than in the mRNA per se, raising the possibility that the regulation of the stability of tubulin mRNA is mediated through binding of tubulin or some other cellular factor to the nascent amino-terminal tubulin peptide. We now show that this putative cotranslational interaction is not mediated by tubulin alone, as no meaningful binding is detectable between tubulin subunits and the amino-terminal beta-tubulin polypeptide. However, microinjection of a monoclonal antibody that binds to the beta-tubulin nascent peptide selectively disrupts the regulation of beta-tubulin, but not alpha-tubulin, synthesis. This finding provides direct evidence for cotranslational degradation of beta-tubulin mRNA mediated through binding of one or more cellular factors to the beta-tubulin nascent peptide.
机译：微管蛋白的合成受自动调节机制的控制，通过这种机制，微管蛋白亚基的细胞内浓度增加会导致微管蛋白mRNA的特异性降解。响应于游离微管蛋白亚基水平的变化而选择性降解β-微管蛋白mRNA所必需和充分的序列位于编码β-微管蛋白Met-Arg-Glu氨基末端序列的前13个翻译核苷酸中-Ile（MREI）。先前的结果表明负责自动调节的序列位于新生肽中，而不是在mRNA本身中，从而增加了微管蛋白mRNA稳定性调节是通过微管蛋白或某些其他细胞因子与新生氨基结合而介导的可能性。 -末端微管蛋白肽。现在我们表明，这种推定的共翻译相互作用不是仅由微管蛋白介导的，因为在微管蛋白亚基和氨基末端β-微管蛋白多肽之间没有可检测到的有意义的结合。然而，与β-微管蛋白新生肽结合的单克隆抗体的显微注射选择性地破坏了β-微管蛋白而不是α-微管蛋白的合成调控。这一发现为通过一种或多种细胞因子与β-微管蛋白新生肽的结合介导的β-微管蛋白mRNA的共翻译降解提供了直接证据。

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