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首页> 外文期刊>Journal of Molecular Biology >PUF3 acceleration of deadenylation in vivo can operate independently of CCR4 activity, possibly involving effects on the PAB1-mRNP structure.
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PUF3 acceleration of deadenylation in vivo can operate independently of CCR4 activity, possibly involving effects on the PAB1-mRNP structure.

机译：体内PUF3加速腺苷酸化作用可以独立于CCR4活性进行，可能涉及对PAB1-mRNP结构的影响。

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摘要

The evolutionarily conserved PUF proteins stimulate CCR4 mRNA deadenylation through binding to 3' untranslated region sequences of specific mRNA. We have investigated the mechanisms by which PUF3 in Saccharomyces cerevisiae accelerates deadenylation of the COX17 mRNA. PUF3 was shown to affect PAN2 deadenylation of the COX17 mRNA independent of the presence of CCR4, suggesting that PUF3 acts through a general mechanism to affect deadenylation. Similarly, eIF4E, the cap-binding translation initiation factor known to control CCR4 deadenylation, was shown to affect PAN2 activity in vivo. PUF3 was found to be required for eIF4E effects on COX17 deadenylation. Both eIF4E and PUF3 effects on deadenylation were shown, in turn, to necessitate a functional poly(A)-binding protein (PAB1) in which removal of the RRM1 (RNA recognition motif 1) domain of PAB1 blocked both their effects on deadenylation. While removal of the proline-rich region (P domain) of PAB1 substantially reduces CCR4 deadenylation at non-PUF3-controlled mRNA and correspondingly blocked eIF4E effects on deadenylation, PUF3 essentially bypassed this P domain requirement. These results indicate that the PAB1-mRNP structure is critical for PUF3 action. We also found that multiple components of the CCR4-NOT deadenylase complex, but not PAN2, interacted with PUF3. PUF3 appears, therefore, both to act independently of CCR4 activity, possibly through effects on PAB1-mRNP structure, and to be capable of retaining the CCR4-NOT complex.
机译：进化保守的PUF蛋白通过与特定mRNA的3'非翻译区序列结合来刺激CCR4 mRNA的腺苷酸化。我们已经研究了酿酒酵母中的PUF3加速COX17 mRNA的腺苷酸化的机制。已显示PUF3会独立于CCR4的存在而影响COX17 mRNA的PAN2腺苷酸化，这表明PUF3通过一般机制影响腺苷酸化。同样，eIF4E是已知的控制CCR4腺苷酸化的帽结合翻译起始因子，已显示其在体内影响PAN2活性。发现PUF3是eIF4E对COX17腺苷酸化作用所必需的。依次显示，eIF4E和PUF3对腺苷酸化的影响都需要一种功能性的聚（A）结合蛋白（PAB1），其中去除PAB1的RRM1（RNA识别基序1）结构域会同时阻止它们对腺苷酸化的影响。虽然去除PAB1的富含脯氨酸的区域（P结构域）可大大减少非PUF3控制的mRNA处的CCR4腺苷酸化并相应地阻断eIF4E对腺苷酸化的影响，但PUF3基本上绕过了该P结构域的要求。这些结果表明，PAB1-mRNP结构对于PUF3的作用至关重要。我们还发现，CCR4-NOT腺苷酸酶复合物的多个成分（而不是PAN2）与PUF3相互作用。因此，PUF3似乎既独立于CCR4活性，又可能通过影响PAB1-mRNP结构而起作用，并且能够保留CCR4-NOT复合物。

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