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首页> 外文期刊>Molecular and Cellular Biology >Phosphorylation of the Transcription Elongation Factor Spt5 by Yeast Bur1 Kinase Stimulates Recruitment of the PAF Complex
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Phosphorylation of the Transcription Elongation Factor Spt5 by Yeast Bur1 Kinase Stimulates Recruitment of the PAF Complex

机译：酵母Bur1激酶的转录延伸因子Spt5的磷酸化刺激PAF复合物的招募。

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摘要

The Saccharomyces cerevisiae kinase Bur1 is involved in coupling transcription elongation to chromatin modification, but not all important Bur1 targets in the elongation complex are known. Using a chemical genetics strategy wherein Bur1 kinase was engineered to be regulated by a specific inhibitor, we found that Bur1 phosphorylates the Spt5 C-terminal repeat domain (CTD) both in vivo and in isolated elongation complexes in vitro. Deletion of the Spt5 CTD or mutation of the Spt5 serines targeted by Bur1 reduces recruitment of the PAF complex, which functions to recruit factors involved in chromatin modification and mRNA maturation to elongating polymerase II (Pol II). Deletion of the Spt5 CTD showed the same defect in PAF recruitment as rapid inhibition of Bur1 kinase activity, and this Spt5 mutation led to a decrease in histone H3K4 trimethylation. Brief inhibition of Bur1 kinase activity in vivo also led to a significant decrease in phosphorylation of the Pol II CTD at Ser-2, showing that Bur1 also contributes to Pol II Ser-2 phosphorylation. Genetic results suggest that Bur1 is essential for growth because it targets multiple factors that play distinct roles in transcription.
机译：酿酒酵母 酿酒酵母激酶Bur1参与了转录延伸与染色质修饰的偶联，但并非已知延伸复合物中所有重要的Bur1靶标。使用化学遗传学策略（其中Bur1激酶经过工程改造以受特定抑制剂调控），我们发现Bur1在体内和体外分离的延伸复合物中都将Spt5 C末端重复域（CTD）磷酸化。 Bur1靶向的Spt5 CTD缺失或Spt5丝氨酸突变可减少PAF复合物的募集，PAF复合物的功能是募集参与染色质修饰和mRNA成熟的因子以延长聚合酶II（Pol II）。 Spt5 CTD的删除显示与快速抑制Bur1激酶活性相同的PAF募集缺陷，并且此Spt5突变导致组蛋白H3K4三甲基化降低。体内Bur1激酶活性的短暂抑制也导致Ser-2上Pol II CTD的磷酸化显着降低，表明Bur1也有助于Pol II Ser-2磷酸化。遗传结果表明Bur1对生长至关重要，因为它靶向多种在转录中起不同作用的因子。

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