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人La抗原丝氨酸366位点的磷酸化可调节RNA聚合酶III转录复合物的再循环。

Phosphorylation of the human La antigen on serine 366 can regulate recycling of RNA polymerase III transcription complexes.

作者信息

Fan H, Sakulich A L, Goodier J L, Zhang X, Qin J, Maraia R J

机构信息

Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.

出版信息

Cell. 1997 Mar 7;88(5):707-15. doi: 10.1016/s0092-8674(00)81913-3.

Abstract

The human La antigen is an RNA-binding protein that facilitates transcriptional termination and reinitiation by RNA polymerase III. Native La protein fractionates into transcriptionally active and inactive forms that are unphosphorylated and phosphorylated at serine 366, respectively, as determined by enzymatic and mass spectrometric analyses. Serine 366 comprises a casein kinase II phosphorylation site that resides within a conserved region in the La proteins from several species. RNA synthesis from isolated transcription complexes is inhibited by casein kinase II-mediated phosphorylation of La serine 366 and is reversible by dephosphorylation. This work demonstrates a novel mechanism of transcriptional control at the level of recycling of stable transcription complexes.

摘要

人类La抗原是一种RNA结合蛋白,可促进RNA聚合酶III的转录终止和重新起始。通过酶促分析和质谱分析确定,天然La蛋白可分为转录活性形式和非活性形式,分别在丝氨酸366处未磷酸化和磷酸化。丝氨酸366包含酪蛋白激酶II磷酸化位点,该位点位于几种物种La蛋白的保守区域内。酪蛋白激酶II介导的La丝氨酸366磷酸化可抑制分离的转录复合物的RNA合成,而去磷酸化可使其逆转。这项工作证明了在稳定转录复合物循环水平上的一种新的转录控制机制。

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