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

被引：98

作者：

Fan, H ^{[1
]}

Sakulich, AL ^{[1
]}

Goodier, JL ^{[1
]}

Zhang, XL ^{[1
]}

Qin, J ^{[1
]}

Maraia, RJ ^{[1
]}

机构：

[1] NHLBI,BIOPHYS CHEM LAB,NIH,BETHESDA,MD 20892

来源：

CELL | 1997年 / 88卷 / 05期

关键词：

D O I：

10.1016/S0092-8674(00)81913-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：707 / 715

页数：9

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