PHOSPHORYLATION OF THE HUMAN LA ANTIGEN ON SERINE-366 CAN REGULATE RECYCLING OF RNA-POLYMERASE-III TRANSCRIPTION COMPLEXES

Citation
H. Fan et al., PHOSPHORYLATION OF THE HUMAN LA ANTIGEN ON SERINE-366 CAN REGULATE RECYCLING OF RNA-POLYMERASE-III TRANSCRIPTION COMPLEXES, Cell, 88(5), 1997, pp. 707-715
Citations number
40
Categorie Soggetti
Biology,"Cell Biology
Journal title
CellACNP
ISSN journal
00928674
Volume
88
Issue
5
Year of publication
1997
Pages
707 - 715
Database
ISI
SICI code
0092-8674(1997)88:5<707:POTHLA>2.0.ZU;2-S
Abstract
The human La antigen is an RNA-binding protein that facilitates transc riptional termination and reinitiation by RNA polymerase III. Native L a protein fractionates into transcriptionally active and inactive form s that are unphosphorylated and phosphorylated at serine 366, respecti vely, as determined by enzymatic and mass spectrometric analyses. Seri ne 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 casei n kinase Ii-mediated phosphorylation of La serine 366 and is reversibl e by dephosphorylation. This work demonstrates a novel mechanism of tr anscriptional control at the level of recycling of stable transcriptio n complexes.