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
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.