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

Fan Hao, Amy L. Sakulich, John L. Goodier, Xiaolong Zhang, Qin Jun, Richard J. Maraia

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)707-715
Number of pages9
JournalCell
Volume88
Issue number5
DOIs
StatePublished - Mar 7 1997

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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