Phosphorylation of C-terminal domain of RNA polymerase II is not required in basal transcription View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-05

AUTHORS

Hiroaki Serizawa, Joan Weliky Conaway, Ronald C. Conaway

ABSTRACT

PHOSPHORYLATION of the heptapeptide repeats in the C-terminal domain (CTD) of the largest subunit of RNA polymerase II has been widely proposed as an essential step in transcription initiation1–8 on the basis of findings indicating (1) that the CTDs of RNA polymerase II molecules actively engaged in transcription are highly phosphorylated4,9,10; (2) that polymerase molecules containing non-phosphorylated CTDs preferentially enter the preinitiation complex3,11,12 where they are subsequently phosphorylated3,13; and (3) that essential initiation factors b from yeast14–16, δ from rat17,18, and BTF2(TFIIH) from human cells19–21 have closely associated CTD-kinase activities. Here we take advantage of a highly purified enzyme system which supports both CTD phosphorylation and basal transcription to test this hypothesis directly. Using the isoquinoline sulphonamide derivative H-8, which is a potent inhibitor of CTD kinase, we show that basal transcription occurs in the absence of CTD phosphorylation. More... »

PAGES

371-374

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/363371a0

DOI

http://dx.doi.org/10.1038/363371a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022940844

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8497323


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