The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex.
Author(s) -
Hua Lu,
Osvaldo Flores,
Roberto Weinmann,
Danny Reinberg
Publication year - 1991
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.22.10004
Subject(s) - transcription preinitiation complex , transcription factor ii e , rna polymerase ii , transcription factor ii f , polymerase , microbiology and biotechnology , chemistry , phosphopeptide , transcription factor ii d , phosphorylation , biophysics , biology , biochemistry , rna dependent rna polymerase , enzyme , gene expression , gene , promoter
The two forms of RNA polymerase II that exist in vivo, phosphorylated (IIO) and nonphosphorylated (IIA), were purified to apparent homogeneity from HeLa cells. The nonphosphorylated form preferentially binds to the preinitiation complex. RNA polymerase II in the complex was converted by a cellular protein kinase to the phosphorylated form.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom