A minimal set of RNA polymerase II transcription protein interactions
- PMID: 8702741
- DOI: 10.1074/jbc.271.33.20170
A minimal set of RNA polymerase II transcription protein interactions
Abstract
All pairwise interactions of RNA polymerase II and general transcription factors (TF) IIB, E, F, and H have been quantitated by surface plasmon resonance with the use of a Ni2+ chelate on the sensor surface where necessary to attain higher sensitivity. Only 4 of 10 possible interactions were found above the detection limit: TFIIB, -E, and -F binding to RNA polymerase II and TFIIE binding to TFIIH. These four interactions constitute a minimal set for the formation of a transcription initiation complex and may represent the primary interactions involved in assembly of the complex. Point mutations in TFIIB that alter the location of transcription start sites in vivo markedly diminished the affinity of TFIIB binding to RNA polymerase II. Protein blotting revealed an interaction between the largest subunit of TFIIE and third largest subunit of TFIIH, which may be responsible for TFIIE binding to TFIIH.
Similar articles
-
An oligomeric form of the large subunit of transcription factor (TF) IIE activates phosphorylation of the RNA polymerase II carboxyl-terminal domain by TFIIH.J Biol Chem. 1994 Aug 12;269(32):20750-6. J Biol Chem. 1994. PMID: 8051177
-
Functional correlation among Gal11, transcription factor (TF) IIE, and TFIIH in Saccharomyces cerevisiae. Gal11 and TFIIE cooperatively enhance TFIIH-mediated phosphorylation of RNA polymerase II carboxyl-terminal domain sequences.J Biol Chem. 1998 Apr 17;273(16):9534-8. doi: 10.1074/jbc.273.16.9534. J Biol Chem. 1998. PMID: 9545282
-
Identification of a minimal set of proteins that is sufficient for accurate initiation of transcription by RNA polymerase II.Genes Dev. 1993 Jul;7(7A):1254-65. doi: 10.1101/gad.7.7a.1254. Genes Dev. 1993. PMID: 8319911
-
Two-dimensional crystallography of TFIIB- and IIE-RNA polymerase II complexes: implications for start site selection and initiation complex formation.Cell. 1996 May 31;85(5):773-9. doi: 10.1016/s0092-8674(00)81242-8. Cell. 1996. PMID: 8646784
-
Conserved RNA polymerase II initiation complex structure.Curr Opin Struct Biol. 2017 Dec;47:17-22. doi: 10.1016/j.sbi.2017.03.013. Epub 2017 Apr 22. Curr Opin Struct Biol. 2017. PMID: 28437704 Review.
Cited by
-
p53 and TFIIEalpha share a common binding site on the Tfb1/p62 subunit of TFIIH.Proc Natl Acad Sci U S A. 2008 Jan 8;105(1):106-11. doi: 10.1073/pnas.0707892105. Epub 2007 Dec 26. Proc Natl Acad Sci U S A. 2008. PMID: 18160537 Free PMC article.
-
Promoter-specific shifts in transcription initiation conferred by yeast TFIIB mutations are determined by the sequence in the immediate vicinity of the start sites.Mol Cell Biol. 2001 Jul;21(14):4427-40. doi: 10.1128/MCB.21.14.4427-4440.2001. Mol Cell Biol. 2001. PMID: 11416123 Free PMC article.
-
Architecture of an RNA polymerase II transcription pre-initiation complex.Science. 2013 Nov 8;342(6159):1238724. doi: 10.1126/science.1238724. Epub 2013 Sep 26. Science. 2013. PMID: 24072820 Free PMC article.
-
Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications for the initiation of transcription.Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):6969-73. doi: 10.1073/pnas.1130601100. Epub 2003 May 13. Proc Natl Acad Sci U S A. 2003. PMID: 12746498 Free PMC article.
-
Structure and mechanism of the RNA polymerase II transcription machinery.Nat Struct Mol Biol. 2004 May;11(5):394-403. doi: 10.1038/nsmb763. Nat Struct Mol Biol. 2004. PMID: 15114340 Free PMC article. Review.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials
Miscellaneous
