A human RNA polymerase II transcription termination factor is a SWI2/SNF2 family member
- PMID: 9748214
- DOI: 10.1074/jbc.273.40.25541
A human RNA polymerase II transcription termination factor is a SWI2/SNF2 family member
Abstract
We obtained protein sequence information from Drosophila factor 2, an ATP-dependent RNA polymerase II transcription termination factor, and discovered that it was identical to a SWI2/SNF2 family member called lodestar. Portions of putative human and Caenorhabditis elegans homologues were found in the sequence data bases and a complete cDNA for the human factor was generated using polymerase chain reaction techniques. Recombinant human factor 2 was produced in a baculovirus expression system, purified, and characterized. Similar to the authentic Drosophila factor, the human factor displayed a strong double-stranded DNA-dependent ATPase activity that was inhibited by single-stranded DNA and exhibited RNA polymerase II termination activity. Both factors were able to work on elongation complexes from either species. We discuss the mechanism of termination by factor 2 and the implications for the role of factor 2 in cellular activities.
Similar articles
-
Cloning and characterization of HARP/SMARCAL1: a prokaryotic HepA-related SNF2 helicase protein from human and mouse.Genomics. 2000 May 1;65(3):274-82. doi: 10.1006/geno.2000.6174. Genomics. 2000. PMID: 10857751
-
Identification and characterization of Drosophila relatives of the yeast transcriptional activator SNF2/SWI2.Mol Cell Biol. 1994 Apr;14(4):2225-34. doi: 10.1128/mcb.14.4.2225-2234.1994. Mol Cell Biol. 1994. PMID: 7908117 Free PMC article.
-
A eukaryotic SWI2/SNF2 domain, an exquisite detector of double-stranded to single-stranded DNA transition elements.J Biol Chem. 2000 Mar 17;275(11):7648-55. doi: 10.1074/jbc.275.11.7648. J Biol Chem. 2000. PMID: 10713074
-
Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptor.Nucleic Acids Res. 1994 May 25;22(10):1815-20. doi: 10.1093/nar/22.10.1815. Nucleic Acids Res. 1994. PMID: 8208605 Free PMC article.
-
Snf2 family ATPases and DExx box helicases: differences and unifying concepts from high-resolution crystal structures.Nucleic Acids Res. 2006;34(15):4160-7. doi: 10.1093/nar/gkl540. Epub 2006 Aug 25. Nucleic Acids Res. 2006. PMID: 16935875 Free PMC article. Review.
Cited by
-
Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA.Nucleic Acids Res. 2002 Nov 15;30(22):4926-36. doi: 10.1093/nar/gkf618. Nucleic Acids Res. 2002. PMID: 12433996 Free PMC article.
-
A Mechanism Leading to Changes in Copy Number Variations Affected by Transcriptional Level Might Be Involved in Evolution, Embryonic Development, Senescence, and Oncogenesis Mediated by Retrotransposons.Front Cell Dev Biol. 2021 Feb 11;9:618113. doi: 10.3389/fcell.2021.618113. eCollection 2021. Front Cell Dev Biol. 2021. PMID: 33644055 Free PMC article.
-
mRNA decapping factors and the exonuclease Xrn2 function in widespread premature termination of RNA polymerase II transcription.Mol Cell. 2012 May 11;46(3):311-24. doi: 10.1016/j.molcel.2012.03.006. Epub 2012 Apr 5. Mol Cell. 2012. PMID: 22483619 Free PMC article.
-
β-CASP proteins removing RNA polymerase from DNA: when a torpedo is needed to shoot a sitting duck.Nucleic Acids Res. 2021 Oct 11;49(18):10221-10234. doi: 10.1093/nar/gkab803. Nucleic Acids Res. 2021. PMID: 34551438 Free PMC article. Review.
-
Unraveling the mechanistic features of RNA polymerase II termination by the 5'-3' exoribonuclease Rat1.Nucleic Acids Res. 2015 Mar 11;43(5):2625-37. doi: 10.1093/nar/gkv133. Epub 2015 Feb 26. Nucleic Acids Res. 2015. PMID: 25722373 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous
