Genomic and proteomic analysis of transcription factor TFII-I reveals insight into the response to cellular stress.

 
TitleGenomic and proteomic analysis of transcription factor TFII-I reveals insight into the response to cellular stress.
Publication TypeJournal Article
Year of Publication2014
AuthorsFan, AXiucheng, Papadopoulos, GL, Hossain, MA, Lin, I-J, Hu, J, Tang, TMing, Kilberg, MS, Renne, R, Strouboulis, J, Bungert, J
JournalNucleic Acids Res
Volume42
Issue12
Pagination7625-41
Date Published2014 Jul
ISSN1362-4962
KeywordsActivating Transcription Factor 3, Binding Sites, Biotinylation, Carbon-Nitrogen Ligases, DNA Topoisomerases, Type II, Escherichia coli Proteins, Genomics, Humans, K562 Cells, Nuclear Proteins, Proteomics, Repressor Proteins, RNA Polymerase II, Stress, Physiological, TATA-Binding Protein Associated Factors, Transcription Factors, Transcription Factors, TFII, Transcription Initiation Site
Abstract

The ubiquitously expressed transcription factor TFII-I exerts both positive and negative effects on transcription. Using biotinylation tagging technology and high-throughput sequencing, we determined sites of chromatin interactions for TFII-I in the human erythroleukemia cell line K562. This analysis revealed that TFII-I binds upstream of the transcription start site of expressed genes, both upstream and downstream of the transcription start site of repressed genes, and downstream of RNA polymerase II peaks at the ATF3 and other stress responsive genes. At the ATF3 gene, TFII-I binds immediately downstream of a Pol II peak located 5 kb upstream of exon 1. Induction of ATF3 expression increases transcription throughout the ATF3 gene locus which requires TFII-I and correlates with increased association of Pol II and Elongin A. Pull-down assays demonstrated that TFII-I interacts with Elongin A. Partial depletion of TFII-I expression caused a reduction in the association of Elongin A with and transcription of the DNMT1 and EFR3A genes without a decrease in Pol II recruitment. The data reveal different interaction patterns of TFII-I at active, repressed, or inducible genes, identify novel TFII-I interacting proteins, implicate TFII-I in the regulation of transcription elongation and provide insight into the role of TFII-I during the response to cellular stress.

DOI10.1093/nar/gku467
Alternate JournalNucleic Acids Res.
PubMed ID24875474
PubMed Central IDPMC4081084
Grant ListR01 CA088763 / CA / NCI NIH HHS / United States
R01DK083389 / DK / NIDDK NIH HHS / United States
R01DK09062 / DK / NIDDK NIH HHS / United States
R01DK094729 / DK / NIDDK NIH HHS / United States