Binding of zinc finger protein transcription factor IIIA to its cognate DNA sequence with single UV photoproducts at specific sites and its effect on DNA repair

YoungHo Kwon; Michael J Smerdon

doi:10.1074/jbc.M308645200

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Binding of zinc finger protein transcription factor IIIA to its cognate DNA sequence with single UV photoproducts at specific sites and its effect on DNA repair

Journal article

Open access

Peer reviewed

Binding of zinc finger protein transcription factor IIIA to its cognate DNA sequence with single UV photoproducts at specific sites and its effect on DNA repair

YoungHo Kwon and Michael J Smerdon

The Journal of biological chemistry, Vol.278(46), pp.45451-45459

11/14/2003

DOI: https://doi.org/10.1074/jbc.M308645200

Handle:

https://hdl.handle.net/2376/108534

PMID: 12963720

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Abstract

Xenopus

Zinc Fingers

Models, Chemical

Xenopus laevis

Molecular Sequence Data

Transcription Factor TFIIIA - chemistry

DNA, Ribosomal - metabolism

DNA - metabolism

Transcription Factor TFIIIA - metabolism

Dose-Response Relationship, Drug

RNA, Ribosomal, 5S - metabolism

Animals

Ultraviolet Rays

Time Factors

Models, Biological

Base Sequence

DNA Repair

Protein Binding

Models, Genetic

DNA Damage

Kinetics

Binding Sites

The relationship between DNA repair efficiency at specific locations in the binding site of the nine-zinc finger protein transcription factor IIIA (TFIIIA) and binding of its individual zinc fingers was studied. Homogeneously damaged oligonucleotides, which contained a single cis-syn cyclobutane thymine dimer (CTD) at one of six different sites in the internal control region (ICR) of the 5 S rRNA gene to generate a series of damaged DNA substrates, were prepared by chemical synthesis. Binding of TFIIIA to the substrates was assayed by measurement of dissociation constants (Kd), dissociation rates (koff), and protein-DNA contacts. The results indicated that a single CTD in the ICR does not significantly affect the Kd of TFIIIA. In contrast, CTDs at positions +55 and +72 (from the transcription start site) in the ICR markedly enhanced koff of TFIIIA from the complex. In addition, CTDs in these two sites increased methylation of the N7 of guanines (by dimethyl sulfate) in the zinc finger contacts of the ICR-TFIIIA complex. Furthermore CTDs at +55 and +72 were more efficiently removed from the complex than CTDs at other sites in the ICR by Xenopus oocyte nuclear extracts. This suggests that repair of CTDs closely correlates with changes in the binding of individual zinc fingers of the ICR-TFIIIA complex. These results have implications for the mechanism of DNA damage recognition and repair in protein-DNA complexes.

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Title: Binding of zinc finger protein transcription factor IIIA to its cognate DNA sequence with single UV photoproducts at specific sites and its effect on DNA repair
Creators: YoungHo Kwon - Biochemistry and Biophysics, School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660, USA
Michael J Smerdon
Publication Details: The Journal of biological chemistry, Vol.278(46), pp.45451-45459
Academic Unit: Molecular Biosciences, School of
Publisher: United States
Grant note: ES02614 / NIEHS NIH HHS
Identifiers: 99900546878901842
Language: English
Resource Type: Journal article