PERFORM Publications

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Title		Authors	PubMed ID
1	O4-alkyl-2'-deoxythymidine cross-linked DNA to probe recognition and repair by O6-alkylguanine DNA alkyltransferases.	McManus FP, O'Flaherty DK, Noronha AM, Wilds CJ	22850722 CHEMBIOCHEM
2	Backbone Flexibility Influences Nucleotide Incorporation by Human Translesion DNA Polymerase η opposite Intrastrand Cross-Linked DNA.	O'Flaherty DK, Guengerich FP, Egli M, Wilds CJ	26624500 CHEMBIOCHEM
3	O(6)-Alkylguanine DNA Alkyltransferase Repair Activity Towards Intrastrand Cross-Linked DNA is Influenced by the Internucleotide Linkage.	O'Flaherty DK, Wilds CJ	26692563 CHEMISTRY
4	Lesion Orientation of O4-Alkylthymidine Influences Replication by Human DNA Polymerase η.	O'Flaherty DK, Patra A, Su Y, Guengerich FP, Egli M, Wilds CJ	27574558 CHEMBIOCHEM
5	Preparation of Intrastrand {G}O(6) -Alkylene-O(6) {G} Cross-Linked Oligonucleotides.	O'Flaherty DK, Wilds CJ	27584704 CHEMBIOCHEM
6	O6-2'-Deoxyguanosine-butylene-O6-2'-deoxyguanosine DNA Interstrand Cross-Links Are Replication-Blocking and Mutagenic DNA Lesions.	Xu W, Kool D, O'Flaherty DK, Keating AM, Sacre L, Egli M, Noronha A, Wilds CJ, Zhao L	27768841 CHEMBIOCHEM
7	Site-specific covalent capture of human O6-alkylguanine-DNA-alkyltransferase using single-stranded intrastrand cross-linked DNA.	O'Flaherty DK, Wilds CJ	27886318 CHEMBIOCHEM
8	Structural basis of interstrand cross-link repair by O6-alkylguanine DNA alkyltransferase.	Denisov AY, McManus FP, O'Flaherty DK, Noronha AM, Wilds CJ	28937154 CHEMBIOCHEM
9	AGT Activity Towards Intrastrand Crosslinked DNA is Modulated by the Alkylene Linker.	O'Flaherty DK, Wilds CJ	28980757 CHEMBIOCHEM
10	Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein.	Schoonhoven NM, O'Flaherty DK, McManus FP, Sacre L, Noronha AM, Kornblatt MJ, Wilds CJ	29137116 CHEMBIOCHEM
11	Covalent capture of OGT's active site using engineered human-E. coli chimera and intrastrand DNA cross-links.	Copp W, O'Flaherty DK, Wilds CJ	30430154 CHEMBIOCHEM

Title:	Backbone Flexibility Influences Nucleotide Incorporation by Human Translesion DNA Polymerase η opposite Intrastrand Cross-Linked DNA.
Authors:	O'Flaherty DK, Guengerich FP, Egli M, Wilds CJ
Link:	https://www.ncbi.nlm.nih.gov/pubmed/26624500?dopt=Abstract
DOI:	10.1021/acs.biochem.5b01078
Publication:	Biochemistry
Keywords:
PMID:	26624500	Category:	Biochemistry	Date Added:	2019-06-20
Dept Affiliation:	CHEMBIOCHEM 1 Department of Chemistry and Biochemistry, Concordia University , 7141 Sherbrooke Street West, Montréal, Québec, Canada H4B 1R6. 2 Department of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine , Nashville, Tennessee 37232-0146, United States.

Description:

Backbone Flexibility Influences Nucleotide Incorporation by Human Translesion DNA Polymerase ? opposite Intrastrand Cross-Linked DNA.

Biochemistry. 2015 Dec 29;54(51):7449-56

Authors: O'Flaherty DK, Guengerich FP, Egli M, Wilds CJ

Abstract

Intrastrand cross-links (IaCL) connecting two purine nucleobases in DNA pose a challenge to high-fidelity replication in the cell. Various repair pathways or polymerase bypass can cope with these lesions. The influence of the phosphodiester linkage between two neighboring 2'-deoxyguanosine (dG) residues attached through the O(6) atoms by an alkylene linker on bypass with human DNA polymerase ? (hPol ?) was explored in vitro. Steady-state kinetics and mass spectrometric analysis of products from nucleotide incorporation revealed that although hPol ? is capable of bypassing the 3'-dG in a mostly error-free fashion, significant misinsertion was observed for the 5'-dG of the IaCL containing a butylene or heptylene linker. The lack of the phosphodiester linkage triggered an important increase in frameshift adduct formation across the 5'-dG by hPol ?, in comparison to the 5'-dG of IaCL DNA containing the phosphodiester group.

PMID: 26624500 [PubMed - indexed for MEDLINE]

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