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:	Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein.
Authors:	Schoonhoven NM, O'Flaherty DK, McManus FP, Sacre L, Noronha AM, Kornblatt MJ, Wilds CJ
Link:	https://www.ncbi.nlm.nih.gov/pubmed/29137116?dopt=Abstract
Publication:
Keywords:
PMID:	29137116	Category:	Molecules	Date Added:	2019-05-31
Dept Affiliation:	CHEMBIOCHEM 1 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. nadiaschoonhoven@hotmail.com. 2 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. derek_oflaherty@hotmail.com. 3 Howard Hughes Medical Institute, Department of Molecular Biology and Center for Computational and Integrative Biology, Massachusetts General Hospital, Boston, MA 02114, USA. derek_oflaherty@hotmail.com. 4 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. shent13@hotmail.com. 5 Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, QC H3T 1J4, Canada. shent13@hotmail.com. 6 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. dlsacre@hotmail.com. 7 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. anne.noronha@concordia.ca. 8 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. Judith.Kornblatt@concordia.ca. 9 Department of Chemistry and Biochemistry, Concordia University, Montréal, QC H4B 1R6, Canada. Chris.Wilds@concordia.ca.

Description:

Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein.

Molecules. 2017 Nov 11;22(11):

Authors: Schoonhoven NM, O'Flaherty DK, McManus FP, Sacre L, Noronha AM, Kornblatt MJ, Wilds CJ

Abstract

O6-Alkylguanine-DNA alkyltransferases (AGTs) are proteins responsible for the removal of mutagenic alkyl adducts at the O6-atom of guanine and O4-atom of thymine. In the current study we set out to understand the role of the Ser134 residue in the Escherichia coli AGT variant OGT on substrate discrimination. The S134P mutation in OGT increased the ability of the protein to repair both O6-adducts of guanine and O4-adducts of thymine. However, the S134P variant was unable, like wild-type OGT, to repair an interstrand cross-link (ICL) bridging two O6-atoms of guanine in a DNA duplex. When compared to the human AGT protein (hAGT), the S134P OGT variant displayed reduced activity towards O6-alkylation but a much broader substrate range for O4-alkylation damage reversal. The role of residue 134 in OGT is similar to its function in the human homolog, where Pro140 is crucial in conferring on hAGT the capability to repair large adducts at the O6-position of guanine. Finally, a method to generate a covalent conjugate between hAGT and a model nucleoside using a single-stranded oligonucleotide substrate is demonstrated.

PMID: 29137116 [PubMed - indexed for MEDLINE]

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