Keyword search (4,163 papers available)

"Noronha AM" Authored Publications:

Title Authors PubMed ID
1 Enhanced binding of guanylated poly(A) RNA by the LaM domain of LARP1 Kozlov G; Jiang J; Rutherford T; Noronha AM; Wilds CJ; Gehring K; 39016322
CHEMBIOCHEM
2 Structural basis of 3'-end poly(A) RNA recognition by LARP1 Kozlov G; Mattijssen S; Jiang J; Nyandwi S; Sprules T; Iben JR; Coon SL; Gaidamakov S; Noronha AM; Wilds CJ; Maraia RJ; Gehring K; 35979957
CHEMBIOCHEM
3 Hydrated electrons induce the formation of interstrand cross-links in DNA modified by cisplatin adducts Behmand B; Noronha AM; Wilds CJ; Marignier JL; Mostafavi M; Wagner JR; Hunting DJ; Sanche L; 32211848
CHEMBIOCHEM
4 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
5 Preparation of covalently linked complexes between DNA and O(6)-alkylguanine-DNA alkyltransferase using interstrand cross-linked DNA. McManus FP, Khaira A, Noronha AM, Wilds CJ 23347328
CHEMBIOCHEM
6 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
7 Influence of nucleotide modifications at the C2' position on the Hoogsteen base-paired parallel-stranded duplex of poly(A) RNA. Copp W, Denisov AY, Xie J, Noronha AM, Liczner C, Safaee N, Wilds CJ, Gehring K 28973475
CHEMBIOCHEM
8 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

 

Title:Structural basis of interstrand cross-link repair by O6-alkylguanine DNA alkyltransferase.
Authors:Denisov AY,  McManus FP,  O'Flaherty DK,  Noronha AM,  Wilds CJ
Link:https://www.ncbi.nlm.nih.gov/pubmed/28937154?dopt=Abstract
Publication:
Keywords:
PMID:28937154 Category:Org Biomol Chem Date Added:2019-05-31
Dept Affiliation: CHEMBIOCHEM
1 Department of Chemistry and Biochemistry, Concordia University, 7141 Sherbrooke Street West, Montréal, Québec, Canada. chris.wilds@concordia.ca.

Description:

Structural basis of interstrand cross-link repair by O6-alkylguanine DNA alkyltransferase.

Org Biomol Chem. 2017 Oct 11;15(39):8361-8370

Authors: Denisov AY, McManus FP, O'Flaherty DK, Noronha AM, Wilds CJ

Abstract

DNA interstrand cross-links (ICL) are among the most cytotoxic lesions found in biological systems. O6-Alkylguanine DNA alkyltransferases (AGTs) are capable of removing alkylation damage from the O6-atom of 2'-deoxyguanosine and the O4-atom of thymidine. Human AGT (hAGT) has demonstrated the ability to repair an interstrand cross-linked duplex where two O6-atoms of 2'-deoxyguanosine were tethered by a butylene (XLGG4) or heptylene (XLGG7) linkage. However, the analogous ICL between the O4-atoms of thymidine was found to evade repair. ICL duplexes connecting the O4-atoms of 2'-deoxyuridine by a butylene (XLUU4) or heptylene (XLUU7) linkage have been prepared to examine the influence of the C5-methyl group on AGT-mediated repair. Both XLUU4 and XLUU7 were refractory to repair by human and E. coli (OGT and Ada-C) AGTs with comparably low µM dissociation constants for 2?:?1 or 4?:?1 AGT/DNA stoichiometries. The solution structures of two heptylene linked DNA duplexes (CGAAAYTTTCG)2, XLUU7 (Y = dU) and XLGG7 (Y = dG), were solved and the global structures were virtually identical with a RMSD of 1.22 Å. The ICL was found to reside in the major groove for both duplexes. The linkage adopts an E conformation about the C4-O4 bond for XLUU7 whereas a Z conformation about the C6-O6 bond was observed for XLGG7. This E versus Z conformation may partially account for hAGTs discrimination towards the repair of these ICL, supported by the crystal structures of hAGT with various substrates which have been observed to adopt a Z conformation. In addition, a higher mobility at the ICL site for XLUU7 is observed relative to XLGG7 that may play a role in repair by hAGT. Taken together, these findings provide insights on the AGT-mediated repair of cytotoxic ICL in terms of its processing capability and substrate specificity.

PMID: 28937154 [PubMed - indexed for MEDLINE]




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