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Resources and Methods for Engineering "Designer" Glycan-Binding Proteins.

Author(s): Warkentin R, Kwan DH

This review provides information on available methods for engineering glycan-binding proteins (GBP). Glycans are involved in a variety of physiological functions and are found in all domains of life and viruses. Due to their wide range of functions, GBPs ha...

Article GUID: 33450899
Cyst Reduction by Melatonin in a Novel Drosophila Model of Polycystic Kidney Disease.

Author(s): Millet-Boureima C; Rozencwaig R; Polyak F; Gamberi C;

Autosomal dominant polycystic kidney disease (ADPKD) causes progressive cystic degeneration of the renal tubules, the nephrons, eventually severely compromising kidney function. ADPKD is incurable, with half of the patients eventually needing renal replacem...

Article GUID: 33238462
Gold Nano-Island Platforms for Localized Surface Plasmon Resonance Sensing: A Short Review.

Author(s): Badilescu S, Raju D, Bathini S, Packirisamy M

Nano-islands are entities (droplets or other shapes) that are formed by spontaneous dewetting (agglomeration, in the early literature) of thin and very thin metallic (especially gold) films on a substrate, done by post-deposition heating or by using other s...

Article GUID: 33066088
Angiotensin-I-Converting Enzyme Inhibitory Activity of Coumarins from Angelica decursiva.

Author(s): Ali MY, Seong SH, Jung HA, Choi JS

Molecules. 2019 Oct 31;24(21): Authors: Ali MY, Seong SH, Jung HA, Choi JS

Article GUID: 31683604
Pyrrole and Fused Pyrrole Compounds with Bioactivity against Inflammatory Mediators.

Author(s): Said Fatahala S, Hasabelnaby S, Goudah A, Mahmoud GI, Helmy Abd-El Hameed R

Molecules. 2017 Mar 17;22(3): Authors: Said Fatahala S, Hasabelnaby S, Goudah A, Mahmoud GI, Helmy Abd-El Hameed R

Article GUID: 28304349
Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein.

Author(s): Schoonhoven NM, O'Flaherty DK, McManus FP, Sacre L, Noronha AM, Kornblatt MJ, Wilds CJ

Molecules. 2017 Nov 11;22(11): Authors: Schoonhoven NM, O'Flaherty DK, McManus FP, Sacre L, Noronha AM, Kornblatt MJ, Wilds CJ

Article GUID: 29137116
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
Category:Molecules
PMID:29137116
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]