scholarly journals Dispensability of the [4Fe-4S] cluster in novel homologues of adenine glycosylase MutY

FEBS Journal ◽  
2016 ◽  
Vol 283 (3) ◽  
pp. 521-540 ◽  
Author(s):  
Carlos H. Trasviña-Arenas ◽  
Laura M. Lopez-Castillo ◽  
Eugenia Sanchez-Sandoval ◽  
Luis G. Brieba
Keyword(s):  
Adenine Glycosylase

Adenine Glycosylase MutY of Corynebacterium pseudotuberculosis presents the antimutator phenotype and evidences of glycosylase/AP lyase activity in vitro

2016 ◽  
Vol 44 ◽  
pp. 318-329 ◽  
Author(s):  
Rafael Cançado de Faria ◽  
Liliane Gonçalves Vila-Nova ◽  
Mainá Bitar ◽  
Bruno Carvalho Resende ◽  
Larissa Sousa Arantes ◽  
...  
Keyword(s):  
Corynebacterium Pseudotuberculosis ◽  
Lyase Activity ◽  
Ap Lyase ◽  
Adenine Glycosylase

scholarly journals Protection of pulmonary epithelial cells from oxidative stress by hMYH adenine glycosylase

2004 ◽  
Vol 5 (1) ◽  
Author(s):  
Ted M Kremer ◽  
Mikael L Rinne ◽  
Yi Xu ◽  
Xian Ming Chen ◽  
Mark R Kelley
Keyword(s):  
Oxidative Stress ◽  
Epithelial Cells ◽  
Pulmonary Epithelial Cells ◽  
Adenine Glycosylase

scholarly journals Molecular Cloning and Functional Analysis of the MutY Homolog of Deinococcus radiodurans

2001 ◽  
Vol 183 (21) ◽  
pp. 6151-6158 ◽  
Author(s):  
Xianghong Li ◽  
A-Lien Lu
Keyword(s):  
Oxidative Stress ◽  
Mutation Frequency ◽  
Deinococcus Radiodurans ◽  
Binding Affinities ◽  
Dna Complexes ◽  
E Coli ◽  
Binding Preference ◽  
Lyase Activity ◽  
Adenine Glycosylase ◽  
And Oxidative Stress

ABSTRACT The mutY homolog gene (mutY Dr) from Deinococcus radiodurans encodes a 39.4-kDa protein consisting of 363 amino acids that displays 35% identity to the Escherichia coli MutY (MutYEc) protein. Expressed MutYDr is able to complement E. coli mutYmutants but not mutM mutants to reduce the mutation frequency. The glycosylase and binding activities of MutYDr with an A/G-containing substrate are more sensitive to high salt and EDTA concentrations than the activities with an A/7,8-dihydro-8-oxoguanine (GO)-containing substrate are. Like the MutYEc protein, purified recombinant MutYDrexpressed in E. coli has adenine glycosylase activity with A/G, A/C, and A/GO mismatches and weak guanine glycosylase activity with a G/GO mismatch. However, MutYDrexhibits limited apurinic/apyrimidinic lyase activity and can form only weak covalent protein-DNA complexes in the presence of sodium borohydride. This may be due to an arginine residue that is present in MutYDr at the position corresponding to the position of MutYEc Lys142, which forms the Schiff base with DNA. The kinetic parameters of MutYDr are similar to those of MutYEc. Although MutYDr has similar substrate specificity and a binding preference for an A/GO mismatch over an A/G mismatch, as MutYEc does, the binding affinities for both mismatches are slightly lower for MutYDr than for MutYEc. Thus, MutYDr can protect the cell from GO mutational effects caused by ionizing radiation and oxidative stress.

scholarly journals MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III

1990 ◽  
Vol 18 (13) ◽  
pp. 3841-3845 ◽  
Author(s):  
Mark Leo Michaels ◽  
Lucie Pham ◽  
Ylan Nghiem ◽  
Christina Cruz ◽  
Jeffrey H. Miller
Keyword(s):  
Endonuclease Iii ◽  
Adenine Glycosylase
Sign in / Sign up

Export Citation Format

Share Document