An investigation of the role of adenine phosphoribosyltransferase for excision repair following UV irradiation in Friend cells

1997 ◽  
Vol 25 (1) ◽  
pp. 149S-149S
Author(s):  
AILEEN A. NELSON ◽  
PATRICK G. MCKENNA ◽  
YVONNE A. BARNETT
DNA Repair ◽  
2010 ◽  
Vol 9 (1) ◽  
pp. 96-100 ◽  
Author(s):  
Erich Heidenreich ◽  
Herfried Eisler ◽  
Theresia Lengheimer ◽  
Petra Dorninger ◽  
Ferdinand Steinboeck

Genetics ◽  
1977 ◽  
Vol 87 (1) ◽  
pp. 1-18
Author(s):  
Takesi Kato ◽  
Robert H Rothman ◽  
Alvin J Clark

ABSTRACT Multiple mutant strains have been tested for their mimicry of the UV-mutagenesis deficiency of a recA single mutant. Revertants to histidine prototrophy and clear plaque mutants of lambda were scored to determine capacity for UV-mutagenesis. Nearly normal capacity was shown by a uvr  +  recB  -  recF  - strain, which shows almost no recA-dependent recombination, by uvr  -  recB  +  recF  - strains, which show almost no recA-dependent repair and by a uvrA  -  recB  -  recF  - strain, which shows neither recA-dependent recombination nor repair. Since the uvr mutants can be assumed to show additionally no excision repair, these results may mean that UV-mutagenesis occurs during processes other than recombination and repair. Alternative hypotheses are discussed. The slight difference in mutagenic capacity was traced to the recF single mutation, which blocks the production of unmixed bursts of clear-plaque lambda mutants. Since this accounts for only about 10% of the mutations leading to clear-plaque mutants, it is suggested that there is more than one UV-mutagenic process.


1999 ◽  
Vol 27 (16) ◽  
pp. 3276-3282 ◽  
Author(s):  
P. P. H. Van Sloun ◽  
J. G. Jansen ◽  
G. Weeda ◽  
L. H. F. Mullenders ◽  
A. A. van Zeeland ◽  
...  

Author(s):  
Lars Mohrhusen ◽  
Jessica Kräuter ◽  
Katharina Al-Shamery

The photochemical conversion of organic compounds on tailored transition metal oxide surfaces by (UV) irradiation has found wide applications ranging from the production of chemicals to the degradation of organic...


2019 ◽  
Vol 26 (8) ◽  
pp. 695-703 ◽  
Author(s):  
Sunbok Jang ◽  
Namrata Kumar ◽  
Emily C. Beckwitt ◽  
Muwen Kong ◽  
Elise Fouquerel ◽  
...  

2014 ◽  
Vol 70 (a1) ◽  
pp. C832-C832
Author(s):  
Menico Rizzi ◽  
Riccardo Miggiano ◽  
Samarpita Lahiri ◽  
Giuseppe Perugino ◽  
Maria Ciaramella ◽  
...  

Mycobacterium tuberculosis (MTB) is an extremely well adapted human pathogen capable to survive for decades inside the hostile environment represented by the host's infected macrophages despite exposure to multiple potential DNA-damaging stresses. In order to maintain a remarkable low level of genetic diversity, MTB deploys different strategies of DNA repair, including multi-enzymatic systems, such as Nucleotide Excision Repair, and single-step repair. In particular, to counteract the mutagenic effects of DNA alkylation, MTB performs the direct alkylated-base reversal by sacrificing one molecule of a DNA-protein alkyltransferase, such as O6-methylguanine methyltransferase (OGT; orf: Rv1316c). We present here the biochemical and structural characterization of recombinant mycobacterial OGT (MtOGT) in its wild-type form along with its mutated variants mimicking the ones occurring in relevant clinical strains (i.e. MtOGT-T15S and MtOGT-R37L). Our studies reveal that MtOGT-R37L is severely impaired in its activity as consequence of its ten-fold lower affinity for modified double-stranded DNA (dsDNA) (1). Further investigations on a new structure-based panel of OGT versions, designed to explore different molecular environment at position 37, allowed us a better understanding of the functional role of the MtOGT Arg37-bearing loop during catalysis. Moreover, we solved the crystal structure of MtOGT in covalent complex with modified dsDNA that reveals an unprecedented MtOGT::DNA architecture, suggesting that the MtOGT monomer performing the catalysis needs assisting unreacted subunits during cooperative DNA binding. This work is supported by European Community FP7 program SYSTEMTB (Health-F4-2010-241587)


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