The activity of yeast Apn2 AP endonuclease at uracil-derived AP sites is dependent on the major carbon source

Yeast Apn2 is an AP endonuclease and DNA 3′-diesterase that belongs to the Exo III family with homology to the E. coli exonuclease III, Schizosaccharomyces pombe eth1, and human AP endonucleases APEX1 and APEX2. In the absence of Apn1, the major AP endonuclease in yeast, Apn2 can cleave the DNA back...

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Bibliographic Details
Published in:	Current genetics Vol. 67; no. 2; pp. 283 - 294
Main Authors:	Stokdyk, Kasey, Berroyer, Alexandra, Grami, Zacharia A., Kim, Nayun
Format:	Journal Article
Language:	English
Published:	Berlin/Heidelberg Springer Berlin Heidelberg 01-04-2021 Springer Nature B.V
Subjects:	AP endonuclease Base excision repair Biochemistry Biomedical and Life Sciences Carbon Carbon sources Catabolite repression Cell Biology Deoxyribonucleic acid Disruption DNA E coli Endonuclease Exonuclease Gene deletion Glucose Homology Life Sciences Microbial Genetics and Genomics Microbiology Mutation Original Article Plant Sciences Proteomics Repair Residues Transversion Uracil Yeast Yeasts Glucose repression AP endonuclease DNA repair Uracil in DNA
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Summary:	Yeast Apn2 is an AP endonuclease and DNA 3′-diesterase that belongs to the Exo III family with homology to the E. coli exonuclease III, Schizosaccharomyces pombe eth1, and human AP endonucleases APEX1 and APEX2. In the absence of Apn1, the major AP endonuclease in yeast, Apn2 can cleave the DNA backbone at an AP lesion initiating the base excision repair pathway. To study the role and relative contribution of Apn2, we took advantage of a reporter system that was previously used to delineate how uracil-derived AP sites are repaired. At this reporter, disruption of the Apn1-initiated base excision repair pathway led to a significant elevation of A:T to C:G transversions. Here we show that such highly elevated A:T to C:G transversion mutations associated with uracil residues in DNA are abolished when apn1∆ yeast cells are grown in glucose as the primary carbon source. We also show that the disruption of Apn2, either by the complete gene deletion or by the mutation of a catalytic residue, results in a similarly reduced rate of the uracil-associated mutations. Overall, our results indicate that Apn2 activity is regulated by the glucose repression pathway in yeast.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0172-8083 1432-0983
DOI:	10.1007/s00294-020-01141-4