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Nabeel-Shah S, Garg J, Saettone A, Ashraf K, Lee H, Wahab S, Ahmed N, Fine J, Derynck J, Pu S, Ponce M, Marcon E, Zhang Z, Greenblatt JF, Pearlman RE, Lambert JP, Fillingham J (2021) Functional characterization of RebL1 highlights the evolutionary conservation of oncogenic activities of the RBBP4/7 orthologue in Tetrahymena thermophila. Nucleic acids research ( ): PUBMED:34086947
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Identifiers and Description
Gene Model Identifier
TTHERM_01243450
Standard Name
OGL1 (OGG1-Like)
Aliases
PreTt01756 | 287.m00027
Description
OGL1 HhH-GPD family base excision DNA repair protein; HhH-GPD superfamily base excision DNA repair protein
Genome Browser (Macronucleus)
Genome Browser (Micronucleus)
Gene Ontology Annotations
Molecular Function
oxidized purine nucleobase lesion DNA N-glycosylase activity (IEA) | GO:0008534
OGG1 Mitochondrial glycosylase
/lyase that specifically excis
es 7,8-dihydro-8-oxoguanine re
sidues located opposite cytosi
ne or thymine residues in DNA,
repairs oxidative damage to m
itochondrial DNA, contributes
to UVA resistance
Tetrahymena thermophila’s OGL1 protein is homologous to proteins from the HhH-GPD and OGG-N superfamilies, which are associated with DNA repair. It contains two domains; the first domain (E-value= 3.0 -17), in the HhH-GPD family, is a Helix-hairpin-helix and Gly/Pro rich loop, found on proteins that remove base lesions. The second domain (E-value=6.9-13), is common to oxoguanine gylcosylases, also known as OGG1, which removes 8-oxoG lesions. The closest homologs are in Scheffersomyces stipitis, a negative Crabtree yeast, and in Taphrina deformans, a fungi/plant pathogen, with 46% identical residues. OGL1 may be an essential protein in preventing mutations in DNA that lead to a short lifespan, early aging, and cancer.
Paragraph by: Lillian Horin, Maite Cortes Garcia, Francis Ryu, Forrest Fulgenzi, Keck Science Center, Pitzer College