The DNA Polymerase Gamma R953C Mutant Is Associated with Antiretroviral Therapy-Induced Mitochondrial Toxicity | Zendy

Min Li | Zendy; Andrea C. Mislak | Zendy; Yram Foli | Zendy; Esinam Agbosu | Zendy; Vivek Bose | Zendy; Shreya Bhandari | Zendy; Michał R. Szymański | Zendy; Christie K. Shumate | Zendy; Y. Whitney Yin | Zendy; Karen S. Anderson | Zendy; Elijah Paintsil | Zendy

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The DNA Polymerase Gamma R953C Mutant Is Associated with Antiretroviral Therapy-Induced Mitochondrial Toxicity

Author(s) -

Min Li,

Andrea C. Mislak,

Yram Foli,

Esinam Agbosu,

Vivek Bose,

Shreya Bhandari,

Michał R. Szymański,

Christie K. Shumate,

Y. Whitney Yin,

Karen S. Anderson,

Elijah Paintsil

Publication year - 2016

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.00976-16

Subject(s) - polymerase , mutant , microbiology and biotechnology , dna polymerase , mitochondrial dna , biology , mitochondrial toxicity , nucleotide , nucleotidyltransferase , wild type , dna , biochemistry , mitochondrion , rna , gene

We found a heterozygous C2857T mutation (R953C) in polymerase gamma (Pol-γ) in an HIV-infected patient with mitochondrial toxicity. The R953C Pol-γ mutant binding affinity for dCTP is 8-fold less than that of the wild type. The R953C mutant shows a 4-fold decrease in discrimination of analog nucleotides relative to the wild type. R953 is located on the "O-helix" that forms the substrate deoxynucleoside triphosphate (dNTP) binding site; the interactions of R953 with E1056 and Y986 may stabilize the O-helix and affect polymerase activity.

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