期刊
NUCLEIC ACIDS RESEARCH
卷 37, 期 2, 页码 568-581出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkn974
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资金
- The European Union FP6 Proteomage
- MRC Career Development Fellowship
- Medical Research Council UK
- Medical Research Council [MC_U105474168] Funding Source: researchfish
- MRC [MC_U105474168] Funding Source: UKRI
Single-stranded DNA-binding proteins (SSB) form a class of proteins that bind preferentially single-stranded DNA with high affinity. They are involved in DNA metabolism in all organisms and serve a vital role in replication, recombination and repair of DNA. In this report, we identify human mitochondrial SSB (HmtSSB) as a novel protein-binding partner of tumour suppressor p53, in mitochondria. It binds to the transactivation domain (residues 161) of p53 via an extended binding interface, with dissociation constant of 12.7 ( 0.7) M. Unlike most binding partners reported to date, HmtSSB interacts with both TAD1 (residues 140) and TAD2 (residues 4161) subdomains of p53. HmtSSB enhances intrinsic 3-5 exonuclease activity of p53, particularly in hydrolysing 8-oxo-7,8-dihydro-2-deoxyguanosine (8-oxodG) present at 3-end of DNA. Taken together, our data suggest that p53 is involved in DNA repair within mitochondria during oxidative stress. In addition, we characterize HmtSSB binding to ssDNA and p53 N-terminal domain using various biophysical measurements and we propose binding models for both.
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