期刊
NUCLEIC ACIDS RESEARCH
卷 42, 期 5, 页码 2893-2905出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkt1261
关键词
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资金
- The University of Michigan Cancer Center and GI Peptide Research Center
- Department of Defense
- National Institute of Health [CA132755, CA130899]
- NIH [R01CA130899]
Ten-eleven translocation (TET) family enzymes convert 5-methylcytosine to 5-hydroxylmethylcytosine. However, the molecular mechanism that regulates this biological process is not clear. Here, we show the evidence that PGC7 (also known as Dppa3 or Stella) interacts with TET2 and TET3 both in vitro and in vivo to suppress the enzymatic activity of TET2 and TET3. Moreover, lacking PGC7 induces the loss of DNA methylation at imprinting loci. Genome-wide analysis of PGC7 reveals a consensus DNA motif that is recognized by PGC7. The CpG islands surrounding the PGC7-binding motifs are hypermethylated. Taken together, our study demonstrates a molecular mechanism by which PGC7 protects DNA methylation from TET family enzyme-dependent oxidation.
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