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RAP1 binding motif of Schizosaccharomyces pombe TAZ1 S. pombe TAZ1 recruits the spRAP1 protein to telomeres. The TAZ1 RAP1-binding motif (RBM) binds the RAP1 C-terminal domain (RCT), which structurally resembles the first 3-helix bundle found in yeast and human RAP1 RCT. TAZ1, an ortholog of TRF1 and TRF2, has a TRF homology (TRFH) domain, the RBM domain, a dimerization domain, and a myb-like C-terminus. RAP1, identified in budding yeast as repressor/activator protein 1, is a well-conserved telomere binding protein and is also found in fission yeast and mammals. In Saccharomyces cerevisiae, RAP1 directly binds DNA and is involved in transcriptional activation and mating type information gene silencing, as well as in binding to numerous binding sites at each telomere, where it functions in telomere length regulation, telomeric position effect gene silencing, and telomere end protection. Like S. pombe RAP1, human RAP1 does not bind telomeric DNA directly, but binds telomere repeat binding factor 2 (TRF2) through the RAP C-terminal domain (RCT). |
Jiyao W et al.(2023). "The conserved domain database in 2023.",