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C-terminal domain of S. pombe RAP1 protein The Schizosaccharomyces pombe RAP1 (repressor activator protein 1) protein C-terminal (RCT) domain structurally resembles the first 3-helix bundle found in yeast and human RAP1 RCT. S. pombe RAP1 (spRap1), like human RAP1, lacks direct DNA-binding activity and is localized to telomeres via Taz1, an ortholog of TRF1 and TRF2. The RAP1 RCT domain interacts with RAP1 binding motif (RBM) of TAZ1. RAP1, identified in budding yeast as repressor/activator protein 1 is a well-conserved telomere binding protein, found in budding yeast, 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 binding at numerous sites at each telomere, where it functions in telomere length regulation, telomeric position effect gene silencing and telomere end protection. Human RAP1 does not bind telomeric DNA directly, but binds telomere repeat binding factor 2 (TRF2) via the RAP C-terminal domain (RCT). Yeast RAP1 has 2 myb-type DNA binding modules, a BRCT domain, and a RCT domain that recruits Sir3 and Sir4 for gene silencing and Rif1 and Rif2 for telomere length maintenance. S. pombe RAP1 has a BRCT domain, 2 myb like domains, and the RCT. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",