Structural highlights
Function
RFA3_TETTS Component of the heterotrimeric replication protein A (RPA) and holoenzyme telomerase ribonucleoprotein complexes (PubMed:26472759, PubMed:27895115). As part of the heterotrimeric RPA complex, binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress (By similarity). It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism (By similarity). Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (By similarity). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation (By similarity). Also part of a subcomplex of the holoenzyme telomerase ribonucleoprotein complex: this subcomplex that contains TEB1, RPA2/TEB2, RPA3/TEB3, but not RPA1, mediates the recruitment of telomerase to telomeric DNA via specific interaction between TEB1 and telomeric ssDNA (PubMed:27895115). In the holoenzyme telomerase ribonucleoprotein complex, RPA2/TEB2 and RPA3/TEB3 act as assembly factors for TEB1 incorporation into telomerase holoenzyme (PubMed:27895115). In the holoenzyme telomerase ribonucleoprotein complex, RPA3/TEB3 does not contribute to ssDNA affinity, while it contributes to ssDNA affinity in the RPA complex (PubMed:27895115).[UniProtKB:P35244][1] [2]
See Also
References
- ↑ Jiang J, Chan H, Cash DD, Miracco EJ, Ogorzalek Loo RR, Upton HE, Cascio D, O'Brien Johnson R, Collins K, Loo JA, Zhou ZH, Feigon J. Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions. Science. 2015 Oct 30;350(6260):aab4070. doi: 10.1126/science.aab4070. Epub 2015, Oct 15. PMID:26472759 doi:http://dx.doi.org/10.1126/science.aab4070
- ↑ Upton HE, Chan H, Feigon J, Collins K. Shared Subunits of Tetrahymena Telomerase Holoenzyme and Replication Protein A Have Different Functions in Different Cellular Complexes. J Biol Chem. 2017 Jan 6;292(1):217-228. PMID:27895115 doi:10.1074/jbc.M116.763664