Revision as of 12:43, 28 September 2023

ATRIP (human)

To further design a system that can detect DNA breaks in vivo, we proposed a FRET (Förster resonance energy transfer) system using the interaction between ATRIP and RPA1. The ATR (ATMand Rad3-related) and ATRIP (ATR-Interacting protein) form a complex under the circumstances of DNA damage (Qinhui Rao et. al., 2017) (Nam, E. A., & Cortez, D., 2011). Due to the double-strand breaks (DSBs), replication protein A (RPA) will bind to the single-stranded DNA (ssDNA) and recruit ATRIP complex. An earlier research (Zou, L., & Elledge, S. J., 2003) demonstrated that the RPA-ssDNA-ATRIP interaction is important in checkpoint signaling. To be specific, the RPA70 (RPA1) N-terminus interacts with the ATRIP N-termius (Ball, H. L., Myers, J. S., & Cortez, D., 2005).

References:

Qinhui Rao et. al. (2017). Cryo-EM structure of human ATR-ATRIP complex. Cell Research (2017) :1-1.

Nam, E. A., & Cortez, D. (2011). ATR signalling: more than meeting at the fork. The Biochemical journal, 436(3), 527–536. https://doi.org/10.1042/BJ20102162

Ball, H. L., Myers, J. S., & Cortez, D. (2005). ATRIP binding to replication protein A-single-stranded DNA promotes ATR-ATRIP localization but is dispensable for Chk1 phosphorylation. Molecular biology of the cell, 16(5), 2372–2381. https://doi.org/10.1091/mbc.e04-11-1006

Zou, L., & Elledge, S. J. (2003). Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes. Science (New York, N.Y.), 300(5625), 1542–1548. https://doi.org/10.1126/science.1083430

Sequence derived from: https://www.uniprot.org/uniprotkb/Q8WXE1/entry https://www.ncbi.nlm.nih.gov/gene/84126