Coding

Part:BBa_K4814005

Designed by: CHIEN-YUEH LIU   Group: iGEM23_PuiChing-Macau   (2023-09-28)
Revision as of 13:04, 28 September 2023 by Ginaliu (Talk | contribs)

RPA1 (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.

Due to the double-strand breaks (DSBs), replication protein A (RPA) will bind to the single-stranded DNA (ssDNA) and recruit ATRIP complex. The RPA70 (RPA1) N-terminus interacts with the ATRIP. (Bhat, K.P. and Cortez, D, 2018) (Maréchal, A. and Zou, L., 2015)

Dueva, R., & Iliakis, G. (2020) stated that ATRIP is one of the prominent RPA-interacting partners, playing a crucial role in the repair mechanism of DNA repairing and DNA damage checkpoints (Zou, Y., Liu, Y., Wu, X., & Shell, S. M., 2006). Moreover, the N-terminus of RPA1 (RPA70) is shown to be binding to the ATRIP protein (Xu, X., et al, 2008). Considering the protein size, we did not use the entire RPA, instead, we chose RPA1, the interacting domain, to design the FRET system.

References:

Bhat, K.P., & Cortez, D. (2018). RPA and RAD51: fork reversal, fork protection, and genome stability. Nature Structural & Molecular Biology, 25(6), 446-453. https://doi.org/10.1038/s41594-018-0075-z

Maréchal, A., & Zou, L. (2015). RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage response. Cell Research, 25(1), 9-23. https://doi.org/10.1038/cr.2014.147

Dueva, R., & Iliakis, G. (2020). Replication protein A: a multifunctional protein with roles in DNA replication, repair and beyond. NAR cancer, 2(3), zcaa022. https://doi.org/10.1093/narcan/zcaa022

Zou, Y., Liu, Y., Wu, X., & Shell, S. M. (2006). Functions of human replication protein A (RPA): from DNA replication to DNA damage and stress responses. Journal of cellular physiology, 208(2), 267–273. https://doi.org/10.1002/jcp.20622

Xu, X., Vaithiyalingam, S., Glick, G. G., Mordes, D. A., Chazin, W. J., & Cortez, D. (2008). The basic cleft of RPA70N binds multiple checkpoint proteins, including RAD9, to regulate ATR signaling. Molecular and cellular biology, 28(24), 7345–7353. https://doi.org/10.1128/MCB.01079-08

Sequence derived from: https://www.uniprot.org/uniprotkb/P27694/entry

[edit]
Categories
Parameters
None