Backbone and ILV side-chain methyl NMR resonance assignments of human Rev7/Rev3-RBM1 and Rev7/Rev3-RBM2 complexes.

Autor: Arianna GA; Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT, 06030, USA., Geddes-Buehre DH; Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT, 06030, USA., Korzhnev DM; Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT, 06030, USA. korzhniev@uchc.edu.
Jazyk: angličtina
Zdroj: Biomolecular NMR assignments [Biomol NMR Assign] 2023 Jun; Vol. 17 (1), pp. 107-114. Date of Electronic Publication: 2023 May 02.
DOI: 10.1007/s12104-023-10128-4
Abstrakt: Rev7 is a versatile HORMA (Hop1, Rev7, Mad2) family adaptor protein with multiple roles in mitotic regulation and DNA damage response, and an essential accessory subunit of the translesion synthesis (TLS) DNA polymerase Polζ employed in replication of damaged DNA. Within Polζ, the two copies of Rev7 interact with the two Rev7-bonding motifs (RBM1 and RBM2) of the catalytic subunit Rev3 by a mechanism characteristic of HORMA proteins whereby the "safety-belt" loop of Rev7 closes on the top of the ligand. Here we report the nearly complete backbone and Ile, Val, Leu side-chain methyl NMR resonance assignments of the 27 kDa human Rev7/Rev3-RBM1 and Rev7/Rev3-RBM2 complexes (BMRB deposition numbers 51651 and 51652) that will facilitate future NMR studies of Rev7 dynamics and interactions.
(© 2023. The Author(s), under exclusive licence to Springer Nature B.V.)
Databáze: MEDLINE
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