Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 115, Issue 35, Page E8191-E8200, Year 2018
Publish date	Aug 28, 2018
Authors	Alessandro A Rizzo / Faye-Marie Vassel / Nimrat Chatterjee / Sanjay D'Souza / Yunfeng Li / Bing Hao / Michael T Hemann / Graham C Walker / Dmitry M Korzhnev /
PubMed Abstract	The translesion synthesis (TLS) polymerases Polζ and Rev1 form a complex that enables replication of damaged DNA. The Rev7 subunit of Polζ, which is a multifaceted HORMA (Hop1, Rev7, Mad2) protein ...The translesion synthesis (TLS) polymerases Polζ and Rev1 form a complex that enables replication of damaged DNA. The Rev7 subunit of Polζ, which is a multifaceted HORMA (Hop1, Rev7, Mad2) protein with roles in TLS, DNA repair, and cell-cycle control, facilitates assembly of this complex by binding Rev1 and the catalytic subunit of Polζ, Rev3. Rev7 interacts with Rev3 by a mechanism conserved among HORMA proteins, whereby an open-to-closed transition locks the ligand underneath the "safety belt" loop. Dimerization of HORMA proteins promotes binding and release of this ligand, as exemplified by the Rev7 homolog, Mad2. Here, we investigate the dimerization of Rev7 when bound to the two Rev7-binding motifs (RBMs) in Rev3 by combining in vitro analyses of Rev7 structure and interactions with a functional assay in a Rev7 cell line. We demonstrate that Rev7 uses the conventional HORMA dimerization interface both to form a homodimer when tethered by the two RBMs in Rev3 and to heterodimerize with other HORMA domains, Mad2 and p31 Structurally, the Rev7 dimer can bind only one copy of Rev1, revealing an unexpected Rev1/Polζ architecture. In cells, mutation of the Rev7 dimer interface increases sensitivity to DNA damage. These results provide insights into the structure of the Rev1/Polζ TLS assembly and highlight the function of Rev7 homo- and heterodimerization.
External links	Proc Natl Acad Sci U S A / PubMed:30111544 / PubMed Central
Methods	SAS (X-ray synchrotron) / X-ray diffraction
Resolution	1.43 - 2.8 Å
Structure data	SASDC29: Human Rev7 dimer in complex with Rev3 peptide @ 10.6 mg/mL Method: SAXS/SANS SASDC39: Human Rev7 dimer in complex with Rev3 peptide @ 9.1mg/mL Method: SAXS/SANS SASDC49: Human Rev7 dimer in complex with Rev3 peptide @ 6.1mg/mL Method: SAXS/SANS SASDC59: Human Rev7 dimer in complex with Rev3 peptide @ 7.6mg/mL Method: SAXS/SANS SASDC69: Human Rev7 dimer in complex with Rev3 peptide @ 4.6mg/mL Method: SAXS/SANS SASDC79: Human Rev7 dimer in complex with Rev3 peptide @ 3.0mg/mL Method: SAXS/SANS SASDC89: Human Rev7 dimer in complex with Rev3 peptide @ 1.5 mg/mL Method: SAXS/SANS SASDCW8: Human Rev7 monomer (R124A mutant) in complex with Rev3 peptide @ 4mg/mL Method: SAXS/SANS SASDCX8: Human Rev7 monomer (R124A mutant) in complex with Rev3 peptide @ 6mg/mL Method: SAXS/SANS SASDCY8: Human Rev7 monomer (R124A mutant) in complex with Rev3 peptide @ 8mg/mL Method: SAXS/SANS SASDCZ8: Human Rev7 dimer in complex with Rev3 peptide @ 12.2 mg/mL Method: SAXS/SANS PDB-6bc8: Crystal structure of Rev7-R124A/Rev3-RBM2 (residues 1988-2014) complex Method: X-RAY DIFFRACTION / Resolution: 1.68 Å PDB-6bcd: Crystal structure of Rev7-K44A/R124A/A135D in complex with Rev3-RBM2 (residues 1988-2014) Method: X-RAY DIFFRACTION / Resolution: 1.43 Å PDB-6bi7: Crystal structure of Rev7-WT/Rev3 as a monomer under high-salt conditions Method: X-RAY DIFFRACTION / Resolution: 2.8 Å
Chemicals	ChemComp-SO4: SULFATE ION ChemComp-ACT: ACETATE ION ChemComp-HOH: WATER
Source	homo sapiens (human)
Keywords	REPLICATION / DNA damage tolerance / translesion DNA synthesis