Structural transitions and mechanochemical coupling in the nucleoprotein filament explain homology selectivity and Rad51 protein cooperativity in cellular DNA repair

SX Atwell, D Migliozzi, A Dupont, JL Viovy, G Cappello - Physical Review E, 2020 - APS
The nucleoprotein filament (NPF) is the fundamental element of homologous recombination
(HR), a major mechanism for the repair of double-strand DNA breaks in the cell. The NPF is …

[PDF][PDF] Physical Mechanisms of DNA repair: A single molecule perspective

A Candelli - 2013 - research.vu.nl
Figure 6 RAD51 filament formation at the single-molecule level using DNA manipulation. 23
Figure 7 RAD51 filament formation at the single-molecule level using fluorescence …

[PDF][PDF] DNA repair mechanisms revisited By single molecule approaches

J Miné-Hattab - 2022 - hal.science
I am a biophysicist who is passionate about understanding how different kind of stresses can
alter molecular organization and dynamics and the resulting consequences on cell …

Evidence for conformational capture mechanism for damage recognition by DNA repairprotein Rad4

S Chakraborty, S Baral, D Paul, PJ Steinbach… - Biophysical …, 2019 - cell.com
XPC protein recognizes diverse DNA lesions including ultraviolet-photolesions and
carcinogen-DNA adducts, initiating nucleotide excision repair. Structural studies showed …

RAD 51 discrimination between single‐and double‐strand DNA: a matter of flexibility and enthalpy

S Subramanyam, M Spies - The EMBO journal, 2020 - embopress.org
In selecting ss DNA over ds DNA, the RAD 51 DNA strand exchange protein has to
overcome the entropy associated with straightening of single‐strand DNA upon …

Dissecting elastic heterogeneity along DNA molecules coated partly with Rad51 using concurrent fluorescence microscopy and optical tweezers

J van Mameren, M Modesti, R Kanaar, C Wyman… - Biophysical journal, 2006 - cell.com
Nucleoprotein filament formation by recombinases is central to homologous recombination.
To follow this process, we used fluorescent human Rad51 recombinase to visualize the …

The role of nucleotide opening dynamics in facilitated target search by DNA-repair proteins

SK Mishra, DW Heermann, A Bhattacherjee - Biochimica et Biophysica …, 2024 - Elsevier
Preserving the genomic integrity stands a fundamental necessity, primarily achieved by the
DNA repair proteins through their continuous patrolling on the DNA in search of lesions …

Molecular flexibility of DNA as a key determinant of RAD 51 recruitment

F Paoletti, AH El‐Sagheer, J Allard, T Brown… - The EMBO …, 2020 - embopress.org
The timely activation of homologous recombination is essential for the maintenance of
genome stability, in which the RAD 51 recombinase plays a central role. Biochemically …

Tethering-facilitated DNA 'opening'and complementary roles of β-hairpin motifs in the Rad4/XPC DNA damage sensor protein

D Paul, H Mu, A Tavakoli, Q Dai, X Chen… - Nucleic acids …, 2020 - academic.oup.com
XPC/Rad4 initiates eukaryotic nucleotide excision repair on structurally diverse helix-
destabilizing/distorting DNA lesions by selectively 'opening'these sites while rapidly diffusing …

Local structural dynamics of Rad51 protomers revealed by cryo-electron microscopy of Rad51-ssDNA filaments

J Liu, S Gore, WD Heyer - bioRxiv, 2024 - biorxiv.org
Homologous recombination (HR) is a high-fidelity repair mechanism for double-strand
breaks. Rad51 is the key enzyme that forms filaments on single-stranded DNA (ssDNA) to …