scholarly journals The Fanconi Anemia Protein FANCM Can Promote Branch Migration of Holliday Junctions and Replication Forks

2008 ◽  
Vol 29 (1) ◽  
pp. 141-148 ◽  
Author(s):  
Kerstin Gari ◽  
Chantal Décaillet ◽  
Alicja Z. Stasiak ◽  
Andrzej Stasiak ◽  
Angelos Constantinou
Cells ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1357
Author(s):  
Rubén Torres ◽  
Carolina Gándara ◽  
Begoña Carrasco ◽  
Ignacio Baquedano ◽  
Silvia Ayora ◽  
...  

The DNA damage checkpoint protein DisA and the branch migration translocase RecG are implicated in the preservation of genome integrity in reviving haploid Bacillus subtilis spores. DisA synthesizes the essential cyclic 3′, 5′-diadenosine monophosphate (c‑di-AMP) second messenger and such synthesis is suppressed upon replication perturbation. In vitro, c-di-AMP synthesis is suppressed when DisA binds DNA structures that mimic stalled or reversed forks (gapped forks or Holliday junctions [HJ]). RecG, which does not form a stable complex with DisA, unwinds branched intermediates, and in the presence of a limiting ATP concentration and HJ DNA, it blocks DisA-mediated c-di-AMP synthesis. DisA pre-bound to a stalled or reversed fork limits RecG-mediated ATP hydrolysis and DNA unwinding, but not if RecG is pre-bound to stalled or reversed forks. We propose that RecG-mediated fork remodeling is a genuine in vivo activity, and that DisA, as a molecular switch, limits RecG-mediated fork reversal and fork restoration. DisA and RecG might provide more time to process perturbed forks, avoiding genome breakage.


1994 ◽  
Vol 22 (3) ◽  
pp. 308-313 ◽  
Author(s):  
Gary J. Sharples ◽  
Matthew C. Whitby ◽  
Lizanne Ryder ◽  
Robert G. Lloyd

Nature ◽  
2006 ◽  
Vol 442 (7102) ◽  
pp. 590-593 ◽  
Author(s):  
Dmitry V. Bugreev ◽  
Olga M. Mazina ◽  
Alexander V. Mazin

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Ann-Marie K. Shorrocks ◽  
Samuel E. Jones ◽  
Kaima Tsukada ◽  
Carl A. Morrow ◽  
Zoulikha Belblidia ◽  
...  

AbstractThe Bloom syndrome helicase BLM interacts with topoisomerase IIIα (TOP3A), RMI1 and RMI2 to form the BTR complex, which dissolves double Holliday junctions to produce non-crossover homologous recombination (HR) products. BLM also promotes DNA-end resection, restart of stalled replication forks, and processing of ultra-fine DNA bridges in mitosis. How these activities of the BTR complex are regulated in cells is still unclear. Here, we identify multiple conserved motifs within the BTR complex that interact cooperatively with the single-stranded DNA (ssDNA)-binding protein RPA. Furthermore, we demonstrate that RPA-binding is required for stable BLM recruitment to sites of DNA replication stress and for fork restart, but not for its roles in HR or mitosis. Our findings suggest a model in which the BTR complex contains the intrinsic ability to sense levels of RPA-ssDNA at replication forks, which controls BLM recruitment and activation in response to replication stress.


2012 ◽  
Author(s):  
Natalia Y. Karpechenko ◽  
Nina G. Dolinnaya ◽  
Vladimir I. Popenko ◽  
Marianna G. Yakubovskaya ◽  
Victoria K. Gasanova

Structure ◽  
2016 ◽  
Vol 24 (8) ◽  
pp. 1292-1300 ◽  
Author(s):  
Soochul Shin ◽  
Jinwoo Lee ◽  
Sangwoon Yoo ◽  
Tomasz Kulikowicz ◽  
Vilhelm A. Bohr ◽  
...  

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