scholarly journals Nuclear myosin/actin-motored contact between homologous chromosomes is initiated by ATM kinase and homology-directed repair proteins at double-strand DNA breaks to suppress chromosome rearrangements

Oncotarget ◽  
2018 ◽  
Vol 9 (17) ◽  
pp. 13612-13622 ◽  
Author(s):  
Viktoria N. Evdokimova ◽  
Manoj Gandhi ◽  
Alyaksandr V. Nikitski ◽  
Christopher J. Bakkenist ◽  
Yuri E. Nikiforov
2020 ◽  
Author(s):  
Dorota Rousova ◽  
Saskia K. Funk ◽  
Heidi Reichle ◽  
John R. Weir

One of the defining features of sexual reproduction is the recombination events that take place during meiosis I. Recombination is both evolutionarily advantageous, but also mechanistically necessary to form the crossovers that link homologous chromosomes. Meiotic recombination is initiated through the placement of programmed double-strand DNA breaks (DSBs) mediated by the protein Spo11. The timing, number, and physical placement of DSBs are carefully controlled through a variety of protein machinery. Previous work has implicated Mer2(IHO1 in mammals) to be involved in both the placement of breaks, and their timing. In this study we use a combination of protein biochemistry and biophysics to extensively characterise various roles of the Mer2. We gain further insights into the details of Mer2 interaction with the PHD protein Spp1, reveal that Mer2 is a novel nucleosome binder, and suggest how Mer2’s interaction with the HORMA domain protein Hop1 (HORMAD1/2 in mammals) is controlled.


Genetics ◽  
1996 ◽  
Vol 143 (3) ◽  
pp. 1115-1125 ◽  
Author(s):  
Fei Xu ◽  
Thomas D Petes

Abstract Meiotic recombination in Saccharomyces cerevisiae is initiated by double-strand DNA breaks (DSBs). Using two approaches, we mapped the position of DSBs associated with a recombination hotspot created by insertion of telomeric sequences into the region upstream of HIS4. We found that the breaks have no obvious sequence specificity and localize to a region of ~50 bp adjacent to the telomeric insertion. By mapping the breaks and by studies of the exonuclease III sensitivity of the broken ends, we conclude that most of the broken DNA molecules have blunt ends with 3′-hydroxyl groups.


2010 ◽  
Vol 32 (1) ◽  
pp. 39-47 ◽  
Author(s):  
Anna Łękawa–Ilczuk ◽  
Halina Antosz ◽  
Beata Rymgayłło–Jankowska ◽  
Tomasz Żarnowski

2017 ◽  
Vol 23 (26) ◽  
pp. 6459-6459
Author(s):  
Sebastian Bestgen ◽  
Carmen Seidl ◽  
Thomas Wiesner ◽  
Andreas Zimmer ◽  
Martina Falk ◽  
...  

Gerontology ◽  
2015 ◽  
Vol 62 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Jin-Sun Ryu ◽  
Hyeon-Sook Koo

Werner syndrome protein (WRN) is unusual among RecQ family DNA helicases in having an additional exonuclease activity. WRN is involved in the repair of double-strand DNA breaks via the homologous recombination and nonhomologous end joining pathways, and also in the base excision repair pathway. In addition, the protein promotes the recovery of stalled replication forks. The helicase activity is thought to unwind DNA duplexes, thereby moving replication forks or Holliday junctions. The targets of the exonuclease could be the nascent DNA strands at a replication fork or the ends of double-strand DNA breaks. However, it is not clear which enzyme activities are essential for repairing different types of DNA damage. Model organisms such as mice, flies, and worms deficient in WRN homologs have been investigated to understand the physiological results of defects in WRN activity. Premature aging, the most remarkable characteristic of Werner syndrome, is also seen in the mutant mice and worms, and hypersensitivity to DNA damage has been observed in WRN mutants of all three model organisms, pointing to conservation of the functions of WRN. In the nematode Caenorhabditis elegans, the WRN homolog contains a helicase domain but no exonuclease domain, so that this animal is very useful for studying the in vivo functions of the helicase without interference from the activity of the exonuclease. Here, we review the current status of investigations of C. elegans WRN-1 and discuss its functional differences from the mammalian homologs.


Andrology ◽  
2020 ◽  
Vol 8 (5) ◽  
pp. 1287-1303
Author(s):  
Ana Tímermans ◽  
Rosana Vázquez ◽  
Fátima Otero ◽  
Jaime Gosálvez ◽  
Stephen Johnston ◽  
...  

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