scholarly journals MHF 1 plays F anconi anaemia complementation group M protein ( FANCM )‐dependent and FANCM ‐independent roles in DNA repair and homologous recombination in plants

2014 ◽  
Vol 78 (5) ◽  
pp. 822-833 ◽  
Author(s):  
Natalie J. Dangel ◽  
Alexander Knoll ◽  
Holger Puchta
2013 ◽  
Vol 41 (6) ◽  
pp. 1726-1730 ◽  
Author(s):  
Fekret Osman ◽  
Matthew C. Whitby

Centromere proteins CENP-S and CENP-X are members of the constitutive centromere-associated network, which is a conserved group of proteins that are needed for the assembly and function of kinetochores at centromeres. Intriguingly CENP-S and CENP-X have alter egos going by the names of MHF1 (FANCM-associated histone-fold protein 1) and MHF2 respectively. In this guise they function with a DNA translocase called FANCM (Fanconi’s anemia complementation group M) to promote DNA repair and homologous recombination. In the present review we discuss current knowledge of the biological roles of CENP-S and CENP-X and how their dual existence may be a common feature of CCAN (constitutive centromere-associated network) proteins.


iScience ◽  
2021 ◽  
pp. 102534
Author(s):  
Shibin Xu ◽  
Xingxuan Wu ◽  
Peipei Wang ◽  
Sheng-Li Cao ◽  
Bin Peng ◽  
...  

2020 ◽  
Vol 117 (4) ◽  
pp. 2084-2091
Author(s):  
Jekaterina Vohhodina ◽  
Kimberly J. Toomire ◽  
Sarah A. Petit ◽  
Goran Micevic ◽  
Geeta Kumari ◽  
...  

BRCA1 promotes error-free, homologous recombination-mediated repair (HRR) of DNA double-stranded breaks (DSBs). When excessive and uncontrolled, BRCA1 HRR activity promotes illegitimate recombination and genome disorder. We and others have observed that the BRCA1-associated protein RAP80 recruits BRCA1 to postdamage nuclear foci, and these chromatin structures then restrict the amplitude of BRCA1-driven HRR. What remains unclear is how this process is regulated. Here we report that both BRCA1 poly-ADP ribosylation (PARsylation) and the presence of BRCA1-bound RAP80 are critical for the normal interaction of BRCA1 with some of its partners (e.g., CtIP and BACH1) that are also known components of the aforementioned focal structures. Surprisingly, the simultaneous loss of RAP80 and failure therein of BRCA1 PARsylation results in the dysregulated accumulation in these foci of BRCA1 complexes. This in turn is associated with the intracellular development of a state of hyper-recombination and gross chromosomal disorder. Thus, physiological RAP80-BRCA1 complex formation and BRCA1 PARsylation contribute to the kinetics by which BRCA1 HRR-sustaining complexes normally concentrate in nuclear foci. These events likely contribute to aneuploidy suppression.


2005 ◽  
Vol 37 (9) ◽  
pp. 958-963 ◽  
Author(s):  
Amom Ruhikanta Meetei ◽  
Annette L Medhurst ◽  
Chen Ling ◽  
Yutong Xue ◽  
Thiyam Ramsing Singh ◽  
...  

2013 ◽  
Vol 41 (1) ◽  
pp. 314-320 ◽  
Author(s):  
John K. Blackwood ◽  
Neil J. Rzechorzek ◽  
Sian M. Bray ◽  
Joseph D. Maman ◽  
Luca Pellegrini ◽  
...  

During DNA repair by HR (homologous recombination), the ends of a DNA DSB (double-strand break) must be resected to generate single-stranded tails, which are required for strand invasion and exchange with homologous chromosomes. This 5′–3′ end-resection of the DNA duplex is an essential process, conserved across all three domains of life: the bacteria, eukaryota and archaea. In the present review, we examine the numerous and redundant helicase and nuclease systems that function as the enzymatic analogues for this crucial process in the three major phylogenetic divisions.


2015 ◽  
Vol 155 (1) ◽  
pp. 53-63 ◽  
Author(s):  
Eloïse Véquaud ◽  
Grégoire Desplanques ◽  
Pascal Jézéquel ◽  
Philippe Juin ◽  
Sophie Barillé-Nion

Cell Reports ◽  
2017 ◽  
Vol 20 (8) ◽  
pp. 1921-1935 ◽  
Author(s):  
Waaqo Daddacha ◽  
Allyson E. Koyen ◽  
Amanda J. Bastien ◽  
PamelaSara E. Head ◽  
Vishal R. Dhere ◽  
...  

2018 ◽  
Vol 144 (4) ◽  
pp. 755-766 ◽  
Author(s):  
Catia Mio ◽  
Lorenzo Gerratana ◽  
Marco Bolis ◽  
Federica Caponnetto ◽  
Andrea Zanello ◽  
...  

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