scholarly journals Phosphorylation of the Archaeal Holliday Junction Resolvase Hjc Inhibits Its Catalytic Activity and Facilitates DNA Repair in Sulfolobus islandicus REY15A

2019 ◽  
Vol 10 ◽  
Author(s):  
Qihong Huang ◽  
Joseph Badys Mayaka ◽  
Qing Zhong ◽  
Chao Zhang ◽  
Guihua Hou ◽  
...  
2009 ◽  
Vol 138 (1) ◽  
pp. 78-89
Author(s):  
Samira Fekairi ◽  
Sarah Scaglione ◽  
Charly Chahwan ◽  
Ewan R. Taylor ◽  
Agnès Tissier ◽  
...  

2009 ◽  
Vol 138 (1) ◽  
pp. 63-77
Author(s):  
Jennifer M. Svendsen ◽  
Agata Smogorzewska ◽  
Mathew E. Sowa ◽  
Brenda C. O'Connell ◽  
Steven P. Gygi ◽  
...  

Cell ◽  
2009 ◽  
Vol 138 (1) ◽  
pp. 78-89 ◽  
Author(s):  
Samira Fekairi ◽  
Sarah Scaglione ◽  
Charly Chahwan ◽  
Ewan R. Taylor ◽  
Agnès Tissier ◽  
...  

Cell ◽  
2009 ◽  
Vol 138 (1) ◽  
pp. 63-77 ◽  
Author(s):  
Jennifer M. Svendsen ◽  
Agata Smogorzewska ◽  
Mathew E. Sowa ◽  
Brenda C. O'Connell ◽  
Steven P. Gygi ◽  
...  

2021 ◽  
Vol 22 (18) ◽  
pp. 9811 ◽  
Author(s):  
Paula Alonso-Ramos ◽  
David Álvarez-Melo ◽  
Katerina Strouhalova ◽  
Carolina Pascual-Silva ◽  
George B. Garside ◽  
...  

Meiotic defects derived from incorrect DNA repair during gametogenesis can lead to mutations, aneuploidies and infertility. The coordinated resolution of meiotic recombination intermediates is required for crossover formation, ultimately necessary for the accurate completion of both rounds of chromosome segregation. Numerous master kinases orchestrate the correct assembly and activity of the repair machinery. Although much less is known, the reversal of phosphorylation events in meiosis must also be key to coordinate the timing and functionality of repair enzymes. Cdc14 is a crucial phosphatase required for the dephosphorylation of multiple CDK1 targets in many eukaryotes. Mutations that inactivate this phosphatase lead to meiotic failure, but until now it was unknown if Cdc14 plays a direct role in meiotic recombination. Here, we show that the elimination of Cdc14 leads to severe defects in the processing and resolution of recombination intermediates, causing a drastic depletion in crossovers when other repair pathways are compromised. We also show that Cdc14 is required for the correct activity and localization of the Holliday Junction resolvase Yen1/GEN1. We reveal that Cdc14 regulates Yen1 activity from meiosis I onwards, and this function is essential for crossover resolution in the absence of other repair pathways. We also demonstrate that Cdc14 and Yen1 are required to safeguard sister chromatid segregation during the second meiotic division, a late action that is independent of the earlier role in crossover formation. Thus, this work uncovers previously undescribed functions of the evolutionary conserved Cdc14 phosphatase in the regulation of meiotic recombination.


Genetics ◽  
1996 ◽  
Vol 144 (1) ◽  
pp. 27-41 ◽  
Author(s):  
Larry A Gilbertson ◽  
Franklin W Stahl

Abstract We tested predictions of the double-strand break repair (DSBR) model for meiotic recombination by examining the segregation patterns of small palindromic insertions, which frequently escape mismatch repair when in heteroduplex DNA. The palindromes flanked a well characterized DSB site at the ARC4 locus. The “canonical” DSBR model, in which only 5′ ends are degraded and resolution of the four-stranded intermediate is by Holliday junction resolvase, predicts that hDNA will frequently occur on both participating chromatids in a single event. Tetrads reflecting this configuration of hDNA were rare. In addition, a class of tetrads not predicted by the canonical DSBR model was identified. This class represented events that produced hDNA in a “trans” configuration, on opposite strands of the same duplex on the two sides of the DSB site. Whereas most classes of convertant tetrads had typical frequencies of associated crossovers, tetrads with trans hDNA were parental for flanking markers. Modified versions of the DSBR model, including one that uses a topoisomerase to resolve the canonical DSBR intermediate, are supported by these data.


Sign in / Sign up

Export Citation Format

Share Document