2018
DOI: 10.1101/gad.308510.117
|View full text |Cite
|
Sign up to set email alerts
|

A meiotic XPF–ERCC1-like complex recognizes joint molecule recombination intermediates to promote crossover formation

Abstract: Meiotic crossover formation requires the stabilization of early recombination intermediates by a set of proteins and occurs within the environment of the chromosome axis, a structure important for the regulation of meiotic recombination events. The molecular mechanisms underlying and connecting crossover recombination and axis localization are elusive. Here, we identified the ZZS (Zip2-Zip4-Spo16) complex, required for crossover formation, which carries two distinct activities: one provided by Zip4, which acts… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

18
149
1

Year Published

2018
2018
2024
2024

Publication Types

Select...
4
4
1

Relationship

4
5

Authors

Journals

citations
Cited by 90 publications
(175 citation statements)
references
References 65 publications
18
149
1
Order By: Relevance
“…lack or altered distribution of meiotic crossovers is a major source of aneuploidies, 23 leading to sterility or disorders such as the Down syndrome, highlighting the 24 importance of understanding how crossovers are controlled during meiosis. 25 Meiotic recombination is triggered by the formation of programmed DNA DSBs, 26 catalyzed by Spo11 together with several conserved protein partners 2,3 . 27 Following Spo11 removal, 5' DSB ends are resected and the 3' ends invade a 28 homologous template, leading to formation of D-loop intermediates.…”
Section: A 22mentioning
confidence: 99%
“…lack or altered distribution of meiotic crossovers is a major source of aneuploidies, 23 leading to sterility or disorders such as the Down syndrome, highlighting the 24 importance of understanding how crossovers are controlled during meiosis. 25 Meiotic recombination is triggered by the formation of programmed DNA DSBs, 26 catalyzed by Spo11 together with several conserved protein partners 2,3 . 27 Following Spo11 removal, 5' DSB ends are resected and the 3' ends invade a 28 homologous template, leading to formation of D-loop intermediates.…”
Section: A 22mentioning
confidence: 99%
“…Distinct activities of the ZMMs influence different aspects of crossover maturation and couple these events to homolog synapsis. The DNA helicase, Mer3, functions both to regulate the extension of nascent D-loops by DNA synthesis and stabilize JMs (Borner et al, 2004;Duroc et al, 2017;Mazina et al, 2004;Nakagawa and Kolodner, 2002); the XPF-ERCC1 related complex, Zip2-Spo16, specifically binds JMs (De Muyt et al, 2018;Guiraldelli et al, 2018;Macaisne et al, 2011); Zip1 acts both locally to promote ZMM function and globally as the major component of SCs (Chen et al, 2015;Sym et al, 1993;Voelkel-Meiman et al, 2015); Zip3 is a SUMO E3 ligase that helps localize other ZMMs to nascent crossover sites and facilitates synapsis (Agarwal and Roeder, 2000;Cheng et al, 2006;Macqueen and Roeder, 2009;Shinohara et al, 2008); and Zip4 is a large TPR repeat protein thought to bridge interactions between Zip2-Spo16, Zip3, MutSγ and the chromosome axis protein Red1 (De Muyt et al, 2018). Several activities are ascribed to MutSγ: (i) specific binding to JM structures (D-loops and Holliday junctions) (Snowden et al, 2004); (ii) stabilization of nascent JMs following ATPdependent conversion of JM-bound MutSγ into a sliding clamp that diffuse away from the junction point while embracing two DNA duplexes (Snowden et al, 2004); (iii) protection of dHJs from the anti-crossover "dissolution" activity of the STR decatenase complex, Sgs1-Top3-Rmi1 (equivalent to the human BTR complex, BLM-TOPIIIα-RMI1/2) (Jessop et al, 2006;Kaur et al, 2015;Oh et al, 2007;Tang et al, 2015) (Tang and Hunter, unpublished); (iv) direct or indirect recruitment and activation of crossover-biased JM resolving factors such as the MutLγ endonuclease (Manhart et al, 2017;Nishant et al, 2008;Ranjha et al, 2014;Zakharyevich et al, 2012); (v) formation and/or stabilization of homolog synapsis (Borner et al, 2004;…”
Section: The Crossover Activity Of Mutsγ Is Activated By Stabilizing mentioning
confidence: 99%
“…ZMMs include Zip1, Zip2, Zip3, Mer3, Msh4, Msh5, Spo22/Zip4 and Spo16. Msh4-Msh5 and Zip2-Zip4-Spo16 sub-complexes bind to branched DNAs (SNOWDEN et al 2004; ARORA AND CORBETT 2018;DE MUYT et al 2018). Mer3 encodes a 5'-3' DNA helicase (NAKAGAWA AND OGAWA 1999;NAKAGAWA et al 2001).…”
Section: Introductionmentioning
confidence: 99%