Proteomics,Multiomics

Dataset Information

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Identification of a new XPF-ERCC1-like complex important for meiotic crossovers production


ABSTRACT: Proteins of the XPF-ERCC1 complex family play roles in DNA repair. Known members (four in mammals, two in budding yeast) recognize branched DNA structures and most bear nuclease activity. Here, we identified a new XPF-ERCC1-like complex important for meiotic crossovers production. Through a proteomic screen, we found that Zip2 and Spo16, two proteins important for CO formation in budding yeast, form a complex and share structural similarities with XPF-ERCC1. Zip2 XPF domain is important for CO formation and, in complex with Spo16, preferentially binds branched DNA molecules. However, Zip2-Spo16 lacks endonucleolytic activity. This suggests that Zip2-Spo16 works as a structural module that recognizes and stabilizes joint molecules to ensure CO formation. Moreover, Zip2-Spo16 forms a complex (called ZZS) with Zip4, another protein important for CO formation, which directly interacts with components of the chromosome axis, providing a link between recombination intermediates and the underlying chromosome structure.

OTHER RELATED OMICS DATASETS IN: PRJNA407372

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Yohann Couté  

LAB HEAD: Virginie Brun

PROVIDER: PXD007735 | Pride | 2018-04-10

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
QEx2_001342.raw Raw
QEx2_001344.raw Raw
QEx2_001818.raw Raw
QEx2_001827.raw Raw
QEx2_007389.raw Raw
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Publications


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 Z  ...[more]

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