6bzg
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ZIP2_YEAST ZIP2_YEAST]] Required for initiation of meiotic chromosome synapsis. Involved in synaptonemal complex formation, a structure that tethers a pair of homologous chromosomes along their lengths and plays a central role in recombination and homolog segregation during meiosis. Required for the normal localization of MSH4 to chromosomes.<ref>PMID:10319812</ref> <ref>PMID:10848609</ref> <ref>PMID:10943844</ref> <ref>PMID:11454751</ref> <ref>PMID:15805472</ref> <ref>PMID:16740482</ref> <ref>PMID:9590170</ref> [[http://www.uniprot.org/uniprot/SPO16_YEAST SPO16_YEAST]] Necessary for efficient spore formation. | [[http://www.uniprot.org/uniprot/ZIP2_YEAST ZIP2_YEAST]] Required for initiation of meiotic chromosome synapsis. Involved in synaptonemal complex formation, a structure that tethers a pair of homologous chromosomes along their lengths and plays a central role in recombination and homolog segregation during meiosis. Required for the normal localization of MSH4 to chromosomes.<ref>PMID:10319812</ref> <ref>PMID:10848609</ref> <ref>PMID:10943844</ref> <ref>PMID:11454751</ref> <ref>PMID:15805472</ref> <ref>PMID:16740482</ref> <ref>PMID:9590170</ref> [[http://www.uniprot.org/uniprot/SPO16_YEAST SPO16_YEAST]] Necessary for efficient spore formation. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In eukaryotic meiosis, generation of haploid gametes depends on the formation of inter-homolog crossovers, which enable the pairing, physical linkage, and eventual segregation of homologs in the meiosis I division. A class of conserved meiosis-specific proteins, collectively termed ZMMs, are required for formation and spatial control of crossovers throughout eukaryotes. Here, we show that three Saccharomyces cerevisiae ZMM proteins-Zip2, Zip4 and Spo16-interact with one another and form a DNA-binding complex critical for crossover formation and control. We determined the crystal structure of a Zip2:Spo16 subcomplex, revealing a heterodimer structurally related to the XPF:ERCC1 endonuclease complex. Zip2:Spo16 lacks an endonuclease active site, but binds specific DNA structures found in early meiotic recombination intermediates. Mutations in multiple DNA-binding surfaces on Zip2:Spo16 severely compromise DNA binding, supporting a model in which the complex's central and HhH domains cooperate to bind DNA. Overall, our data support a model in which the Zip2:Zip4:Spo16 complex binds and stabilizes early meiotic recombination intermediates, then coordinates additional factors to promote crossover formation and license downstream events including synaptonemal complex assembly. | ||
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| + | The conserved XPF:ERCC1-like Zip2:Spo16 complex controls meiotic crossover formation through structure-specific DNA binding.,Arora K, Corbett KD Nucleic Acids Res. 2018 Dec 19. pii: 5253063. doi: 10.1093/nar/gky1273. PMID:30566683<ref>PMID:30566683</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6bzg" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 08:07, 21 February 2019
Structure of S. cerevisiae Zip2:Spo16 complex, P212121 form
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