Full-Length Synaptonemal Complex Grows Continuously during Meiotic Prophase in Budding Yeast 英文参考文献.docVIP

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Full-Length Synaptonemal Complex Grows Continuously during Meiotic Prophase in Budding Yeast 英文参考文献.doc

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Full-Length Synaptonemal Complex Grows Continuously during Meiotic Prophase in Budding Yeast 英文参考文献

Full-LengthSynaptonemalComplexGrowsContinuously duringMeioticProphaseinBuddingYeast KarenVoelkel-Meiman1.,SarahS.Moustafa1,2.,PhilippeLefranc?ois2,AnneM.Villeneuve3, AmyJ.MacQueen1* 1DepartmentofMolecularBiologyandBiochemistry,WesleyanUniversity,Middletown,Connecticut,UnitedStatesofAmerica,2DepartmentofMolecular,Cellular,and Developmental Biology, Yale University, New Haven, Connecticut, United States of America, 3Department of Developmental Biology, Stanford University, Stanford, California,UnitedStatesofAmerica Abstract The synaptonemal complex (SC) links two meiotic prophase chromosomal events: homolog pairing and crossover recombination. SC formation involves the multimeric assembly of coiled-coil proteins (Zip1 in budding yeast) at the interface of aligned homologous chromosomes. However, SC assembly is indifferent to homology and thus is normally regulated such that it occurs only subsequent to homology recognition. Assembled SC structurally interfaces with and influencesthelevelanddistributionofinterhomologcrossoverrecombinationevents.Despiteitsinvolvementindynamic chromosome behaviors such as homolog pairing and recombination, the extent to which SC, once installed, acts as an irreversible tether or maintains the capacity to remodel is not clear. Experiments presented here reveal insight into the dynamics of the full-length SC in budding yeast meiotic cells. We demonstrate that Zip1 continually incorporates into previously assembled synaptonemal complex during meiotic prophase. Moreover, post-synapsis Zip1 incorporation is sufficienttorescuethesporulationdefecttriggeredbySCsbuiltwithamutantversionofZip1,Zip1-4LA.Post-synapsisZip1 incorporationoccursinitiallywithanon-uniformspatialdistribution,predominantlyassociatedwithZip3,acomponentof thesynapsisinitiationcomplexthatispresumedtomarkasubsetofcrossoversites.Anon-uniformdynamicarchitectureof the SC is observed independently of (i) synapsis initiation components, (ii) the Pch2 and Pph3 proteins that have bee