RRC ID 46568
Author Baudrimont A, Penkner A, Woglar A, Machacek T, Wegrostek C, Gloggnitzer J, Fridkin A, Klein F, Gruenbaum Y, Pasierbek P, Jantsch V.
Title Leptotene/zygotene chromosome movement via the SUN/KASH protein bridge in Caenorhabditis elegans.
Journal PLoS Genet
Abstract The Caenorhabditis elegans inner nuclear envelope protein matefin/SUN-1 plays a conserved, pivotal role in the process of genome haploidization. CHK-2-dependent phosphorylation of SUN-1 regulates homologous chromosome pairing and interhomolog recombination in Caenorhabditis elegans. Using time-lapse microscopy, we characterized the movement of matefin/SUN-1::GFP aggregates (the equivalent of chromosomal attachment plaques) and showed that the dynamics of matefin/SUN-1 aggregates remained unchanged throughout leptonene/zygotene, despite the progression of pairing. Movement of SUN-1 aggregates correlated with chromatin polarization. We also analyzed the requirements for the formation of movement-competent matefin/SUN-1 aggregates in the context of chromosome structure and found that chromosome axes were required to produce wild-type numbers of attachment plaques. Abrogation of synapsis led to a deceleration of SUN-1 aggregate movement. Analysis of matefin/SUN-1 in a double-strand break deficient mutant revealed that repair intermediates influenced matefin/SUN-1 aggregate dynamics. Investigation of movement in meiotic regulator mutants substantiated that proper orchestration of the meiotic program and effective repair of DNA double-strand breaks were necessary for the wild-type behavior of matefin/SUN-1 aggregates.
Volume 6(11)
Pages e1001219
Published 2010-11-24
DOI 10.1371/journal.pgen.1001219
PMID 21124819
PMC PMC2991264
MeSH Animals Caenorhabditis elegans / cytology* Caenorhabditis elegans / metabolism* Caenorhabditis elegans Proteins / chemistry Caenorhabditis elegans Proteins / metabolism* Cell Cycle Proteins / metabolism* Cell Nucleus / metabolism Chromatin / metabolism Chromosomes / metabolism* Cytoskeleton / metabolism DNA Breaks, Double-Stranded Genotype Meiotic Prophase I* Mitosis Models, Biological Nuclear Proteins / metabolism* Protein Structure, Quaternary Protein Transport Receptors, Cytoplasmic and Nuclear / chemistry Receptors, Cytoplasmic and Nuclear / metabolism* Synaptonemal Complex / metabolism
IF 5.175
Times Cited 47
WOS Category GENETICS & HEREDITY
Resource
C.elegans tm2144