Chromosomes that have undergone crossing over in meiotic prophase must maintain sister chromatid cohesion somewhere along their length between the first and second meiotic divisions. Although many eukaryotes use the centromere as a site to maintain cohesion, the holocentric organism instead creates two chromosome domains of unequal length termed the short arm and long arm, which become the first and second site of cohesion loss at meiosis I and II. The mechanisms that confer distinct functions to the short and long arm domains remain poorly understood. Here, we show that phosphorylation of the synaptonemal complex protein SYP-1 is required to create these domains. Once crossover sites are designated, phosphorylated SYP-1 and PLK-2 become cooperatively confined to short arms and guide phosphorylated histone H3 and the chromosomal passenger complex to the site of meiosis I cohesion loss. Our results show that PLK-2 and phosphorylated SYP-1 ensure creation of the short arm subdomain, promoting disjunction of chromosomes in meiosis I.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5800814PMC
http://dx.doi.org/10.1083/jcb.201707161DOI Listing

Publication Analysis

Top Keywords

phosphorylation synaptonemal
8
synaptonemal complex
8
complex protein
8
protein syp-1
8
short arm
8
long arm
8
cohesion loss
8
phosphorylated syp-1
8
syp-1
4
syp-1 promotes
4

Similar Publications

This study investigated the effects of bisphenol A (BPA) and the involvement of nuclear estrogen receptors (ESR) on testicular energy metabolism and spermatogenesis in zebrafish. Testes were incubated with DMSO, 10 pM or 10μM BPA for 6 or 72h, with some samples pre-incubated with the ESRα/β antagonist ICI 182,780. Gene and protein expressions were analyzed using real-time PCR and Western blot, respectively.

View Article and Find Full Text PDF

The synaptonemal complex (SC) is a zipper-like protein structure that aligns homologous chromosome pairs and regulates recombination during meiosis. Despite its conserved appearance and function, how synapsis occurs between chromosome axes remains elusive. Here, we demonstrate that Polo-like kinases (PLKs) phosphorylate a single conserved residue in the disordered C-terminal tails of two paralogous SC subunits, SYP-5 and SYP-6, to establish an electrostatic interface between the SC central region and chromosome axes in C.

View Article and Find Full Text PDF

Chemically induced proximity reveals a Piezo-dependent meiotic checkpoint at the oocyte nuclear envelope.

Science

November 2024

California Institute for Quantitative Biosciences (QB3) and Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA, USA.

Sexual reproduction relies on robust quality control during meiosis. Assembly of the synaptonemal complex between homologous chromosomes (synapsis) regulates meiotic recombination and is crucial for accurate chromosome segregation in most eukaryotes. Synapsis defects can trigger cell cycle delays and, in some cases, apoptosis.

View Article and Find Full Text PDF

The synaptonemal complex (SC) is a zipper-like protein structure that aligns homologous chromosome pairs and regulates recombination during meiosis. Despite its conserved appearance and function, how synapsis occurs between chromosome axes remains elusive. Here, we demonstrate that Polo-like kinases (PLKs) phosphorylate a single conserved residue in the disordered C-terminal tails of two paralogous SC subunits, SYP-5 and SYP-6, to establish an electrostatic interface between the SC central region and chromosome axes in .

View Article and Find Full Text PDF

Meiosis is a form of cell division that is essential to sexually reproducing organisms and is therefore highly regulated. Each event of meiosis must occur at the correct developmental stage to ensure that chromosomes are segregated properly during both meiotic divisions. One unique meiosis-specific structure that is tightly regulated in terms of timing of assembly and disassembly is the synaptonemal complex (SC).

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!