Related Experiment Video
Updated: Mar 5, 2026

Investigation of Protein Recruitment to DNA Lesions Using 405 Nm Laser Micro-irradiation
Published on: March 20, 2018
Polo-like kinase-dependent phosphorylation of the synaptonemal complex protein SYP-4 regulates double-strand break
Saravanapriah Nadarajan1, Talley J Lambert2, Elisabeth Altendorfer1
1Department of Genetics, Harvard Medical School, Boston, United States.
Abstract:
The synaptonemal complex (SC) is an ultrastructurally conserved proteinaceous structure that holds homologous chromosomes together and is required for the stabilization of pairing interactions and the completion of crossover (CO) formation between homologs during meiosis I. Here, we identify a novel role for a central region component of the SC, SYP-4, in negatively regulating formation of recombination-initiating double-strand breaks (DSBs) via a feedback loop triggered by crossover designation in C. elegans. We found that SYP-4 is phosphorylated dependent on Polo-like kinases PLK-1/2. SYP-4 phosphorylation depends on DSB formation and crossover designation, is required for stabilizing the SC in pachytene by switching the central region of the SC from a more dynamic to a less dynamic state, and negatively regulates DSB formation. We propose a model in which Polo-like kinases recognize crossover designation and phosphorylate SYP-4 thereby stabilizing the SC and making chromosomes less permissive for further DSB formation.
More Related Videos
Related Concept Videos
Single-Strand DNA Binding Proteins
DNA Damage can Stall the Cell Cycle
DNA Damage Can Stall the Cell Cycle
Restarting Stalled Replication Forks
Fixing Double-strand Breaks
Fixing Double-strand Breaks

