Investigating the Interaction Between ZYG-1 606–706 and CHC-1201– 1681 in Centrosome Duplication

Department

Department of Biology

Document Type

Oral Presentation

Publication Date

4-17-2026

Abstract

Centrosome duplication is a tightly regulated process essential for accurate cell division, ensuring that each daughter cell inherits a single centrosome. In Caenorhabditis elegans, the serine/threonine kinase ZYG-1 plays a critical role in initiating centriole duplication by promoting procentriole formation and recruiting key assembly factors to the centrosome. Previous studies have shown that full-length ZYG-1 interacts with amino acids 1201–1681 of CHC-1, suggesting a potential functional relationship between these proteins in centrosome biology. This study aims to further investigate this interaction by determining whether a specific C- terminal region of ZYG-1 (amino acids 606–716) is sufficient to bind CHC-1 (amino acids 1201–1681). To address this, two plasmid constructs have been generated encoding ZYG-1(aa 606–716) and CHC-1(aa 1201– 1681). These constructs will be used in a yeast two-hybrid assay to test for protein–protein interaction. In this assay, the zyg-1 and chc-1 constructs will be co-expressed in yeast cells, and interaction between the proteins will be evaluated based on yeast growth on selective media. If the ZYG-1 C-terminal region interacts with CHC- 1, yeast growth is expected, indicating a positive interaction; conversely, lack of growth will suggest no interaction. Overall, this study will provide insight into the specific domains responsible for ZYG-1 and CHC-1 binding, thereby advancing our understanding of the molecular mechanisms underlying centrosome duplication. Elucidating these interactions will enhance our understanding of cell division and its roles in development and disease.

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