N-Terminal Disordered Domain of Saccharomyces cerevisiae Hop1 Protein Is Dispensable for DNA Binding, Bridging, and Synapsis of Double-Stranded DNA Molecules But Is Necessary for Spore Formatio
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- 作者：Krishnendu Khan ; T. P. Vipin Madhavan ; Rucha Kshirsagar ; Kannan N. Boosi ; Parag Sadhale ; K. Muniyappa
- 刊名：Biochemistry
- 出版年：2013
- 出版时间：August 6, 2013
- 年：2013
- 卷：52
- 期：31
- 页码：5265-5279
- 全文大小：878K
- 年卷期：v.52,no.31(August 6, 2013)
- ISSN：1520-4995
文摘
The cytological architecture of the synaptonemal complex (SC), a meiosis-specific proteinaceous structure, is evolutionarily conserved among eukaryotes. However, little is known about the biochemical properties of SC components or the mechanisms underlying their roles in meiotic chromosome synapsis and recombination. Functional analysis of Saccharomyces cerevisiae Hop1, a key structural component of SC, has begun to reveal important insights into its function in interhomolog recombination. Previously, we showed that Hop1 is a structure-specific DNA-binding protein, exhibits higher binding affinity for the Holliday junction, and induces structural distortion at the core of the junction. Furthermore, Hop1 promotes DNA condensation and intra- and intermolecular synapsis between duplex DNA molecules. Here, we show that Hop1 possesses a modular domain organization, consisting of an intrinsically disordered N-terminal domain and a protease-resistant C-terminal domain (Hop1CTD). Furthermore, we found that Hop1CTD exhibits strong homotypic as well as heterotypic protein鈥損rotein interactions, and its biochemical activities were similar to those of the full-length Hop1 protein. However, Hop1CTD failed to complement the meiotic recombination defects of the 螖hop1 strain, indicating that both N- and C-terminal domains of Hop1 are essential for meiosis and spore formation. Altogether, our findings reveal novel insights into the structure鈥揻unction relationships of Hop1 and help to further our understanding of its role in meiotic chromosome synapsis and recombination.