Dr. Rucha Kshirsagar

Profil

Zusammenfassung

Dr. Rucha Kshirsagar erforscht die molekularen Mechanismen der Chromosomensegregation und Meiose in Hefezellen, insbesondere die Struktur und Funktion von Kinetochor-Proteinen sowie Synaptonemal-Komplex-Komponenten. Ihre Expertise liegt in der biochemischen Charakterisierung von DNA-bindenden Proteinen und post-translationalen Modifikationen, die für die korrekte Chromosomensegregation und meiotische Rekombination entscheidend sind.

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Name

Dr. Rucha Kshirsagar

Titel

Dr.

Fakultät

Lebenswissenschaftliche Fakultät

Institut

Institut für Biologie

Arbeitsgruppe

Molekulare Zellbiologie

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28.6.2026, 01:08:37

• Strukturelle und funktionelle Analyse der Interaktion zwischen Kinetochor und zentrometrischem Chromatin in Saccharomyces cerevisiae

  Quelle ↗

  Förderer: DFG Eigene Stelle (Sachbeihilfe) Zeitraum: 10/2018 - 07/2023 Projektleitung: Dr. Rucha Kshirsagar

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• The HORMA domain: an evolutionarily conserved domain discovered in chromatin-associated proteins, has unanticipated diverse functions

  2014

  Gene · 26 Zitationen · DOI

• Probing the Potential Role of Non-B DNA Structures at Yeast Meiosis-Specific DNA Double-Strand Breaks

  2017

  Biophysical Journal · 22 Zitationen · DOI

• N-Terminal Disordered Domain of <i>Saccharomyces cerevisiae</i> Hop1 Protein Is Dispensable for DNA Binding, Bridging, and Synapsis of Double-Stranded DNA Molecules But Is Necessary for Spore Formation

  2013

  Biochemistry · 13 Zitationen · DOI

  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-protein 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 Δhop1 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-function relationships of Hop1 and help to further our understanding of its role in meiotic chromosome synapsis and recombination.

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