Publications by authors named "K H KLARE"
Centromeres are unique chromosomal loci that promote the assembly of kinetochores, macromolecular complexes that bind spindle microtubules during mitosis. In most organisms, centromeres lack defined genetic features. Rather, they are specified epigenetically by a centromere-specific histone H3 variant, CENP-A.
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- Chromosomes play a crucial role in carrying genetic material, and kinetochores help ensure their accurate transfer during cell division by connecting them to the mitotic spindle.
- Kinetochores are complex structures made up of various protein subunits, with the inner kinetochore formed by a group of centromeric proteins (CCAN), and the outer kinetochore created by the KMN network, which binds microtubules.
- The study reveals how a specific CCAN subcomplex (CHIKMLN) increases the binding selectivity for CENP-A nucleosomes, forming a strong link between CENP-A and microtubules, and sheds light on the organization and function of kinetocho
G-quadruplex (G4)-forming genomic sequences, including telomeres, represent natural replication fork barriers. Stalled replication forks can be stabilized and restarted by homologous recombination (HR), which also repairs DNA double-strand breaks (DSBs) arising at collapsed forks. We have previously shown that HR facilitates telomere replication.
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- Kinetochores are essential protein complexes that form on centromeres, binding to spindle microtubules to ensure proper chromosome separation during cell division.
- The study focuses on CENP-C, a key component of the constitutive centromere-associated network (CCAN), which facilitates the assembly of kinetochores and connects centromeres with microtubules.
- The researchers discovered that the PEST domain in CENP-C directly interacts with the CENP-HIKM subcomplex, revealing how CENP-C helps target other CCAN subunits to the kinetochore, highlighting its role in the overall assembly process.
Although our understanding of centromere maintenance, marked by the histone H3 variant CenH3(CENP-A) in most eukaryotes, has progressed, the mechanism underlying the de novo formation of centromeres remains unclear. We used a synthetic system to dissect how CenH3(CENP-A) contributes to the accumulation of CENP-C and CENP-T, two key components that are necessary for the formation of functional kinetochores. We find that de novo CENP-T accumulation depends on CENP-C and that recruitment of these factors requires two domains in CenH3(CENP-A): the HJURP-binding region (CATD) and the CENP-C-binding region (CAC).
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