Faculty Advisor

Dr. Michael Parra

Start Date

27-4-2021 12:00 AM

End Date

27-4-2021 12:00 AM

Description

In eukaryotic genomes, DNA is packaged with a group of proteins called histones to form chromatin. The basic repeating subunit of chromatin, the nucleosome core particle (NCP), is made up of two copies each of the canonical histones H2A, H2B, H3, and H4. Though compaction allows large amounts of DNA to fit into the relatively small space of the nucleus, it establishes a physical barrier to the DNA template. Because of their close association with DNA, histones play integral roles in DNA-templated processes (e.g. transcription, DNA repair, and DNA replication). The N-terminal domain of histones H2B (amino acids 3-37) makes close and intimate contact with DNA and has been shown to repress the transcription of a large set of genes in the yeast genome. Indeed, the relevant residues on H2B comprise a small portion of the N-terminal ‘tail’ (amino acids 30-37). This domain is termed the histone H2B repression (HBR) domain. Previous studies have implicated these domains in regulating transcription as well as the cellular response to DNA damage. Here we define a novel role for this domain in regulating cellular division, DNA double-strand break repair, and DNA replication

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Biochemistry Commons

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Apr 27th, 12:00 AM Apr 27th, 12:00 AM

Histone H2B Repression (HBR) Domain Regulates Cell Cycle Progression and DNA Damage Response in the Yeast Saccharomyces cerevisiae

In eukaryotic genomes, DNA is packaged with a group of proteins called histones to form chromatin. The basic repeating subunit of chromatin, the nucleosome core particle (NCP), is made up of two copies each of the canonical histones H2A, H2B, H3, and H4. Though compaction allows large amounts of DNA to fit into the relatively small space of the nucleus, it establishes a physical barrier to the DNA template. Because of their close association with DNA, histones play integral roles in DNA-templated processes (e.g. transcription, DNA repair, and DNA replication). The N-terminal domain of histones H2B (amino acids 3-37) makes close and intimate contact with DNA and has been shown to repress the transcription of a large set of genes in the yeast genome. Indeed, the relevant residues on H2B comprise a small portion of the N-terminal ‘tail’ (amino acids 30-37). This domain is termed the histone H2B repression (HBR) domain. Previous studies have implicated these domains in regulating transcription as well as the cellular response to DNA damage. Here we define a novel role for this domain in regulating cellular division, DNA double-strand break repair, and DNA replication

 

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