Abstract 1503 Hho1 as a posttranslational modification (PTM) regulator: Identifying protein-protein interactions between histone H3 and the Saccharomyces cerevisiae linker histone, Hho1

This research aims to enhance our understanding of Hho1 as a transcriptional regulator via direct protein-protein interaction with histone H3 (H3), detailing the contacts made between these two proteins. Current literature suggests that Hho1, and its homologs, play a critical role in gene repression and that Hho1 makes direct contact with H3 during this process. In order to further investigate how linker histone - H3 interactions regulate chromosomal dynamics, we employed the artificial crosslinking amino acid, p-benzoylphenylalanine (pBPA), which was installed through site-specific genetic encoding, to scan for H3 N-terminal tail - Hho1 binding.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109242
Primary Topic
Steroid Chemistry and Biochemistry
Type
article
Field-Weighted Citation Impact
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article

Abstract 1503 Hho1 as a posttranslational modification (PTM) regulator: Identifying protein-protein interactions between histone H3 and the Saccharomyces cerevisiae linker histone, Hho1

Joseph A. Campolo, Hanna Farzin
Journal of Biological Chemistry
Steroid Chemistry and Biochemistry
article

Abstract 1503 Hho1 as a posttranslational modification (PTM) regulator: Identifying protein-protein interactions between histone H3 and the Saccharomyces cerevisiae linker histone, Hho1

Joseph A. Campolo, Hanna Farzin
article en

Abstract

This research aims to enhance our understanding of Hho1 as a transcriptional regulator via direct protein-protein interaction with histone H3 (H3), detailing the contacts made between these two proteins. Current literature suggests that Hho1, and its homologs, play a critical role in gene repression and that Hho1 makes direct contact with H3 during this process. In order to further investigate how linker histone - H3 interactions regulate chromosomal dynamics, we employed the artificial crosslinking amino acid, p-benzoylphenylalanine (pBPA), which was installed through site-specific genetic encoding, to scan for H3 N-terminal tail - Hho1 binding.

Journal of Biological ChemistryVol. 301(5)
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Steroid Chemistry and Biochemistry
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