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World J Biol Chem. Aug 12, 2024; 15(1): 97938
Published online Aug 12, 2024. doi: 10.4331/wjbc.v15.i1.97938
Hmo1: A versatile member of the high mobility group box family of chromosomal architecture proteins
Xin Bi
Xin Bi, Department of Biology, University of Rochester, Rochester, NY 14627, United States
Author contributions: Bi X designed the overall concept and wrote the manuscript.
Conflict-of-interest statement: The authors declare that they have no conflict of interest.
Open-Access: This article is an open-access article that was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution NonCommercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: https://creativecommons.org/Licenses/by-nc/4.0/
Corresponding author: Xin Bi, PhD, Professor, Department of Biology, University of Rochester, 500 Joseph C, Wilson Boulevard, Rochester, NY 14627, United States. xin.bi@rochester.edu
Received: June 13, 2024
Revised: July 21, 2024
Accepted: August 1, 2024
Published online: August 12, 2024
Processing time: 56 Days and 5.1 Hours
Core Tip

Core Tip: The evolutionarily conserved high mobility group box (HMGB) family proteins are major non-histone chromosomal architectural factors characterized by one or more HMGB motifs that bind DNA in a sequence nonspecific fashion. They play a major role in chromatin dynamics that impact various cellular functions. The Saccharomyces cerevisiae (yeast hereafter) HMGB protein Hmo1 contains two HMGB motifs. Hmo1 functions in multiple cellular processes including genome maintenance, chromatin dynamics, gene transcription, and DNA damage response. However, the underlying mechanisms have only been partially elucidated. Moreover, to what extent Hmo1 functionally resembles its mammalian counterparts has not been fully addressed. Recent studies revealed that Hmo1 binds and destabilizes/disrupts nucleosome similarly as well-characterized human HMGB proteins and that Hmo1 plays a role in maintaining a topological architecture of genes in the yeast genome.