The C-Terminal Domain of Yeast High Mobility Group Protein HMO1 Mediates Lateral Protein Accretion and In-Phase DNA Bending

Xiao, Lijuan; Williams, Alan M; Grove, Anne

doi:10.1021/bi1003603

Cited by 28 publications

(32 citation statements)

References 45 publications

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“…The association of HMO1 with such junctions has also been implicated as one of the mechanisms by which HMO1 promotes the error-free DNA damage tolerance pathway by facilitating template switching (197), and it is consistent with the preferred binding of HMO1 to four-way DNA junctions compared to linear DNA (132). These functions of HMO1 require its C-terminal extension (197), shown to be required for DNA bending and bridging (133,134).…”

Section: Hmo1 Stabilizes Noncanonical Chromatin Structuresmentioning

confidence: 62%

“…The finding that chromatin-remodeling events associated with DSB repair occur faster in the absence of HMO1 points to a role for HMO1 in stabilizing chromatin. Notably, this stabilization requires the lysine-rich C-terminal domain, which was previously shown to be required for bridging separate DNA strands (134,177). A role for the basic extension in chromatin stabilization is corroborated by the increased sensitivity to MNase characteristic of chromatin isolated from both hmo1Δ cells and cells expressing HMO1 deleted for its C-terminal extension (198).…”

Section: Hmo1 and Dna Double-strand Break Repairmentioning

confidence: 66%

“…Deletion of the lysine-rich extension does not reduce the affinity for linear DNA, arguing against a direct interaction between the CTD and this type of DNA substrate. Instead, interactions between box A and the C-terminal extension were reported to induce a conformation that is required for in-phase DNA bending in vitro (133,134).…”

Section: Hmo1 Domain Organizationmentioning

confidence: 99%

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Yeast HMO1: Linker Histone Reinvented

Panday

Grove

2017

Microbiol Mol Biol Rev

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SUMMARY Eukaryotic genomes are packaged in chromatin. The higher-order organization of nucleosome core particles is controlled by the association of the intervening linker DNA with either the linker histone H1 or high mobility group box (HMGB) proteins. While H1 is thought to stabilize the nucleosome by preventing DNA unwrapping, the DNA bending imposed by HMGB may propagate to the nucleosome to destabilize chromatin. For metazoan H1, chromatin compaction requires its lysine-rich C-terminal domain, a domain that is buried between globular domains in the previously characterized yeast Saccharomyces cerevisiae linker histone Hho1p. Here, we discuss the functions of S. cerevisiae HMO1, an HMGB family protein unique in containing a terminal lysine-rich domain and in stabilizing genomic DNA. On ribosomal DNA (rDNA) and genes encoding ribosomal proteins, HMO1 appears to exert its role primarily by stabilizing nucleosome-free regions or “fragile” nucleosomes. During replication, HMO1 likewise appears to ensure low nucleosome density at DNA junctions associated with the DNA damage response or the need for topoisomerases to resolve catenanes. Notably, HMO1 shares with the mammalian linker histone H1 the ability to stabilize chromatin, as evidenced by the absence of HMO1 creating a more dynamic chromatin environment that is more sensitive to nuclease digestion and in which chromatin-remodeling events associated with DNA double-strand break repair occur faster; such chromatin stabilization requires the lysine-rich extension of HMO1. Thus, HMO1 appears to have evolved a unique linker histone-like function involving the ability to stabilize both conventional nucleosome arrays as well as DNA regions characterized by low nucleosome density or the presence of noncanonical nucleosomes.

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Section: Hmo1 Stabilizes Noncanonical Chromatin Structuresmentioning

confidence: 62%

Section: Hmo1 and Dna Double-strand Break Repairmentioning

confidence: 66%

Section: Hmo1 Domain Organizationmentioning

confidence: 99%

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Yeast HMO1: Linker Histone Reinvented

Panday

Grove

2017

Microbiol Mol Biol Rev

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“…They bind to the minor groove of DNA through a cluster of hydrophobic residues [32]. They may cover a long region of DNA through the formation of oligomers [33,34]. All these properties are consistent with specific binding to alternating AT clusters, in particular if they are unstabilized by torsional stress or cruciform formation: HMGB proteins always bind to distorted DNA regions.…”

Section: Homologue Chromosome Recognition In Meiosismentioning

confidence: 76%

The distribution of alternating AT sequences in eukaryotic genomes suggests a role in homologous chromosome recognition in meiosis

Subirana

Messeguer

2011

Journal of Theoretical Biology

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There are general features of chromosome dynamics, such as homologue recognition in early meiosis, which are expected to involve related sequence motifs in non-coding DNA, with a similar distribution in different species. A search for such motifs is presented here. It has been carried out with the CONREPP program. It has been found that short alternating AT sequences (10-20 bases) have a similar distribution in most eukaryotic organisms, with some exceptions related to unique meiotic features. All other microsatellite and repeat sequences vary significantly in different organisms. It is concluded that the unique structural features and uniform distribution of alternating AT sequences indicate that they may facilitate homologous chromosome pairing in the early preleptotene stage of meiosis. They may also play a role in the compaction of DNA in mitotic chromosomes.

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“…21) Furthermore, box A may interact with the carboxy-terminal tail of Hmo1 to bend DNA, 22) or with box A itself to form dimer or oligomer. 32) However, the significance of these properties of box A in vivo has not been verified.…”

Section: Discussionmentioning

confidence: 99%

Both HMG boxes in Hmo1 are essential for DNA binding in vitro and in vivo

Higashino

Shiwa

Yoshikawa

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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Hmo1, a member of the high mobility group B family proteins in Saccharomyces cerevisiae, associates with the promoters of ribosomal protein genes (RPGs) to direct accurate transcriptional initiation. Here, to identify factors involved in the binding of Hmo1 to its targets and the mechanism of Hmo1-dependent transcriptional initiation, we developed a novel reporter system using the promoter of the RPG RPS5. A genetic screen did not identify any factors that influence Hmo1 binding, but did identify a number of mutations in Hmo1 that impair its DNA binding activity in vivo and in vitro. These results suggest that Hmo1 binds to its target promoters autonomously without any aid of additional factors. Furthermore, characterization of Hmo1 mutants showed that the box A domain plays a pivotal role in DNA binding and may be required for the recognition of structural properties of target promoters that occur in native chromatin.

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The C-Terminal Domain of Yeast High Mobility Group Protein HMO1 Mediates Lateral Protein Accretion and In-Phase DNA Bending

Cited by 28 publications

References 45 publications

Yeast HMO1: Linker Histone Reinvented

Yeast HMO1: Linker Histone Reinvented

The distribution of alternating AT sequences in eukaryotic genomes suggests a role in homologous chromosome recognition in meiosis

Both HMG boxes in Hmo1 are essential for DNA binding in vitro and in vivo

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