The MUT9p kinase phosphorylates histone H3 threonine 3 and is necessary for heritable epigenetic silencing in
            <i>Chlamydomonas</i>

Casas-Mollano, J. Armando; Jeong, Byeong‐ryool; Xu, Jianping; Moriyama, Hideaki; Cerutti, Heriberto

doi:10.1073/pnas.0711310105

Cited by 61 publications

(113 citation statements)

References 47 publications

(86 reference statements)

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“…Reduction of global H3T3ph levels in the dm supports the proposition that MLK1 and MLK2, like their Chlamydomonas homolog MUT9 (28), are involved in histone H3T3 phosphorylation in vivo. However, MLK1 and MLK2 depletion did not completely abolish H3T3ph, indicating the existence of other kinases capable of targeting histone H3 at Thr 3 in Arabidopsis.…”

Section: Discussionsupporting

confidence: 56%

“…We previously demonstrated that the MUT9 Ser/Thr protein kinase is necessary for heritable epigenetic silencing in the alga Chlamydomonas (15,27,28). To address the role(s) of related protein kinases in land plants, we have now extended our studies to Arabidopsis.…”

Section: Resultsmentioning

confidence: 99%

“…The Chlamydomonas mut9 mutant is very sensitive to several abiotic stresses (27,28). Thus, we examined the response of the Arabidopsis dm to drought mimicking conditions.…”

Section: Resultsmentioning

confidence: 99%

“…We have previously characterized MUT9, a green algae/land plant-specific Ser/Thr protein kinase capable of phosphorylating H3T3 in the alga Chlamydomonas reinhardtii, and found that H3T3ph functions as a repressive epigenetic mark (15,27,28). In land plants, however, there is scant information on the existence of H3T3 phosphorylation in interphase cells and on its possible involvement in responses to abiotic stress.…”

Section: Significancementioning

confidence: 99%

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Osmotic stress induces phosphorylation of histone H3 at threonine 3 in pericentromeric regions of Arabidopsis thaliana

Wang

Casas-Mollano

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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132

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Histone phosphorylation plays key roles in stress-induced transcriptional reprogramming in metazoans but its function(s) in land plants has remained relatively unexplored. Here we report that an Arabidopsis mutant defective in At3g03940 and At5g18190, encoding closely related Ser/Thr protein kinases, shows pleiotropic phenotypes including dwarfism and hypersensitivity to osmotic/salt stress. The double mutant has reduced global levels of phosphorylated histone H3 threonine 3 (H3T3ph), which are not enhanced, unlike the response in the wild type, by drought-like treatments. Genome-wide analyses revealed increased H3T3ph, slight enhancement in trimethylated histone H3 lysine 4 (H3K4me3), and a modest decrease in histone H3 occupancy in pericentromeric/knob regions of wild-type plants under osmotic stress. However, despite these changes in heterochromatin, transposons and repeats remained transcriptionally repressed. In contrast, this reorganization of heterochromatin was mostly absent in the double mutant, which exhibited lower H3T3ph levels in pericentromeric regions even under normal environmental conditions. Interestingly, within actively transcribed protein-coding genes, H3T3ph density was minimal in 5′ genic regions, coincidental with a peak of H3K4me3 accumulation. This pattern was not affected in the double mutant, implying the existence of additional H3T3 protein kinases in Arabidopsis. Our results suggest that At3g03940 and At5g18190 are involved in the phosphorylation of H3T3 in pericentromeric/knob regions and that this repressive epigenetic mark may be important for maintaining proper heterochromatic organization and, possibly, chromosome function(s).epigenetics | heterochromatin | histone phosphorylation | abiotic stress | protein kinase

show abstract

Section: Discussionsupporting

confidence: 56%

Section: Resultsmentioning

confidence: 99%

“…The Chlamydomonas mut9 mutant is very sensitive to several abiotic stresses (27,28). Thus, we examined the response of the Arabidopsis dm to drought mimicking conditions.…”

Section: Resultsmentioning

confidence: 99%

Section: Significancementioning

confidence: 99%

See 2 more Smart Citations

Osmotic stress induces phosphorylation of histone H3 at threonine 3 in pericentromeric regions of Arabidopsis thaliana

Wang

Casas-Mollano

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

132

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“…In mammalian cells, casein kinase I is involved in vesicular trafficking, DNA repair, the circadian rhythm, and morphogenesis (McKay et al, 2001;Milne et al, 2001). In the alga Chlamydomonas, MUT9p, which is related to casein kinase I, is capable of phosphorylating H3 at threonine 3 (Casas-Mollano et al, 2008). The Arabidopsis genome encodes four proteins (MLK1, MLK2, MLK3, and MLK4) related to MUT9p (Cerutti and Casas-Mollano, 2009;Wang et al, 2015;Huang et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of Histone H2A at Serine 95: A Plant-Specific Mark Involved in Flowering Time Regulation and H2A.Z Deposition

Wang

Zhang

et al. 2017

Plant Cell

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Phosphorylation of histone H3 affects transcription, chromatin condensation, and chromosome segregation. However, the role of phosphorylation of histone H2A remains unclear. Here, we found that Arabidopsis thaliana MUT9P-LIKE-KINASE (MLK4) phosphorylates histone H2A on serine 95, a plant-specific modification in the histone core domain. Mutations in MLK4 caused late flowering under long-day conditions but no notable phenotype under short days. MLK4 interacts with CIRCADIAN CLOCK ASSOCIATED1 (CCA1), which allows MLK4 to bind to the GIGANTEA (GI) promoter. CCA1 interacts with YAF9a, a co-subunit of the Swi2/Snf2-related ATPase (SWR1) and NuA4 complexes, which are responsible for incorporating the histone variant H2A.Z into chromatin and histone H4 acetylase activity, respectively. Importantly, loss of MLK4 function led to delayed flowering by decreasing phosphorylation of H2A serine 95, along with attenuated accumulation of H2A.Z and the acetylation of H4 at GI, thus reducing GI expression. Together, our results provide insight into how phosphorylation of H2A serine 95 promotes flowering time and suggest that phosphorylation of H2A serine 95 modulated by MLK4 is required for the regulation of flowering time and is involved in deposition of the histone variant H2A.Z and H4 acetylation in Arabidopsis.

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Epigenetics in Algae

Tyler

2023

Epigenetics in Aquaculture

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The MUT9p kinase phosphorylates histone H3 threonine 3 and is necessary for heritable epigenetic silencing in Chlamydomonas

Cited by 61 publications

References 47 publications

Osmotic stress induces phosphorylation of histone H3 at threonine 3 in pericentromeric regions of Arabidopsis thaliana

Osmotic stress induces phosphorylation of histone H3 at threonine 3 in pericentromeric regions of Arabidopsis thaliana

Phosphorylation of Histone H2A at Serine 95: A Plant-Specific Mark Involved in Flowering Time Regulation and H2A.Z Deposition

Epigenetics in Algae

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