NAP1-RELATED PROTEIN1 and 2 negatively regulate H2A.Z abundance in chromatin in Arabidopsis

Wang, Yafei; Zhong, Zhenhui; Zhang, Yaxin; Xu, Linhao; Feng, Suhua; Rayatpisheh, Shima; Wohlschlegel, James A.; Wang, Zonghua; Jacobsen, Steven E.; Ausín, Israel

doi:10.1038/s41467-020-16691-x

Cited by 31 publications

(34 citation statements)

References 56 publications

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“…This splicing factor, which belongs to a zinc finger CCCH domain-containing protein that is proposed to be important in the salt tolerance of plants, is upregulated six-fold in quinoa GCs [ 33 ]. NAP1-related protein X2, which belongs to a family of chaperones and is involved in DNA repair, is also critical under stress conditions [ 34 ]. This protein was also upregulated under salt stress (two-fold).…”

Section: Resultsmentioning

confidence: 99%

Salinity Effects on Guard Cell Proteome in Chenopodium quinoa

Rasouli

Kiani‐Pouya

Shabala

et al. 2021

IJMS

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Epidermal fragments enriched in guard cells (GCs) were isolated from the halophyte quinoa (Chenopodium quinoa Wild.) species, and the response at the proteome level was studied after salinity treatment of 300 mM NaCl for 3 weeks. In total, 2147 proteins were identified, of which 36% were differentially expressed in response to salinity stress in GCs. Up and downregulated proteins included signaling molecules, enzyme modulators, transcription factors and oxidoreductases. The most abundant proteins induced by salt treatment were desiccation-responsive protein 29B (50-fold), osmotin-like protein OSML13 (13-fold), polycystin-1, lipoxygenase, alpha-toxin, and triacylglycerol lipase (PLAT) domain-containing protein 3-like (eight-fold), and dehydrin early responsive to dehydration (ERD14) (eight-fold). Ten proteins related to the gene ontology term “response to ABA” were upregulated in quinoa GC; this included aspartic protease, phospholipase D and plastid-lipid-associated protein. Additionally, seven proteins in the sucrose–starch pathway were upregulated in the GC in response to salinity stress, and accumulation of tryptophan synthase and L-methionine synthase (enzymes involved in the amino acid biosynthesis) was observed. Exogenous application of sucrose and tryptophan, L-methionine resulted in reduction in stomatal aperture and conductance, which could be advantageous for plants under salt stress. Eight aspartic proteinase proteins were highly upregulated in GCs of quinoa, and exogenous application of pepstatin A (an inhibitor of aspartic proteinase) was accompanied by higher oxidative stress and extremely low stomatal aperture and conductance, suggesting a possible role of aspartic proteinase in mitigating oxidative stress induced by saline conditions.

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Section: Resultsmentioning

confidence: 99%

Salinity Effects on Guard Cell Proteome in Chenopodium quinoa

Rasouli

Kiani‐Pouya

Shabala

et al. 2021

IJMS

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“…Distinct from the sole OsChz1, NAP1 is represented by a family of 5–6 members in rice or Arabidopsis 25 . Interestingly, a recent study showed that the Arabidopsis NRP1 and NRP2 negatively regulate H2A.Z abundance in chromatin and their loss causes over-accumulation of H2A.Z genome-wide, especially at heterochromatin regions normally depleted for H2A.Z in wild-type plants 34 . In parallel to specific functions, it is worth to note that redundant functions also exist between Chz1 and NAP1.…”

Section: Discussionmentioning

confidence: 99%

“…In contrast to the prediction by the anti-correlation rule, the decreased level of H2A.Z was observed without any detectable increase of DNA methylation in the rice oschz1 mutant (this study). Also, loss of H2A.Z in Arabidopsis has only a minor effect on DNA methylation 20 , and the nrp1-1nrp2-2 mutant displays H2A.Z accumulation but largely unaltered DNA methylation or even slight increases of CG/CHG methylation at some TEs 34 . Together, these studies support the proposition that the global anti-correlation between DNA methylation and H2A.Z is primarily caused by the exclusion of H2A.Z from methylated DNA 20 .…”

Section: Discussionmentioning

confidence: 99%

“…More recently, a DEF/Y motif located at the C-terminus of yChz1 was identified to directly engage the arginine residues within the H2A.Z L2 loop and a hydrophobic pocket in H2B for H2A.Z-H2B dimer interaction, enhancing the binding preference of yChz1 for H2A.Z-H2B 33 . Surprisingly, instead of working in H2A.Z incorporation, the Arabidopsis NAP1-RELATED PROTEIN1 (NRP1) and NRP2 were proposed to regulate gene expression by counteracting SWR1 to prevent excessive accumulation of H2A.Z in chromatin 34 .…”

Section: Introductionmentioning

confidence: 99%

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OsChz1 acts as a histone chaperone in modulating chromatin organization and genome function in rice

Luo

Yin

et al. 2020

Nat Commun

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While the yeast Chz1 acts as a specific histone-chaperone for H2A.Z, functions of CHZ-domain proteins in multicellular eukaryotes remain obscure. Here, we report on the functional characterization of OsChz1, a sole CHZ-domain protein identified in rice. OsChz1 interacts with both the canonical H2A-H2B dimer and the variant H2A.Z-H2B dimer. Within crystal structure the C-terminal region of OsChz1 binds H2A-H2B via an acidic region, pointing to a previously unknown recognition mechanism. Knockout of OsChz1 leads to multiple plant developmental defects. At genome-wide level, loss of OsChz1 causes mis-regulations of thousands of genes and broad alterations of nucleosome occupancy as well as reductions of H2A.Z-enrichment. While OsChz1 associates with chromatin regions enriched of repressive histone marks (H3K27me3 and H3K4me2), its loss does not affect the genome landscape of DNA methylation. Taken together, it is emerging that OsChz1 functions as an important H2A/H2A.Z-H2B chaperone in dynamic regulation of chromatin for higher eukaryote development.

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“…NRP proteins localized predominantly in the nucleus ( Gonzalez-Arzola et al, 2017 ) genetically interact with the SWR1 core components and link with H2A.Z. It is proposed that, in Arabidopsis , NRP proteins counteract the activity of the SWR1 complex and associate with the dynamic regulation of H2A.Z ( Wang et al, 2020 ).…”

Section: Chromatin Modifications In Plant Stress Tolerancementioning

confidence: 99%

Role of Chromatin Architecture in Plant Stress Responses: An Update

et al. 2021

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Sessile plants possess an assembly of signaling pathways that perceive and transmit environmental signals, ultimately resulting in transcriptional reprogramming. Histone is a key feature of chromatin structure. Numerous histone-modifying proteins act under different environmental stress conditions to help modulate gene expression. DNA methylation and histone modification are crucial for genome reprogramming for tissue-specific gene expression and global gene silencing. Different classes of chromatin remodelers including SWI/SNF, ISWI, INO80, and CHD are reported to act upon chromatin in different organisms, under diverse stresses, to convert chromatin from a transcriptionally inactive to a transcriptionally active state. The architecture of chromatin at a given promoter is crucial for determining the transcriptional readout. Further, the connection between somatic memory and chromatin modifications may suggest a mechanistic basis for a stress memory. Studies have suggested that there is a functional connection between changes in nuclear organization and stress conditions. In this review, we discuss the role of chromatin architecture in different stress responses and the current evidence on somatic, intergenerational, and transgenerational stress memory.

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NAP1-RELATED PROTEIN1 and 2 negatively regulate H2A.Z abundance in chromatin in Arabidopsis

Cited by 31 publications

References 56 publications

Salinity Effects on Guard Cell Proteome in Chenopodium quinoa

Salinity Effects on Guard Cell Proteome in Chenopodium quinoa

OsChz1 acts as a histone chaperone in modulating chromatin organization and genome function in rice

Role of Chromatin Architecture in Plant Stress Responses: An Update

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