Calmodulin-Mediated Signal Transduction Pathways in Arabidopsis Are Fine-Tuned by Methylation

Banerjee, Joydeep; Magnani, Roberta; Nair, Meera G.; Dirk, Lynnette M.A.; DeBolt, Seth; Maiti, Indu B.; Houtz, Robert L.

doi:10.1105/tpc.113.119115

Cited by 33 publications

(42 citation statements)

References 83 publications

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“…The cml9 mutant exhibits hypersensitivity to ABA and enhanced tolerance to stress and drought (Magnan et al 2008). CaM methylation is also involved in the early growth of Arabidopsis and responds to ABA, cold, and heat stress during germination (Banerjee et al 2013). As mentioned earlier, the calmodulin-binding transcriptional activator CAMTA3 is involved in the regulation of freezing tolerance (Doherty et al 2009).…”

Section: Second Messengers Integrate Cold and Aba Signallingmentioning

confidence: 96%

ABA Regulation of the Cold Stress Response in Plants

Shi

Yang

2014

Abscisic Acid: Metabolism, Transport and Signaling

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Low temperature is a major environmental factor that limits plant growth, productivity, and distribution. To ensure optimal growth and survival, plants must respond and adapt to cold stress using a variety of biochemical and physiological processes. Currently, the most thoroughly understood cold-signalling pathway is the C-repeat binding factor/DRE-binding factor (CBF/DREB) transcriptional regulatory cascade. Abscisic acid (ABA) is an important stress hormone in plants that has been demonstrated to be involved in the cold stress response through regulation of a set of specific stress-responsive genes. The current consensus is that both ABA-dependent and ABA-independent pathways are involved in plant responses to cold stress. This chapter summarises recent progress made in our understanding of cold signalling and the role of ABA in cold stress, and we also address cross talk between ABA and several classical phytohormones that integrate with cold signalling.

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Section: Second Messengers Integrate Cold and Aba Signallingmentioning

confidence: 96%

ABA Regulation of the Cold Stress Response in Plants

Shi

Yang

2014

Abscisic Acid: Metabolism, Transport and Signaling

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“…Among them, [36]. Calmodulin can undergo post-translation modifications, such as phosphorylation, acetylation, methylation and proteolytic cleavage, each of which has potential to modulate its actions [37]. For absence of clues about connection between calmodulin and the 286 bp fragment, a possibility is that calmodulin might form a complex with other protein or proteins to fulfil the regulatory responsibilities.…”

Section: Discussionmentioning

confidence: 99%

In Search of Regulators of <i>LeSPL-CNR</i> by South-Western Blotting and Yeast One-Hybrid Library Screening System

Wang¹,

Ye²,

Wang³

et al. 2018

AJPS

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LeSPL-CNR is a crucial transcription factor for fruit ripening of Solanum lycopersicum. The cnr (colorless non-ripening) epimutation resulted from hypermethylation in a 286 bp region of LeSPL-CNR promoter inhibits normal fruit ripening. In present study, potential regulators of LeSPL-CNR, which could bind to the specific 286 bp region, were screened via south-western blotting and yeast one-hybrid (Y1H) library screening system. Results indicated that a total of 13 and 19 candidate proteins were acquired respectively, and both ribulose-1,5-bisphosphate carboxylase/oxygenase and 40S ribosomal protein were identified by two methods. These would provide some information for revealing roles of DNA methylation and the regulatory mechanism for LeSPL-CNR.

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“…Possibly, either unknown proteins or mechanisms are involved in exposing specific regions of OsCML3 for binding to OsHMGB1, or that post-translational modification of OsHMGB1 or OsCML3 facilitates the interaction. The latter scenario has been observed from the phosphorylation of maize HMGB1 by protein kinase CK2 that abolishes its interaction with transcription factor Dof2 and the stimulation of Dof2 DNA binding [53] or the methylation and phosphorylation of CaM, which affect its activity for binding to target proteins [54][55][56].…”

Section: Discussionmentioning

confidence: 99%

C-terminal extension of calmodulin-like 3 protein from <italic>Oryza sativa</italic> L.: interaction with a high mobility group target protein

Chinpongpanich

Phean-o-pas

Thongchuang

et al. 2015

ABBS

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A large number of calmodulin-like (CML) proteins are present in plants, but there is little detailed information on the functions of these proteins in rice (Oryza sativa L.). Here, the CML3 protein from rice (OsCML3) and its truncated form lacking the C-terminal extension (OsCML3m) were found to exhibit a Ca 2+ -binding property and subsequent conformational change, but the ability to bind the CaM kinase II peptide was only observed for OsCML3m. Changes in their secondary structure upon Ca 2+ -binding measured by circular dichroism revealed that OsCML3m had a higher helical content than OsCML3. Moreover, OsCML3 was mainly localized in the plasma membrane, whereas OsCML3m was found in the nucleus. The rice high mobility group B1 (OsHMGB1) protein was identified as one of the putative OsCML3 target proteins. Bimolecular fluorescence complementation analysis revealed that OsHMGB1 bound OsCML3, OsCML3m or OsCML3s (cysteine to serine mutation at the prenylation site) in the nucleus presumably through the methionine and phenylalaninerich hydrophobic patches, confirming that OsHMGB1 is a target protein in planta. The effect of OsCML3 or OsCML3m on the DNA-binding ability of OsHMGB1 was measured using an electrophoretic mobility shift assay. OsCML3m decreased the level of OsHMGB1 binding to pUC19 doublestranded DNA whereas OsCML3 did not. Taken together, OsCML3 probably provides a mechanism for manipulating the DNA-binding ability of OsHMGB1 in the nucleus and its C-terminal extension provides an intracellular Ca 2+ regulatory switch.

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Calmodulin-Mediated Signal Transduction Pathways in Arabidopsis Are Fine-Tuned by Methylation

Cited by 33 publications

References 83 publications

ABA Regulation of the Cold Stress Response in Plants

ABA Regulation of the Cold Stress Response in Plants

In Search of Regulators of <i>LeSPL-CNR</i> by South-Western Blotting and Yeast One-Hybrid Library Screening System

C-terminal extension of calmodulin-like 3 protein from <italic>Oryza sativa</italic> L.: interaction with a high mobility group target protein

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Calmodulin-Mediated Signal Transduction Pathways in Arabidopsis Are Fine-Tuned by Methylation

Cited by 33 publications

References 83 publications

ABA Regulation of the Cold Stress Response in Plants

ABA Regulation of the Cold Stress Response in Plants

In Search of Regulators of &lt;i&gt;LeSPL-CNR&lt;/i&gt; by South-Western Blotting and Yeast One-Hybrid Library Screening System

C-terminal extension of calmodulin-like 3 protein from &lt;italic&gt;Oryza sativa&lt;/italic&gt; L.: interaction with a high mobility group target protein

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Product

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In Search of Regulators of <i>LeSPL-CNR</i> by South-Western Blotting and Yeast One-Hybrid Library Screening System

C-terminal extension of calmodulin-like 3 protein from <italic>Oryza sativa</italic> L.: interaction with a high mobility group target protein