High-capacity calcium-binding chitinase III from pomegranate seeds (<i>Punica granatum</i>Linn.) is located in amyloplasts

Lv, Chenyan; Masuda, Taro; Yang, Haixia; Sun, Lei; Zhao, Guanghua

doi:10.4161/psb.6.12.18147

Cited by 5 publications

(3 citation statements)

References 19 publications

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“…Recently, a proteomic study of pine and poplar has also suggested the role of class III acidic endochitinases during gravitropic response. These genes are associated with carbohydrate metabolism, and are also storage proteins (Azri et al, 2009; Herrera et al, 2010), residing at the starch granules of the amyloplast, which is known to be involved in sensing the direction of gravity to promote downward gravitropic curvature (Lv et al, 2011). In plants, carbonic anhydrases are also involved in carbohydrate metabolism and photomorphogenesis (Wang et al, 2012).…”

Section: Peg Gravitropism: Deciphering the Molecular Pathwaysmentioning

confidence: 99%

Peg Biology: Deciphering the Molecular Regulations Involved During Peanut Peg Development

et al. 2019

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Peanut or groundnut is one of the most important legume crops with high protein and oil content. The high nutritional qualities of peanut and its multiple usage have made it an indispensable component of our daily life, in both confectionary and therapeutic food industries. Given the socio-economic significance of peanut, understanding its developmental biology is important in providing a molecular framework to support breeding activities. In peanut, the formation and directional growth of a specialized reproductive organ called a peg, or gynophore, is especially relevant in genetic improvement. Several studies have indicated that peanut yield can be improved by improving reproductive traits including peg development. Therefore, we aim to identify unifying principles for the genetic control, underpinning molecular and physiological basis of peg development for devising appropriate strategy for peg improvement. This review discusses the current understanding of the molecular aspects of peanut peg development citing several studies explaining the key mechanisms. Deciphering and integrating recent transcriptomic, proteomic, and miRNA-regulomic studies provide a new perspective for understanding the regulatory events of peg development that participate in pod formation and thus control yield.

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Section: Peg Gravitropism: Deciphering the Molecular Pathwaysmentioning

confidence: 99%

Peg Biology: Deciphering the Molecular Regulations Involved During Peanut Peg Development

et al. 2019

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“…Class III chitinases belong to the GH18 endochitinase family (Adrangi and Faramarzi 2013). Machi3-1 is an acidic class III chitinase (calculated isoelectric point is 4.4), which shows strong sequence similarity (66.4%) to the wellcharacterized class III chitinases as PSC (pomegranate seed chitinase) and Hevamine (64.18%) (Terwisscha Van Scheltinga et al 1996;Lv et al 2011;Masuda et al 2015). The critical catalytic amino acids and the cis-peptides (involved in chitin binding) are all conserved (Fig.…”

Section: A Class III Chitinase-like Protein Accumulates In the Nectarmentioning

confidence: 99%

Nectar- and stigma exudate-specific expression of an acidic chitinase could partially protect certain apple cultivars against fire blight disease

Kurilla

Tóth²,

Dorgai³

et al. 2019

Planta

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“…We assigned magnesium to the major electron densities having proper coordination environment on the surface of PSC, because high concentration (0.2 M) of magnesium salts was contained in the crystallization condition. Since the PSC associates calcium ions with low affinity, 11,12) it is possible that magnesium ions can associate with PSC in such extreme conditions. There are at least 13 magnesium ions clearly identified in our structural model.…”

Section: Metal Association To Pscmentioning

confidence: 99%

Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity

Masuda

Zhao

Mikami

2015

Bioscience, Biotechnology, and Biochemistry

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Chitinase hydrolyzes the β-1,4-glycosidic bond in chitin. In higher plants, this enzyme has been regarded as a pathogenesis-related protein. Recently, we identified a class III chitinase, which functions as a calcium storage protein in pomegranate (Punica granatum) seed (PSC, pomegranate seed chitinase). Here, we solved a crystal structure of PSC at 1.6 Å resolution. Although its overall structure, including the structure of catalytic site and non-proline cis-peptides, was closely similar to those of other class III chitinases, PSC had some unique structural characteristics. First, there were some metal-binding sites with coordinated water molecules on the surface of PSC. Second, many unconserved aspartate residues were present in the PSC sequence which rendered the surface of PSC negatively charged. This acidic electrostatic property is in contrast to that of hevamine, well-characterized plant class III chitinase, which has rather a positively charged surface. Thus, the crystal structure provides a clue for metal association property of PSC.

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High-capacity calcium-binding chitinase III from pomegranate seeds (Punica granatumLinn.) is located in amyloplasts

Cited by 5 publications

References 19 publications

Peg Biology: Deciphering the Molecular Regulations Involved During Peanut Peg Development

Peg Biology: Deciphering the Molecular Regulations Involved During Peanut Peg Development

Nectar- and stigma exudate-specific expression of an acidic chitinase could partially protect certain apple cultivars against fire blight disease

Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity

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