Plants water soluble chlorophyll binding proteins act as enzyme-inhibitor pair

Gholizadeh, Ashraf

doi:10.1134/s1021443717010095

Cited by 4 publications

(2 citation statements)

References 21 publications

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“…The most structurally studied plant proteins containing a DUF538 domain are from Celosia cristata, which show partial structural homology to BPI (bactericidal/permeability increasing) proteins of the mammalian innate immune system [17]. DUF538 domaincontaining proteins from C. cristata also exhibited a binding capacity and esterase-type hydrolytic activity towards bacterial lipopolysaccharides and chlorophyll molecules [19,26,27] and a methylesterase activity towards pectin molecules [28], suggesting a probable cooperation between DUF538 and pectin methylesterase protein families in cell wall-associated defense responses in plants.…”

Section: Introductionmentioning

confidence: 99%

Overexpression of DUF538 from Wild Arachis Enhances Plant Resistance to Meloidogyne spp.

et al. 2021

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DUF538 proteins belong to a large group of uncharacterized protein families sharing the highly conserved Domain of Unknown Function (DUF). Attention has been given to DUF538 domain-containing proteins due to changes in their gene expression behavior and protein abundance during plant development and responses to stress. Putative roles attributed to DUF538 in plants under abiotic and biotic constraints include involvement in cell redox balance, chlorophyll breakdown and pectin degradation. Our previous transcriptome studies suggested that DUF538 is also involved in the resistance responses of wild Arachis species against the highly hazardous root-knot nematodes (RKNs). To clarify the role of the AsDUF538 gene from the wild peanut relative Arachis stenosperma in this interaction, we analyzed the effect of its overexpression on RKN infection in peanut and soybean hairy roots and Arabidopsis transgenic plants. AsDUF538 overexpression significantly reduced the infection in all three heterologous plant systems against their respective RKN counterparts. The distribution of AsDUF538 transcripts in RKN-infected Arachis roots and the effects of AsDUF538 overexpression on hormonal pathways and redox system in transgenic Arabidopsis were also evaluated. This is the first time that a DUF538 gene is functionally validated in transgenic plants and the earliest report on its role in plant defense against RKNs.

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Section: Introductionmentioning

confidence: 99%

Overexpression of DUF538 from Wild Arachis Enhances Plant Resistance to Meloidogyne spp.

et al. 2021

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“…Interestingly, following finding the similarity of DUF538 to type 1 water soluble chlorophyll binding protein (WSCP 1), the binding ability of DUF538 to chlorophyll molecules was also predicted in plant system. DUF538 proteins were shown to contain esterase-type hydrolytic domain that is able to hydrolyze chlorophyll molecules in vitro (Gholizadeh 2017(Gholizadeh , 2018.…”

Section: Introductionmentioning

confidence: 99%

Pectin methylesterase activity of plant DUF538 protein superfamily

Gholizadeh

2020

Physiol Mol Biol Plants

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DUF538 (domain of unknown function 538) proteins are known as a group of putative hypothetical proteins in a wide range of plant species. They have been identified from some plants challenged with various environmental stresses. However, a little is known about their functional properties. They have been newly predicted to have binding capacity and esterase-type hydrolytic activity towards bacterial lipopolysaccharides and chlorophyll molecules as carboxylic compounds in plants. In the present study, the binding ability and the methylesterase activity of DUF538 proteins towards pectin molecules were also predicted. Their similarities to pectin methylesterases and their binding ability to pectin molecule were predicted using bioinformatic tools as well as the experimental method. A probable cooperation was speculated between DUF538 and pectin methylesterase protein families in cell wall associated defense responses in plants.

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