Mutations in Glucan, Water Dikinase Affect Starch Degradation and Gametophore Development in the Moss Physcomitrella patens

Mdodana, Ntombizanele T.; Jewell, Jonathan F.; Phiri, Ethel E.; Smith, Marthinus L.; Oberlander, Kenneth C.; Mahmoodi, Saire; Kossmann, Jens; Lloyd, J. R.

doi:10.1038/s41598-019-51632-9

Cited by 8 publications

(8 citation statements)

References 81 publications

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“…Mutations in Arabidopsis Starch Synthase III were found to increase enzyme expression level and its activity [57]. Numerous studies documented that mutations in gene resulted in increased enzyme activity [39,58]. In the present study, molecular simulation results revealed that these mutations are favoring the bonding between the enzyme and its cofactor by stabilizing the structure, decreasing the binding free energy, and increasing its binding site residues.…”

Section: Discussionmentioning

confidence: 47%

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Ethylene Biosynthesis Inhibition Combined with Cyanide Degradation Confer Resistance to Quinclorac in Echinochloa crus-galli var. mitis

Haq

Zhang

Wei

et al. 2020

IJMS

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Echinochloa crus-galli var. mitis has rarely been reported for herbicide resistance, and no case of quinclorac resistance has been reported so far. Synthetic auxin-type herbicide quinclorac is used extensively to control rice weeds worldwide. A long history of using quinclorac in Chinese rice fields escalated the resistance in E. crus-galli var. mitis against this herbicide. Bioassays in Petri plates and pots exhibited four biotypes that evolved into resistance to quinclorac ranking as JS01-R > AH01-R > JS02-R > JX01-R from three provinces of China. Ethylene production in these biotypes was negatively correlated with resistance level and positively correlated with growth inhibition. Determination of the related ethylene response pathway exhibited resistance in biotypes that recorded a decline in 1-aminocyclopropane-1-carboxylic acid (ACC) content, ACC synthase oxidase activities, and less inducible ACS and ACO genes expressions than the susceptible biotype, suggesting that there was a positive correlation between quinclorac resistance and ethylene biosynthesis inhibition. Cyanides produced during the ethylene biosynthesis pathway mainly degraded by the activity of β-cyanoalanine synthase (β-CAS). Resistant biotypes exhibited higher β-CAS activity than the susceptible ones. Nucleotide changes were found in the EcCAS gene of resistant biotypes as compared to sensitive ones that caused three amino acid substitutions (Asn-105-Lys, Gln-195-Glu, and Gly-298-Val), resulting in alteration of enzyme structure, increased binding residues in the active site with its cofactor, and decreased binding free energy; hence, its activity was higher in resistant biotypes. Moreover, these mutations increased the structural stability of the enzyme. In view of the positive correlation between ethylene biosynthesis inhibition and cyanide degradation with resistance level, it is concluded that the alteration in ethylene response pathway or at least variation in ACC synthase and ACC oxidase enzyme activities—due to less relative expression of ACS and ACO genes and enhanced β-CAS activity, as well as mutation and increased relative expression of EcCAS gene—can be considered as a probable mechanism of quinclorac resistance in E. crus-galli var. mitis.

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Section: Discussionmentioning

confidence: 47%

“…Contrarily, quinclorac resistance in E. phyllopogan might solely depend on ethylene biosynthesis inhibition rather than cyanide degradation [38]. However, it is a fact that mutations can increase enzyme activity [39]. β-CAS mainly depends upon pyridoxal phosphate (PLP) for its activity [35].…”

Section: Introductionmentioning

confidence: 99%

Ethylene Biosynthesis Inhibition Combined with Cyanide Degradation Confer Resistance to Quinclorac in Echinochloa crus-galli var. mitis

Haq

Zhang

Wei

et al. 2020

IJMS

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“…Two copies of the GWD gene were also observed in some angiosperm families, suggesting a divergence in function between GWD1 and GWD2 paralogs of these species. A different functional evolution may exist regarding PWD, another paralog of GWD, as described [ 2 ], but not the focus of current study. In M. esculenta , GWD2 and the other GWD isoforms were implicated by Zhou et al [ 45 ] in storage starch degradation, due to increased expressions during post-harvest physiological deterioration where its activity was linked to seed development in A. thaliana and not the degradation of transitory starch at night [ 8 ].…”

Section: Discussionmentioning

confidence: 98%

“…The plastid-localized alpha-glucan water dikinase ( GWD ) gene is encoded by the nuclear genome and its products catalyzes reactions responsible for starch phosphorylation, an essential step in the de novo biosynthesis of this polysaccharide [ 1 ]. Generally, two plastidial isoforms of GWD; GWD1 (EC 2.7.9.4) and phosphoglucan water dikinase (PWD) or GWD3 (PWD; EC 2.7.9.5) have been identified in most plants [ 2 ]. The dikinase mechanism of GWD and PWD involve autophosphorylation of the catalytic histidine by the β-phosphate of ATP, and the transfer of β-phosphate from the stable phosphohistidine to either the C3 or C6 position of the glucosyl residue of starch, while the γ -phosphate is transferred to water [ 1 , 3 ].…”

Section: Introductionmentioning

confidence: 99%

“…Furthermore, GWD1 and PWD have been linked to starch degradation. While less is known about this phenomenon, the model for plastidial starch degradation starts with its phosphorylation, orchestrated by the activities of GWD1 and PWD [ 2 ]. In addition to the pervasive GWD isoforms, another isoform, GWD2, uniquely localized in the cytosol, has been identified [ 8 ].…”

Section: Introductionmentioning

confidence: 99%

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Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants

Adegbaju

Morenikeji

Borrego

et al. 2020

Plants

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The alpha-glucan water dikinase (GWD) enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation. The high phosphate content in stored starch has great industrial value, due to its physio–chemical properties making it more versatile, although the phosphate content of stored starch varies depending on the botanical source. In this study, we used various computational approaches to gain insights into the evolution of the GWD protein in 48 plant species with possible roles in enzyme function and alteration of phosphate content in their stored starch. Our analyses identified deleterious mutations, particularly in the highly conserved 5 aromatic amino acid residues in the dual tandem carbohydrate binding modules (CBM-45) of GWD protein in C. zofingiensis, G. hirsutum, A. protothecoides, P. miliaceum, and C. reinhardtii. These findings will inform experimental designs for simultaneous repression of genes coding for GWD and the predicted interacting proteins to elucidate the role this enzyme plays in starch degradation. Our results reveal significant diversity in the evolution of GWD enzyme across plant species, which may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments.

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The nuclear GUCT domain-containing DEAD-box RNA helicases govern gametophytic and sporophytic development in Physcomitrium patens

et al. 2021

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Key messageIn Physcomitrium patens, PpRH1/PpRH2 are GUCT-domain-containing DEAD-BOX RNA helicases localize to the nucleus. They are implicated in cell and tissue development in all stages of the moss life cycle. Abstract The DEAD-box-containing RNA helicase family encompasses a large and functionally important group of enzymes involved in cellular processes committed to the metabolism of RNA, including its transcription, processing, transport, translation and decay. Studies indicate this protein family has implied roles in plant vegetative and reproductive developmental processes as well as response to environmental stresses such has cold and high salinity. We focus here on a small conserved sub-group of GUCT domain-containing RNA helicase in the moss Physcomitrium patens. Phylogenetic analysis shows that RNA helicases containing the GUCT domain form a distinct conserved clade across the green lineage. In this clade, the P. patens genome possesses two closely related paralogues RNA helicases predicted to be nuclear, PpRH1 and PpRH2. Using in-locus gene fluorescent tagging we show that PpRH1 is localized to the nucleus in protonema. Analysis of PpRH1 and PpRH2 deletions, individually and together, indicates their potential roles in protonema, gametophore and sporophyte cellular and tissue development in P. patens. Additionally, the ultrastructural analysis of phyllid chloroplasts in Δrh2 and Δrh1/2 shows distinct starch granule accumulation under standard growth conditions associated with changes in photosynthetic activity parameters. We could not detect effects of either temperature or stress on protonema growth or PpRH1 and PpRH2 expression. Together, these results suggest that nuclear GUCT-containing RNA helicases play a role primarily in developmental processes directly or indirectly linked to photosynthesis activity in the moss P. patens.

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Mutations in Glucan, Water Dikinase Affect Starch Degradation and Gametophore Development in the Moss Physcomitrella patens

Cited by 8 publications

References 81 publications

Ethylene Biosynthesis Inhibition Combined with Cyanide Degradation Confer Resistance to Quinclorac in Echinochloa crus-galli var. mitis

Ethylene Biosynthesis Inhibition Combined with Cyanide Degradation Confer Resistance to Quinclorac in Echinochloa crus-galli var. mitis

Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants

The nuclear GUCT domain-containing DEAD-box RNA helicases govern gametophytic and sporophytic development in Physcomitrium patens

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