Structural complexity and functional diversity of plant NADPH oxidases

Gurpreet Kaur, Kunchur Guruprasad, Brenda R.S. Temple, David G. Shirvanyants, Nikolay Dokholyan, Pratap Kumar Pati

Research output: Contribution to journalArticle

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Abstract

Plant NADPH oxidases also known as respiratory burst oxidase homologs (Rbohs) are a family of membrane-bound enzymes that play diverse roles in the defense response and morphogenetic processes via regulated generation of reactive oxygen species. Rbohs are associated with a variety of functions, although the reason for this is not clear. To evaluate using bioinformatics, the possible mechanisms for the observed functional diversity within the plant kingdom, 127 Rboh protein sequences representing 26 plant species were analyzed. Multiple clusters were identified with gene duplications that were both dicot as well as monocot-specific. The N-terminal sequences were observed to be highly variable. The conserved cysteine (equivalent of Cys890) in C-terminal of AtRbohD suggested that the redox-based modification like S-nitrosylation may regulate the activity of other Rbohs. Three-dimensional models corresponding to the N-terminal domain for Rbohs from Arabidopsis thaliana and Oryza sativa were constructed and molecular dynamics studies were carried out to study the role of Ca 2+ in the folding of Rboh proteins. Certain mutations indicated possibly affect the structure and function of the plant NADPH oxidases, thereby providing the rationale for further experimental validation.

Original languageEnglish (US)
Pages (from-to)79-94
Number of pages16
JournalAmino Acids
Volume50
Issue number1
DOIs
StatePublished - Jan 1 2018

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NADPH Oxidase
Plant Structures
Gene Duplication
Protein Folding
Molecular Dynamics Simulation
Bioinformatics
Computational Biology
Arabidopsis
Oxidation-Reduction
Cysteine
Molecular dynamics
Reactive Oxygen Species
Proteins
Genes
Membranes
Mutation
superoxide-forming enzyme
Enzymes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

Cite this

Kaur, G., Guruprasad, K., Temple, B. R. S., Shirvanyants, D. G., Dokholyan, N., & Pati, P. K. (2018). Structural complexity and functional diversity of plant NADPH oxidases. Amino Acids, 50(1), 79-94. https://doi.org/10.1007/s00726-017-2491-5
Kaur, Gurpreet ; Guruprasad, Kunchur ; Temple, Brenda R.S. ; Shirvanyants, David G. ; Dokholyan, Nikolay ; Pati, Pratap Kumar. / Structural complexity and functional diversity of plant NADPH oxidases. In: Amino Acids. 2018 ; Vol. 50, No. 1. pp. 79-94.
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Kaur, G, Guruprasad, K, Temple, BRS, Shirvanyants, DG, Dokholyan, N & Pati, PK 2018, 'Structural complexity and functional diversity of plant NADPH oxidases', Amino Acids, vol. 50, no. 1, pp. 79-94. https://doi.org/10.1007/s00726-017-2491-5

Structural complexity and functional diversity of plant NADPH oxidases. / Kaur, Gurpreet; Guruprasad, Kunchur; Temple, Brenda R.S.; Shirvanyants, David G.; Dokholyan, Nikolay; Pati, Pratap Kumar.

In: Amino Acids, Vol. 50, No. 1, 01.01.2018, p. 79-94.

Research output: Contribution to journalArticle

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