Title

In silico physicochemical characterization and topology analysis of Respiratory burst oxidase homolog (Rboh) proteins from Arabidopsis and rice

Authors

Gurpreet Kaur^1,2, Pratap Kumar Pati^1*

Affiliation

¹Department of Biotechnology, Guru Nanak Dev University (GNDU), Amritsar 143005, Punjab, India;

²Present Address: Max Planck Institute for Developmental Biology, Tuebingen 72076, Germany;

E-mail

pkpati@yahoo.com;

Article Type

Hypothesis

Date

Received January 17, 2018; Revised February 6, 2018; Accepted February 10, 2018; Published March 31, 2018

NADPH oxidase (NOX) is a key enzyme involved in the production of apoplastic superoxide (O2-), a type of reactive oxygen species (ROS). Plant Noxes are the homologs of mammalian NADPH oxidase’s catalytic subunit and are documented as respiratory burst oxidase homologs (Rbohs). A number of studies have reported their diverse functions in combating various stresses and in plant growth and development. In the present study, a total of 19 Rboh proteins (10 from Arabidopsis thaliana and 9 from Oryza sativa Japonica) were analyzed. We employed in silico approaches to compute the physiochemical properties (molecular weight, isoelectric point, total number of negatively and positively charged residues, extinction coefficient, half-life, instability and aliphatic index, grand average of hydropathicity, amino acid percentage). We observed a lot of variability in these parameters among the Rbohs accounting for their functional diversification. Their topological analysis, subcellular localization and signal peptide detection are also performed. To the best of our knowledge, the present study report on in silico physiochemical characterization, topology analysis, subcellular localization and signal peptide detection of Rboh proteins within two model plants. The study elucidates the variations in the key properties among Rbohs proteins, which may be responsible for their functional multiplicity.

Keywords:

plant NADPH oxidase, in silico, physicochemical characterization, subcellular localization, signal peptide, topology.

Citation

Kaur & Pati. Bioinformation 14(3): 93-100 (2018)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.