Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/31528
Title: Structural and functional analysis of chitinase gene family in wheat (Triticum aestivum)
Authors: Mishra, A K
Pandey, Bharati
Tyagi, Chetna
Chakraborty, Ohika
Kumar, Amrender
Jain, A K
Keywords: Chitinase gene;Signature patterns;Secondary structure;Phylogenetic analysis;Expression profile Wheat;Triticum aestivum
Issue Date: Apr-2015
Publisher: NISCAIR-CSIR, India
Abstract: Chitinases are the hydrolytic enzymes which protect plants against pathogen attack. However, the precise role of chitinases in disease resistance has not been explored in wheat. In the present study, in silico approach, including secondary structure analysis, detailed signature pattern study, cis-acting regulatory elements survey, evolutionary trends and three-dimensional molecular modeling was used for different chitinase classes of wheat (Triticum aestivum). Homology modeling of class I, II, IV and 3 chitinase proteins was performed using the template crystal structure. The model structures were further refined by molecular mechanics methods using different tools, such as Procheck, ProSA and Verify3D. Secondary structure studies revealed greater percentage of residues forming α helix conformation with specific signature pattern, similar to casein kinase II phosphorylation site, amidation site, N-myristoylation (N-MYR) site and protein kinase C phoshorylation site. The expression profile suggested that wheat chitinase gene was highly expressed in cell culture and callus. We found that wheat chitinases showed more functional similarity with rice and barley. The results provide insight into the evolution of the chitinase family, constituting a diverse array of pathogenesis-related proteins. The study also provides insight into the possible binding sites of chitinase proteins and may further enhance our knowledge of fungal resistance mechanism in plants.
Page(s): 169-178
URI: http://hdl.handle.net/123456789/31528
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.52(2) [April 2015]

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