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<span style="font-size:11.0pt;mso-bidi-font-size: 10.0pt;font-family:"Times New Roman";mso-fareast-font-family:"Times New Roman"; mso-bidi-font-family:"Times New Roman";mso-ansi-language:EN-GB;mso-fareast-language: EN-US;mso-bidi-language:AR-SA" lang="EN-GB">Structural and functional analysis of <i style="mso-bidi-font-style:normal">chitinase</i> gene family in wheat (<i style="mso-bidi-font-style:normal">Triticum aestivum</i>)</span>

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Title Structural and functional analysis of chitinase gene family in wheat (Triticum aestivum)
 
Creator Mishra, A K
Pandey, Bharati
Tyagi, Chetna
Chakraborty, Ohika
Kumar, Amrender
Jain, A K
 
Subject Chitinase gene
Signature patterns
Secondary structure
Phylogenetic analysis
Expression profile Wheat
Triticum aestivum
 
Description 169-178
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.
 
Date 2015-05-14T11:37:38Z
2015-05-14T11:37:38Z
2015-04
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/31528
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.52(2) [April 2015]