Record Details

Oxalate decarboxylase from Collybia velutips: molecular cloning and its over expression to confer resistance to fungal infection in transgenic tobacco and tomato

NIPGR Digital Knowledge Repository (NDKR)

View Archive Info
 
 
Field Value
 
Title Oxalate decarboxylase from Collybia velutips: molecular cloning and its over expression to confer resistance to fungal infection in transgenic tobacco and tomato
 
Creator Kesarwani, Meenu
Azam, Mohammad
Natarajan, K
Mehta, Anuradha
Datta, Asis
 
Subject Transgenic Tobacco and Tomato
Molecular Cloning
Fungal Infection
Amaranth and Lathyrus
 
Description Oxalic acid is present as nutritional stress in many
crop plants like Amaranth and Lathyrus. Oxalic acid has
also been found to be involved in the attacking mecha-
nism of several phytopathogenic fungi. A full-length
cDNA for oxalate decarboxylase, an oxalate-catabolizing
enzyme, was isolated by using 5؅-rapid amplification of
cDNA ends-polymerase chain reaction of a partial cDNA
as cloned earlier from our laboratory (Mehta, A., and
Datta, A. (1991) J. Biol. Chem. 266, 23548 –23553). By
screening a genomic library from Collybia velutipes
with this cDNA as a probe, a genomic clone has been
isolated. Sequence analyses and comparison of the
genomic sequence with the cDNA sequence revealed
that the cDNA is interrupted with 17 small introns. The
cDNA has been successfully expressed in cytosol and
vacuole of transgenic tobacco and tomato plants. The
transgenic plants show normal phenotype, and the
transferred trait is stably inherited to the next generation. The recombinant enzyme is partially glycosylated
and shows oxalate decarboxylase activity in vitro as well
as in vivo. Transgenic tobacco and tomato plants ex-
pressing oxalate decarboxylase show remarkable resistance to phytopathogenic fungus Sclerotinia sclerotio-
rum that utilizes oxalic acid during infestation. The
result presented in the paper represents a novel approach to develop transgenic plants resistant to fungal
infection.
 
Date 2013-10-07T08:55:42Z
2013-10-07T08:55:42Z
2000
 
Type Article
 
Identifier J. Biol. Chem., 275: 7230-7238
http://hdl.handle.net/123456789/14
 
Language en
 
Publisher The American Society for Biochemistry and Molecular Biology, Inc.