Literature DB >> 12381160

Plant seed cystatins and their target enzymes of endogenous and exogenous origin.

Soichi Arai1, Ichiro Matsumoto, Yasufumi Emori, Keiko Abe.   

Abstract

Cystatins are protein inhibitors of cysteine proteinases of the papain family, and those of animal origin have long been studied from medical and physiological aspects. In the meantime, oryzacystatin cloned from rice seeds in 1987 was recognized as the first well-defined cystatin of plant origin. Cloning studies followed to disclose various plant cytstatins including those of corn and soybean origin, their similarities to and differences from animal cystatins being analyzed in detail. Plant seed cystatins are now understood as factors controlling germination by inhibition of endogenous cysteine proteinases. They can also recognize insect midgut proteinases as exogenous target enzymes to control. This paper discusses chemical and phytophysiological relationships between cystatins and their targets.

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Year:  2002        PMID: 12381160     DOI: 10.1021/jf0201935

Source DB:  PubMed          Journal:  J Agric Food Chem        ISSN: 0021-8561            Impact factor:   5.279


  31 in total

1.  Molecular analysis of maize cystatin expression as fusion product in Escherichia coli.

Authors:  Ashraf Gholizadeh
Journal:  Physiol Mol Biol Plants       Date:  2012-07

2.  A novel Glycine soja cysteine proteinase inhibitor GsCPI14, interacting with the calcium/calmodulin-binding receptor-like kinase GsCBRLK, regulated plant tolerance to alkali stress.

Authors:  Xiaoli Sun; Shanshan Yang; Mingzhe Sun; Sunting Wang; Xiaodong Ding; Dan Zhu; Wei Ji; Hua Cai; Chaoyue Zhao; Xuedong Wang; Yanming Zhu
Journal:  Plant Mol Biol       Date:  2014-01-10       Impact factor: 4.076

3.  Rice bifunctional phytocystatin is a dual modulator of legumain and papain-like proteases.

Authors:  Ana Paula Christoff; Gisele Passaia; Caroline Salvati; Márcio Alves-Ferreira; Marcia Margis-Pinheiro; Rogerio Margis
Journal:  Plant Mol Biol       Date:  2016-06-20       Impact factor: 4.076

4.  Comparative phylogenetic analysis of cystatin gene families from arabidopsis, rice and barley.

Authors:  Manuel Martínez; Zamira Abraham; Pilar Carbonero; Isabel Díaz
Journal:  Mol Genet Genomics       Date:  2005-05-11       Impact factor: 3.291

5.  Crystal structure of tarocystatin-papain complex: implications for the inhibition property of group-2 phytocystatins.

Authors:  Ming-Hung Chu; Kai-Lun Liu; Hsin-Yi Wu; Kai-Wun Yeh; Yi-Sheng Cheng
Journal:  Planta       Date:  2011-03-18       Impact factor: 4.116

6.  The diversity of rice phytocystatins.

Authors:  Ana Paula Christoff; Rogerio Margis
Journal:  Mol Genet Genomics       Date:  2014-08-07       Impact factor: 3.291

7.  Characterization of the entire cystatin gene family in barley and their target cathepsin L-like cysteine-proteases, partners in the hordein mobilization during seed germination.

Authors:  Manuel Martinez; Ines Cambra; Laura Carrillo; Mercedes Diaz-Mendoza; Isabel Diaz
Journal:  Plant Physiol       Date:  2009-09-16       Impact factor: 8.340

8.  Assessment of adaptive evolution between wheat and rice as deduced from full-length common wheat cDNA sequence data and expression patterns.

Authors:  Kanako Kawaura; Keiichi Mochida; Akiko Enju; Yasushi Totoki; Atsushi Toyoda; Yoshiyuki Sakaki; Chikatoshi Kai; Jun Kawai; Yoshihide Hayashizaki; Motoaki Seki; Kazuo Shinozaki; Yasunari Ogihara
Journal:  BMC Genomics       Date:  2009-06-18       Impact factor: 3.969

9.  Phylogenomic analysis of the cystatin superfamily in eukaryotes and prokaryotes.

Authors:  Dusan Kordis; Vito Turk
Journal:  BMC Evol Biol       Date:  2009-11-18       Impact factor: 3.260

10.  An AC-5 cathepsin B-like protease purified from Haemonchus contortus excretory secretory products shows protective antigen potential for lambs.

Authors:  Erik De Vries; Nicole Bakker; Jeroen Krijgsveld; Dave P Knox; Albert J R Heck; Ana Patricia Yatsuda
Journal:  Vet Res       Date:  2009-04-30       Impact factor: 3.683

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