Catalase activity is modulated by calcium and calmodulin in detached mature leaves of sweet potato

Journal of Plant Physiology
Mufidah Afiyanti, Hsien-Jung Chen

Abstract

Catalase (CAT) functions as one of the key enzymes in the scavenging of reactive oxygen species and affects the H2O2 homeostasis in plants. In sweet potato, a major catalase isoform was detected, and total catalase activity showed the highest level in mature leaves (L3) compared to immature (L1) and completely yellow, senescent leaves (L5). The major catalase isoform as well as total enzymatic activity were strongly suppressed by ethylene glycol-bis(2-aminoethylether)-N,N,N',N'-tetraacetic acid (EGTA). This inhibition could be specifically and significantly mitigated in mature L3 leaves by exogenous CaCl2, but not MgCl2 or CoCl2. EGTA also inhibited the activity of the catalase isoform in vitro. Furthermore, chlorpromazine (CPZ), a calmodulin (CAM) inhibitor, drastically suppressed the major catalase isoform as well as total enzymatic activity, and this suppression was alleviated by exogenous sweet potato calmodulin (SPCAM) fusion protein in L3 leaves. CPZ also inhibited the activity of the catalase isoform in vitro. Protein blot hybridization showed that both anti-catalase SPCAT1 and anti-calmodulin SPCAM antibodies detect a band at the same position, which corresponds to the activity of the major catalase isoform from unboile...Continue Reading

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Citations

May 23, 2015·Ecotoxicology and Environmental Safety·Laira L D OliveiraBruno Nunes
Apr 18, 2015·Journal of Plant Physiology·Hsien-Jung ChenYaw-Huei Lin
Jun 24, 2017·BioMed Research International·Bin YongHuanhuan Shao
Jun 28, 2018·Frontiers in Plant Science·Bingwei YuBihao Cao
Feb 6, 2020·Ecotoxicology and Environmental Safety·Zainab Naser HusseiniMohammad Amin Toghyani

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