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Paraquat-resistant lines in Pisum sativum cv. Alaska: biochemical and phenotypic characterization
Authors:Md. Emdadul Haque  Yusuke Yoshida  Kohji Hasunuma
Affiliation:(1) Kihara Institute for Biological Research, Yokohama City University, 641-12 Maioka-cho, Totsuka-ku, Yokohama 244-0813, Japan
Abstract:In plants, the oxygen generated by photosynthesis can be excited to form reactive oxygen species (ROS) under excessive sunlight. Excess ROS including singlet oxygen (1O2) inhibit the growth, development and photosynthesis of plants. To isolate ROS-resistant crop plants, we used paraquat (PQ), a generator of O2 ·− as a source of screening and mutagen, and obtained two PQ-resistant lines in Pisum sativum, namely R3-1 and R3-2. Both lines showed greater resistance to PQ than their wild type (WT) siblings with respect to germination, root growth, and shoot growth. Biochemical analysis showed differences in these lines, in which ROS-scavenging enzymes undergo changes with a distinguishable increase in Mn-SOD. We further observed that the cytosolic catalases (CATs) in leaves in both lines were shifted in a native-PAGE analysis compared with that of the WT, indicating that the release of bound 1O2 was enhanced. Phenotypic analysis revealed distinguishable differences in leaf development, and in flowering time and position. In addition, R3-1 and R3-2 showed shorter individual internode lengths, dwarf plant height, and stronger branching compared with the WT. These results suggested that PQ-induced ROS-resistant Pisum have the potential pleiotropic effects on flowering time and stem branching, and that ROS including 1O2 plays not only important roles in plant growth and development as a signal transducer, but also appears as a strong inhibitor for crop yield. Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users.
Keywords:Pisum sativum   Paraquat (PQ)  Reactive oxygen species (ROS)  Singlet oxygen (1O2)  Superoxide dismutase (SOD)  Catalase (CAT)
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