Journal
JOURNAL OF EXPERIMENTAL BOTANY
Volume 64, Issue 6, Pages 1615-1624Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jxb/ert016
Keywords
Circular dichroism; dehydrin; disordered protein; heavy metal; histidine; reactive oxygen species
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Funding
- Ministry of Education, Science, Sports and Culture of Japan [23380192]
- Grants-in-Aid for Scientific Research [24658093, 23380192] Funding Source: KAKEN
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Dehydrin is a plant disordered protein whose functions are not yet totally understood. Here it is reported that a KS-type dehydrin can reduce the formation of reactive oxygen species (ROS) from Cu. AtHIRD11, which is the Arabidopsis KS-type dehydrin, inhibited generation of hydrogen peroxide and hydroxyl radicals in the Cuascorbate system. The radical-reducing activity of AtHIRD11 was stronger than those of radical-silencing peptides such as glutathione and serum albumin. The addition of Cu-2 reduced the disordered state, decreased the trypsin susceptibility, and promoted the self-association of AtHIRD11. Domain analyses indicated that the five domains containing histidine showed ROS-reducing activities. Histidine/alanine substitutions indicated that histidine is a crucial residue for reducing ROS generation. Using the 27 peptides which are related to the KnS-type dehydrins of 14 plant species, it was found that the strengths of ROS-reducing activities can be determined by two factors, namely the histidine contents and the length of the peptides. The degree of ROS-reducing activities of a dehydrin can be predicted using these indices.
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