Journal
PLANT CELL AND ENVIRONMENT
Volume 32, Issue 5, Pages 532-541Publisher
WILEY-BLACKWELL PUBLISHING, INC
DOI: 10.1111/j.1365-3040.2009.01947.x
Keywords
cold stress; dehydrin; LEA proteins; metal binding; RNA binding; water stress
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Funding
- Ministry of Education, Science and Culture of Japan [19380182]
- Grants-in-Aid for Scientific Research [19380182] Funding Source: KAKEN
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Dehydrins are hydrophilic proteins that accumulate during embryogenesis and osmotic stress responses in plants. Here, we report an interaction between citrus dehydrin Citrus unshiu cold-regulated 15 kDa protein (CuCOR15) and DNA. Binding of CuCOR15 to DNA was detected by an electrophoretic mobility shift assay, a filter-binding assay and Southwestern blotting. The binding was stimulated by physiological concentrations of Zn(2+), but little stimulation occurred when other divalent cations, such as Mg(2+), Ca(2+), Mn(2+), Ni(2+) and Cu(2+), were substituted for Zn(2+). Ethylenediaminetetraacetic acid cancelled the Zn(2+)-stimulated binding. A binding curve and competitor experiments suggested that the DNA binding of CuCOR15 exhibited low affinity and non-specificity. Moreover, tRNA competed with the DNA binding. Histidine-rich domains and a polylysine segment-containing domain participated in the DNA binding. These results suggest that CuCOR15 can interact with DNA, and also RNA, in the presence of Zn(2+). Dehydrin may protect nucleic acids in plant cells during seed maturation and stress responses.
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