dc.contributor.author | Gao, Y | |
dc.contributor.author | Nishikawa, H | |
dc.contributor.author | Badejo, AA | |
dc.contributor.author | Shibata, H | |
dc.contributor.author | Sawa, Y | |
dc.contributor.author | Nakagawa, T | |
dc.contributor.author | Maruta, T | |
dc.contributor.author | Shigeoka, S | |
dc.contributor.author | Smirnoff, N | |
dc.contributor.author | Ishikawa, T | |
dc.date.accessioned | 2017-02-15T09:08:12Z | |
dc.date.issued | 2011-06 | |
dc.description.abstract | Ascorbate (AsA) is a redox buffer and enzyme cofactor with various proposed functions in stress responses and growth. The aim was to identify genes whose transcript levels respond to changes in leaf AsA. The AsA-deficient Arabidopsis mutant vtc2-1 was incubated with the AsA precursor L-galactono-1,4-lactone (L-GalL) to increase leaf AsA concentration. Differentially expressed genes screened by DNA microarray were further characterized for AsA responsiveness in wild-type plants. The analysis of 14 candidates by real-time PCR identified an aspartyl protease gene (ASP, At1g66180) and a C3HC4-type RING zinc finger gene (AtATL15, At1g22500) whose transcripts were rapidly responsive to increases in AsA pool size caused by L-GalL and AsA supplementation and light. Transgenic Arabidopsis plants expressing an AtATL15 promoter::luciferase reporter confirmed that the promoter is L-GalL, AsA, and light responsive. The expression patterns of ASP and AtATL15 suggest they have roles in growth regulation. The promoter of AtATL15 is responsive to AsA status and will provide a tool to investigate the functions of AsA in plants further. | en_GB |
dc.description.sponsorship | This work was partly supported by Grants-in-aid for Scientific
Research (A) (SS: 22248042) and (B) (TI: 21380207) from
the Ministry of Education, Culture, Sports, Science, and
Technology of Japan, by the Japan Society for the Promotion
of Science, and the Royal Society under the JapanUK
Research Cooperative Program (TI). | en_GB |
dc.identifier.citation | Vol. 62, pp. 3647 - 3657 | en_GB |
dc.identifier.doi | 10.1093/jxb/err068 | |
dc.identifier.uri | http://hdl.handle.net/10871/25859 | |
dc.language.iso | en | en_GB |
dc.publisher | Oxford University Press (OUP) for Society for Experimental Biology (SEB) | en_GB |
dc.relation.url | https://www.ncbi.nlm.nih.gov/pubmed/21421703 | en_GB |
dc.rights | © 2011 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/2.5),
which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. | en_GB |
dc.subject | Arabidopsis | en_GB |
dc.subject | Arabidopsis Proteins | en_GB |
dc.subject | Ascorbic Acid | en_GB |
dc.subject | Aspartic Acid Proteases | en_GB |
dc.subject | Oligonucleotide Array Sequence Analysis | en_GB |
dc.subject | Plants, Genetically Modified | en_GB |
dc.subject | Polymerase Chain Reaction | en_GB |
dc.subject | Sugar Acids | en_GB |
dc.title | Expression of aspartyl protease and C3HC4-type RING zinc finger genes are responsive to ascorbic acid in Arabidopsis thaliana. | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2017-02-15T09:08:12Z | |
dc.identifier.issn | 1460-2431 | |
exeter.place-of-publication | England | en_GB |
dc.description | This is the final version of the article. Available from the publisher via the DOI in this record. | en_GB |
dc.identifier.journal | Journal of Experimental Botany | en_GB |
dc.identifier.pmcid | PMC3130181 | |
dc.identifier.pmid | 21421703 | |