Arabidopsis Histidine Phosphotransfer Proteins Are Redundant Positive Regulators of Cytokinin Signaling

Arabidopsis thaliana histidine phosphotransfer proteins (AHPs) are similar to bacterial and yeast histidine phosphotransfer proteins (HPts), which act in multistep phosphorelay signaling pathways. A phosphorelay pathway is the current model for cytokinin signaling. To assess the role of AHPs in cyto...

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Published inThe Plant cell Vol. 18; no. 11; pp. 3073 - 3087
Main Authors Hutchison, Claire E, Li, Jie, Argueso, Cristiana, Gonzalez, Monica, Lee, Eurie, Lewis, Michael W, Maxwell, Bridey B, Perdue, Tony D, Schaller, G. Eric, Alonso, Jose M, Ecker, Joseph R, Kieber, Joseph J
Format Journal Article
LanguageEnglish
Published England American Society of Plant Biologists 01.11.2006
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Summary:Arabidopsis thaliana histidine phosphotransfer proteins (AHPs) are similar to bacterial and yeast histidine phosphotransfer proteins (HPts), which act in multistep phosphorelay signaling pathways. A phosphorelay pathway is the current model for cytokinin signaling. To assess the role of AHPs in cytokinin signaling, we isolated T-DNA insertions in the five AHP genes that are predicted to encode functional HPts and constructed multiple insertion mutants, including an ahp1,2,3,4,5 quintuple mutant. Single ahp mutants were indistinguishable from wild-type seedlings in cytokinin response assays. However, various higher-order mutants displayed reduced sensitivity to cytokinin in diverse cytokinin assays, indicating both a positive role for AHPs in cytokinin signaling and functional overlap among the AHPs. In contrast with the other four AHPs, AHP4 may play a negative role in some cytokinin responses. The quintuple ahp mutant showed various abnormalities in growth and development, including reduced fertility, increased seed size, reduced vascular development, and a shortened primary root. These data indicate that most of the AHPs are redundant, positive regulators of cytokinin signaling and affect multiple aspects of plant development.
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Current address: Department of Genetics, North Carolina State University, Raleigh, NC 27695.
www.plantcell.org/cgi/doi/10.1105/tpc.106.045674
To whom correspondence should be addressed. E-mail jkieber@unc.edu; fax 919-962-1625.
Online version contains Web-only data.
The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantcell.org) is: Joseph J. Kieber (jkieber@unc.edu).
ISSN:1040-4651
1532-298X
1532-298X
DOI:10.1105/tpc.106.045674