Journal Article

Two Types of Putative Nuclear Factors that Physically Interactwith Histidine-Containing Phosphotransfer (Hpt) Domains, SignalingMediators in His-to-Asp Phosphorelay, in <i>Arabidopsisthaliana</i>

Tomomi Suzuki, Kensuke Sakurai, Chiharu Ueguchi and Takeshi Mizuno

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 42, issue 1, pages 37-45
Published in print January 2001 | ISSN: 0032-0781
Published online January 2001 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pce011
Two Types of Putative Nuclear Factors that Physically Interactwith Histidine-Containing Phosphotransfer (Hpt) Domains, SignalingMediators in His-to-Asp Phosphorelay, in Arabidopsisthaliana

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The higher plant, Arabidopsis thaliana, has a large number of genes, each of which encodes a component of His-to-Asp phosphorelay signal transduction systems. One type of such signal transducers are the histidine-containing phosphotransmitters (termed AHPs), which presumably mediate His-to-Asp phosphorelay. Here we attempted to isolate a factor or factors that interact with AHP1, AHP2 and AHP3 by means of a yeast two-hybrid system. This allowed us to identify two types of nuclear-localizing proteins. They are the members of the type-B family of response regulators (specifically, ARR1, APP2 and ARR10), and a novel protein named TCP10. The binding of ARR1 to AHP2 was also confirmed by in vitro binding assays. Moreover, dephosphorylation of AHP2 was observed in a manner dependent on ARR in vitro. A subset of AHPs appeared to also interact with a protein that contains a TCP domain, a recently proposed basic helix-loop-helix motif. Because several factors carrying the TCP domain have been implicated in the regulation of growth and development in lateral organs, the binding of TCP10 to this subset of AHPs suggests a possible linkage between the His-to-Asp phosphorelay systems and plant growth regulation.

Keywords: Key words: HPt domain — Phosphorelay — Response regulator — Signal transduction — TCP domain.

Journal Article.  4413 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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