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JXB Advance Access originally published online on January 29, 2007
Journal of Experimental Botany 2007 58(5):1173-1183; doi:10.1093/jxb/erl284
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© 2007 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/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

Molecular properties of a novel, hydrophilic cation-binding protein associated with the plasma membrane

Yuki Ide, Nahoko Nagasaki, Rie Tomioka, Momoe Suito, Takehiro Kamiya and Masayoshi Maeshima*

Laboratory of Cell Dynamics, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan

* To whom correspondence should be addressed. E-mail: maeshima{at}agr.nagoya-u.ac.jp

A new type of protein was found in Arabidopsis thaliana, PCaP1, which is rich in glutamate and lysine residues. The protein bound 45Ca2+ even in the presence of a high concentration of Mg2+. Real-time polymerase chain reaction and histochemical analysis of promoter–ß-glucuronidase fusions revealed that PCaP1 was expressed in most organs. The PCaP1 protein was detected immunochemically in these organs. Treatment of Arabidopsis seedlings with Cu2+, sorbitol, or flagellin oligopeptide enhanced the transcription. On the other hand, other sugars, abscisic acid, gibberellic acid, dehydration, and low temperature had little or no effect on PCaP1 transcript abundance. The transient expression of PCaP1 fused to green fluorescent protein in Arabidopsis cells and the subcellular fractionation of tissue homogenate showed that PCaP1 protein is localized to the plasma membrane, although PCaP1 has no predicted transmembrane domain. PCaP1 was associated with the plasma membrane under natural conditions and was released from the membrane at high concentrations of Ca2+ or Mg2+ in vitro. These results suggest that the hydrophilic protein PCaP1 binds Ca2+ and other cations and is stably associated with the plasma membrane.

Key words: Arabidopsis thaliana, calcium, cation, membrane-associated protein, myristoylation, plasma membrane

Received 27 June 2006; Revised 23 November 2006 Accepted 23 November 2006


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