Plant and Cell Physiology Supplement
Abstract of the Annual Meeting of JSPP 2009
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Functional analysis of a PPR protein with the NYN domain
*Yoshihiro KomuraHiroyuki SatohMamoru Sugita
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Pages 0478

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Abstract
Pentatricopeptide repeat (PPR) proteins are thought to possess important physiological roles in plant organelle biogenesis, organ development, cell differentiation, and so on. Although several PPR proteins was reported to be involved in RNA processing of RNA precursors in plastids and mitochondria, the function of most PPR proteins remains to be elucidated. To investigate the function of PPR proteins, we have been performing loss-of-function analyses of Physcomitrella patens PPR protein genes. In the present study, we report the phenotypes of PpPPR_63 gene disruptant. PpPPR_63 consists of two PPR motifs and the C-terminal NYN domain. The disruptant showed the impaired growth of protonemal colony and abnormal cell shape of branched protomemata. To investigate the subcellular localization of PpPPR_63, stable transformants with green fluorescent protein (GFP) knocked-in the PpPPR_63 gene was produced. The GFP fluorescence was observed in the nucleus of the protonemata, rhizoids and buds.
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© 2009 by The Japanese Society of Plant Physiologists
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