Journal Article

Ser162-Dependent Inactivation of Overproduced Sucrose-Phosphate Synthase Protein of Maize Leaf in Transgenic Rice Plants

Sakiko Takahashi, Kiyomi Ono, Masashi Ugaki, Ken Ishimaru, Naohiro Aoki and Ryu Ohsugi

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 41, issue 8, pages 977-981
Published in print July 2000 | ISSN: 0032-0781
Published online July 2000 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcd014
Ser162-Dependent Inactivation of Overproduced Sucrose-Phosphate Synthase Protein of Maize Leaf in Transgenic Rice Plants

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  • Biochemistry
  • Molecular and Cell Biology
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To investigate the role of Ser162 in phosphorylation-dependent regulation of maize sucrose-phosphate synthase (SPS) activities in rice, transgenic rice plants expressing wild-type or mutagenized maize SPS were produced. Our results indicate that Ser162 was responsible for overproduction-induced inactivation of SPS protein and for light/dark modulation of this protein in vivo.

Keywords: Key words: Phosphorylation — Rice (Oryza sativa L.) — Sucrose-phosphate synthase (EC 2.4.14) — Transgenic plant.; Abbreviations: Fru6P, fructose-6-phosphate; Glc6P, glucose-6-phosphate; S162A, Ser162-to-Ala mutation; S162AZm plant, transgenic rice plant expressing Ser162-to-Ala mutagenized maize leaf sucrose-phosphate synthase; SPS, sucrose-phosphate synthase; UDPGlc, uridine diphosphoglucose; Vmax, maximum velocity; WT, wild-type; WTZm plant, transgenic rice plant expressing wild-type maize leaf sucrose-phosphate synthase.

Journal Article.  3132 words.  Illustrated.

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

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