Journal Article

Inhibition of the Light-Independent Synthesis of Chlorophyll in Pine Cotyledons at Low Temperature

Shinya Muramatsu, Katsumi Kojima, Tomohiro Igasaki, Yoshitaka Azumi and Kenji Shinohara

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 42, issue 8, pages 868-872
Published in print August 2001 | ISSN: 0032-0781
Published online August 2001 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pce103
Inhibition of the Light-Independent Synthesis of Chlorophyll in
Pine Cotyledons at Low
Temperature

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry

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Cotyledons of Japanese black pine (Pinus thunbergii) were yellow when they developed in darkness at 8°C since the light-independent synthesis of chlorophyll was almost completely inhibited in these cotyledons. The level of chlorophyll in dark-grown cotyledons was less than one-twentieth of that in light-grown cotyledons at the same temperature. In the yellow cotyledons, levels of transcripts of cab, rbcS, rbcL and psbA genes were quite high. The large and small subunits of ribulose-1,5-bisphosphate carboxylase/oxygenase were also detected at relatively high levels in yellow cotyledons. However, the accumulation of the two apoproteins of the light-harvesting chlorophyll a/b-binding protein of PSII was limited because of the limited supply of chlorophyll.

Keywords: Key words: Chloroplast proteins— Dark-grown cotyledon — Gene expression — Light-independent synthesis of chlorophyll — Low temperature — Pine (Pinus thunbergii).; Abbreviations: LHC, light-harvesting Chl-protein complex; LHCPII, light-harvesting Chl a/b-binding protein of PSII; LSU, the large subunit of RuBisCO; Pchlide, protochlorophyllide; RuBisCO, ribulose-1,5-bisphosphate carboxylase/oxygenase; SSU, the small subunit of RuBisCO.

Journal Article.  3422 words.  Illustrated.

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

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