Journal Article

Characterization of Mitochondria-Located Small Heat Shock Protein from Tomato (<i>Lycopersicon esculentum</i>)

Jian Lui and Mariko Shono

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 40, issue 12, pages 1297-1304
Published in print January 1999 | ISSN: 0032-0781
Published online January 1999 | e-ISSN: 1471-9053 | DOI: https://dx.doi.org/10.1093/oxfordjournals.pcp.a029518
Characterization of Mitochondria-Located Small Heat Shock Protein from Tomato (Lycopersicon esculentum)

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  • Biochemistry
  • Molecular and Cell Biology
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We cloned and sequenced a full-length cDNA encoding the precursor of the mitochondria-located small heat shock protein (MT-sHSP) gene (LeHSP23.8) from tomato (Lycopersicon esculentum). The deduced protein precursor with a calculated molecular weight of 23.8 kDa was predicted to target mitochondria and was classified as a plant MT-sHSP. A single copy of LeHSP23.8 was found in tomato genomic DNA by southern-blot analysis. Northern-blot analysis revealed the heat inducible character of LeHSP23.8 mRNA. The LeHSP23.8 mRNA was hardly detectable at about 36°C but accumulated markedly at 40°C. The molecular chaperone function of LeHSP23.8 was confirmed in vitro. The recombinant LeHSP23.8 was able to enhance the renaturation of chemically denatured citrate synthase (CS). Moreover, the recombinant LeHSP23.8 protected CS from thermal inactivation and also promoted the renaturation of thermally inactivated citrate synthase.

Keywords: Lycopersicon esculentum; Mitochondria; Molecular chaperone; Small HSP

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

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