title: The 23-kDa light-stress-regulated heat-shock protein of chenopodium rubrum L. is located in the mitochondria.
abstract: The 23-kDa nuclear-encoded heat-shock protein (HSP) of Chenopodium rubrum L. is regulated by light at the posttranslational level. Higher light intensities are more effective in inducing the accumulation of the mature protein under heat-shock conditions. Based on this and other properties the protein was considered to belong to the group of small chloroplastic HSPs. However, we have now obtained the following evidence that this 23-kDa HSP is localized in the mitochondria: (i) Immunogold-labelled protein was almost exclusively restricted to the mitochondria in electron microscope thin sections. (ii) Using purified, isolated mitochondria from potato tubers the in-vitro-synthesized translation product of 31 kDa was readily transported into mitochondria where it was processed to the 23-kDa product. (iii) The protein could be detected by Western blotting in a preparation of washed mitochondria of Chenopodium, while under the same conditions no signal could be obtained in a preparation of isolated chloroplasts. (iv) Finally, sequence comparison with the published sequences of mitochondrial proteins by Lenne et al. (1995, Biochem J 311:805-813) and LaFayette et al. (1996, Plant Mol Biol 30:159-169) showed clearly that the 23-kDa protein is considerably more similar to these two proteins than to the group of plastid small HSPs. From these data we infer that mitochondria are involved in the response of the plants to high light stress under heat-shock conditions.
authors.affiliation: Institut für Botanik, Universität Hannover, Germany.
authors.forename: K
authors.initials: K
authors.lastname: Debel
authors.forename: W D
authors.initials: WD
authors.lastname: Sierralta
authors.forename: H P
authors.initials: HP
authors.lastname: Braun
authors.forename: U K
authors.initials: UK
authors.lastname: Schmitz
authors.forename: K
authors.initials: K
authors.lastname: Kloppstech
mesh_terms: D000595:Amino Acid Sequence; D002458:Cell Fractionation; D002467:Cell Nucleus / Q000378:metabolism; D002478:Cells, Cultured; D029721:Drosophila Proteins; D006360:Heat-Shock Proteins / Q000032:analysis / Q000096:biosynthesis* / Q000737:chemistry; D006358:Hot Temperature; D008565:Membrane Proteins / Q000032:analysis / Q000096:biosynthesis; D008854:Microscopy, Electron; D008928:Mitochondria / Q000378:metabolism* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000032:analysis / Q000096:biosynthesis*; D010944:Plants / Q000378:metabolism*; D018087:Plastids / Q000378:metabolism / Q000648:ultrastructure; D014176:Protein Biosynthesis; D017386:Sequence Homology, Amino Acid; D014158:Transcription, Genetic
chemical_list: D029721:Drosophila Proteins; D006360:Heat-Shock Proteins; C105998:Hsp23 protein, Drosophila; D008565:Membrane Proteins; D010940:Plant Proteins