PMID: 8605300Feb 1, 1996Paper

Characterization of a plastid-specific HSP90 homologue: identification of a cDNA sequence, phylogenetic descendence and analysis of its mRNA and protein expression

Plant Molecular Biology
G SchmitzJ Feierabend

Abstract

The isolation of cDNAs is described which encode the complete sequence of a precursor protein for a HSP90 homologue consisting of an N-terminal transit peptide of 5850 Da and a mature protein (cpHSP82) of 82 260 Da, located in the plastids of rye leaves (Secale cereale). Hybridization analysis indicated the presence of a single gene in the DNA of rye and a transcript size of 2.8 kb. A phylogenetic tree constructed on the basis of sequence comparisons for HSP90 homologues from different species and compartments indicated that the plastidic HSP82 from rye was more closely related to an eubacterial protein than to HSP90 homologues of the cytosol or ER from both plants and animals. The results suggest that during chloroplast evolution the gene for cpHSP82 was transferred to the nucleus from a prokaryotic endosymbiont. Immunoblots with specific antibodies and Percoll gradient-purified organelles confirmed the location of cpHSP82 in chloroplasts or non-green plastids. In green rye leaves cpHSP82 was constitutively expressed and equally distributed among tissues of different age. The expression of cpHSP82 was enhanced within 2 h by exposure to 42 degrees C. The cpHSP82 transcript and protein were much more strongly expressed in non-gr...Continue Reading

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Citations

Mar 19, 2008·Cell Stress & Chaperones·Takeshi KobayakawaTakayuki K Nemoto
Aug 29, 2003·The Plant Journal : for Cell and Molecular Biology·Dongsun CaoChi-Lien Cheng
Jul 13, 2002·Plant Physiology·Kosmas HaralampidisPolydefkis Hatzopoulos
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Jun 29, 2004·The Journal of Eukaryotic Microbiology·Alexandra Stechmann, Thomas Cavalier-Smith
Apr 16, 2020·Journal of Experimental Botany·Tereza TicháJozef Šamaj

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