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Heat shock proteins of barley mitochondria and chloroplasts Identification of organellar hsp 10 and 12: putative chaperonin 10 homologues
Author(s) -
Hartman Dallas J.,
Dougan David,
Hoogenraad Nicholas J.,
Høj Peter B.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80883-i
Subject(s) - chaperonin , chloroplast , heat shock protein , hsp60 , mitochondrion , biology , biochemistry , groel , methionine , microbiology and biotechnology , amino acid , protein folding , hsp70 , gene , escherichia coli
Tissue slices from barley seedlings were subjected to heat shock and metabolically labelled with [ 35 S]methionine and [ 35 S]lcysteine, Mitochondria and chloroplasts were isolated and shown to contain two novel heat shock proteins of 10 and 12 kDa, respectively. The possibility that these proteins, like a mitochondrial 10 kDa stress protein recently isolated from rat hepatoma cells [(1992) Proc. Natl. Acad. Sci. 89, in press] represent eukaryotic chaperonin 10 homologues is discussed.