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GroEL‐related molecular chaperones are present in the cytosol of oat cells
Author(s) -
Grimm R.,
Speth V.,
Gatenby A.A.,
Schäfer E.
Publication year - 1991
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(91)80963-4
Subject(s) - groel , chaperonin , cytosol , chaperone (clinical) , coleoptile , intracellular , plastid , biochemistry , mitochondrion , groes , antiserum , biology , co chaperone , microbiology and biotechnology , protein folding , chloroplast , chemistry , heat shock protein , hsp90 , antibody , enzyme , genetics , escherichia coli , medicine , pathology , gene
In eukaryotic cells GroEL‐related molecular chaperones (cpn 60) are considered to be restricted to plastids and mitochondria. Re‐evaluation of the intracellular localization of chaperonins by electron microscopy, using two different anti‐chaperonin antisera, revealed additionally their presence in the cytosol of oat primary leaf and coleoptile cells. The distribution of cpn 60 is not influenced by heat or light treatments.