Details
| Original language | English |
|---|---|
| Pages (from-to) | 32-43 |
| Number of pages | 12 |
| Journal | Planta |
| Volume | 190 |
| Issue number | 1 |
| Publication status | Published - May 1993 |
| Externally published | Yes |
Abstract
A 68-kDa heat-stress protein (HSP68) has been purified from cell-suspension cultures of tomato (Lycopersicon peruvianum L.). Antibodies raised against HSP68 cross-react with the Escherichia coli heat-stress protein DnaK. HSP68 was found to be a hydrophilic, ATP-binding protein. Immunological analysis of subcellular fractions and immunogold-labelling of ultrathin sections showed consistently that HSP68 is localized in the mitochondrial matrix. In-vitro translation experiments indicated that HSP68 is synthesized as a precursor protein. Immunoscreening of cDNA libraries from tomato and potato (Solanum tuberosum L.) led to the isolation of corresponding cDNA clones. The deduced amino-acid sequences show strong relationships to the DnaK-like proteins from bacteria and organelles of eukaryotic cells. The protein HSP68 is constitutively expressed, but its synthesis is increased during heat stress in all cells of higher plantes investigated so far.
Keywords
- Chaperonin, Heat stress, Lycopersicon, Mitochondrion, Solanum
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Agricultural and Biological Sciences(all)
- Plant Science
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In: Planta, Vol. 190, No. 1, 05.1993, p. 32-43.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - HSP68
T2 - A DnaK-like heat-stress protein of plant mitochondria
AU - Neumann, D.
AU - Emmermann, Michael
AU - Thierfelder, J. M.
AU - zur Nieden, U.
AU - Clericus, Monika
AU - Braun, Hans-Peter
AU - Nover, L.
AU - Schmitz, Udo
PY - 1993/5
Y1 - 1993/5
N2 - A 68-kDa heat-stress protein (HSP68) has been purified from cell-suspension cultures of tomato (Lycopersicon peruvianum L.). Antibodies raised against HSP68 cross-react with the Escherichia coli heat-stress protein DnaK. HSP68 was found to be a hydrophilic, ATP-binding protein. Immunological analysis of subcellular fractions and immunogold-labelling of ultrathin sections showed consistently that HSP68 is localized in the mitochondrial matrix. In-vitro translation experiments indicated that HSP68 is synthesized as a precursor protein. Immunoscreening of cDNA libraries from tomato and potato (Solanum tuberosum L.) led to the isolation of corresponding cDNA clones. The deduced amino-acid sequences show strong relationships to the DnaK-like proteins from bacteria and organelles of eukaryotic cells. The protein HSP68 is constitutively expressed, but its synthesis is increased during heat stress in all cells of higher plantes investigated so far.
AB - A 68-kDa heat-stress protein (HSP68) has been purified from cell-suspension cultures of tomato (Lycopersicon peruvianum L.). Antibodies raised against HSP68 cross-react with the Escherichia coli heat-stress protein DnaK. HSP68 was found to be a hydrophilic, ATP-binding protein. Immunological analysis of subcellular fractions and immunogold-labelling of ultrathin sections showed consistently that HSP68 is localized in the mitochondrial matrix. In-vitro translation experiments indicated that HSP68 is synthesized as a precursor protein. Immunoscreening of cDNA libraries from tomato and potato (Solanum tuberosum L.) led to the isolation of corresponding cDNA clones. The deduced amino-acid sequences show strong relationships to the DnaK-like proteins from bacteria and organelles of eukaryotic cells. The protein HSP68 is constitutively expressed, but its synthesis is increased during heat stress in all cells of higher plantes investigated so far.
KW - Chaperonin
KW - Heat stress
KW - Lycopersicon
KW - Mitochondrion
KW - Solanum
UR - http://www.scopus.com/inward/record.url?scp=0027349412&partnerID=8YFLogxK
U2 - 10.1007/BF00195672
DO - 10.1007/BF00195672
M3 - Article
C2 - 7763614
AN - SCOPUS:0027349412
VL - 190
SP - 32
EP - 43
JO - Planta
JF - Planta
SN - 0032-0935
IS - 1
ER -