Heat shock proteins from cell cultures of higher plants and their somatic hybrids

1985 ◽  
Vol 4 (1) ◽  
pp. 19-22 ◽  
Author(s):  
S. V. Lopato ◽  
Yu.Yu. Gleba
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Somatic Hybrids ◽  
Higher Plants ◽  
Shock Proteins

scholarly journals Synthesis, modification and structural binding of heat-shock proteins in tomato cell cultures

1984 ◽  
Vol 139 (2) ◽  
pp. 303-313 ◽  
Author(s):  
Lutz NOVER ◽  
Klaus-Dieter SCHARF
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Shock Proteins

scholarly journals Heat shock proteins of higher plants

1981 ◽  
Vol 78 (6) ◽  
pp. 3526-3530 ◽  
Author(s):  
J. L. Key ◽  
C. Y. Lin ◽  
Y. M. Chen
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Higher Plants ◽  
Shock Proteins

The expression of heat-shock genes in higher plants

1986 ◽  
Vol 314 (1166) ◽  
pp. 453-468 ◽  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Higher Plants ◽  
Structural Features ◽  
Amino Acid Sequences ◽  
Heat Shock Gene ◽  
Regulatory Sequences ◽  
Heat Shock Genes ◽  
Control Of Gene Expression ◽  
Shock Proteins

High-temperature stress or heat shock induces the vigorous synthesis of heat-shock proteins in many organisms including the higher plants. This response has been implicated in the acquisition of thermotolerance. The biological importance of a group of low-molecular-mass proteins in the response of plants is indicated by the conservation of the corresponding genes. The steady-state levels of mRNAs for these proteins shift from undetectable levels at normal temperature to about 20 000 molecules per gene in the cell after heat shock. The analysis of ‘run-off’ transcripts from isolated soybean nuclei suggests a transcriptional control of gene expression. The DNA sequence analysis of soybean heat-shock genes revealed a conservation of promoter sequences and 5'-upstream elements. A comparison of the deduced amino acid sequences of polypeptides showed a conservation of structural features in heat-shock proteins between plants and animals. The implication of a common regulatory concept in the heat-shock response makes genes belonging to this family (15-18 kDa proteins) in soybean favourable candidates for investigating thermoregulation of transcription. We have exploited the natural gene transfer system of Agrobacterium tumefaciens to introduce a soybean heat-shock gene into the genomes of sunflower and tobacco. The gene is thermoinducibly transcribed and transcripts are faithfully initiated in transgenic plants. Experiments are in progress to define the regulatory sequences 5'-upstream from the gene. The expression of heat-shock genes in a heterologous genetic background also provides the basis for studying the function of the proteins and their possible role in thermoprotection.

Acidic extracellular environment induces only a subset of heat-shock proteins in primary mouse kidney cell cultures

1990 ◽  
Vol 68 (4) ◽  
pp. 804-807 ◽  
Author(s):  
Edward W. Khandjian
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Kidney Cell ◽  
Acidic Medium ◽  
Stress Proteins ◽  
Cdna Probe ◽  
Mouse Kidney ◽  
Primary Mouse ◽  
Shock Proteins

Exposure of primary mouse kidney cell cultures to acidic medium (pH 5.5) induced the expression of a 70 kilodalton (kDa) protein. This protein was identified as the major inducible heat-shock protein 70 (hsp70) by immunoprecipitation with anti-hsp70 serum and Northern blot analysis with a hsp70 cDNA probe. Maximum induction of the 70-kDa protein at pH 5.5 after 240 min was about 30% of that observed after 60 min of thermal treatment at 43 °C. In addition, there was an apparent induction of the glucose-regulated proteins (GRPs) of 76–78 and 98–100 kDa, but not of the other hsps. This subset induction of the heat-shock response by acidic medium suggests that different mechanisms are responsible for the induction of the various families of hsps.Key words: heat-shock proteins, stress proteins, acidic induction, viral infection, mouse kidney cells.

Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves

1983 ◽  
Vol 3 (9) ◽  
pp. 1648-1655
Author(s):  
L Nover ◽  
K D Scharf ◽  
D Neumann
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Structural Proteins ◽  
Lycopersicon Peruvianum ◽  
Electron Microscopic ◽  
Considerable Part ◽  
Heat Shock Granules ◽  
Simultaneous Synthesis ◽  
Shock Proteins

Biochemical and electron microscopic analyses of heat-shocked suspension cultures of Peruvian tomato (Lycopersicon peruvianum) revealed that a considerable part of the dominant small heat shock proteins (hsps) with an Mr of approximately 17,000 are structural proteins of newly forming granular aggregates in the cytoplasm (heat shock granules), whose formation strictly depends on heat shock conditions (37 to 40 degrees C) and the presence or simultaneous synthesis of hsps. However, under certain conditions, e.g., in preinduced cultures maintained at 25 degrees C, hsps also accumulate as soluble proteins without concomitant assembly of heat shock granules. Similar heat shock-induced cytoplasmic aggregates were also observed in other cell cultures and heat-shocked tomato leaves and corn coleoptiles.

scholarly journals Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs.

1989 ◽  
Vol 9 (3) ◽  
pp. 1298-1308 ◽  
Author(s):  
L Nover ◽  
K D Scharf ◽  
D Neumann
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Animal Cells ◽  
Reversible Aggregation ◽  
Specific Subset ◽  
Messenger Ribonucleoprotein ◽  
Cscl Gradient ◽  
Heat Shock Granules ◽  
Shock Proteins

In heat-shocked tomato cell cultures, cytoplasmic heat shock granules (HSGs) are tightly associated with a specific subset of mRNAs coding mainly for the untranslated control proteins. This messenger ribonucleoprotein complex was banded in a CsCl gradient after fixation with formaldehyde (approximately 1.30 g/cm3). It contains all the heat shock proteins and most of the RNA applied to the gradient. During heat shock, a reversible aggregation of HSGs from 15S precursor particles can be shown. These pre-HSGs are not identical to the 19S plant prosomes. Ultrastructural analysis supports the ribonucleoprotein nature of HSGs and their composition of approximately 10-nm precursor particles. A model summarizes our results. It gives a reasonable explanation for the striking conservation of untranslated mRNAs during heat shock and may apply also to animal cells.

Heat-shock proteins induce heavy-metal tolerance in higher plants

Planta ◽  
1994 ◽  
Vol 194 (3) ◽  
Author(s):  
D. Neumann ◽  
O. Lichtenberger ◽  
D. G�nther ◽  
K. Tschiersch ◽  
L. Nover
Keyword(s):  
Heavy Metal ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Metal Tolerance ◽  
Higher Plants ◽  
Heavy Metal Tolerance ◽  
Shock Proteins

Secreted heat shock proteins in sunflower suspension cell cultures

1997 ◽  
Vol 16 (11) ◽  
pp. 792-796 ◽  
Author(s):  
G. Mita ◽  
G. Nocco ◽  
C. Leuci ◽  
V. Greco ◽  
P. Rampino ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Suspension Cell ◽  
Suspension Cell Cultures ◽  
Shock Proteins
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