Expression of the genes encoding hsp73, hsp18, and ubiquitin in radicles of heat-shocked maize seedlings

Genome ◽  
1989 ◽  
Vol 31 (2) ◽  
pp. 698-704 ◽  
Author(s):  
Burr G. Atkinson ◽  
Ling Liu ◽  
Ing Swie Goping ◽  
David B. Walden
Keyword(s):  
Elevated Temperature ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Continuous Exposure ◽  
State Control ◽  
Fourfold Increase ◽  
Genes Encoding ◽  
Molecular Masses ◽  
Shock Proteins ◽  
Steady State Control

Radicles of intact 5-day-old maize (cv. OH43) seedlings exposed to a rapid, short-term elevation (2 h) in environmental (25 to 42.5 °C) temperature exhibit new and (or) enhanced synthesis of a specific set of proteins, the so-called heat shock proteins (hsps), with molecular masses of 108 000, 89 000, 84 000, 76 000, 73 000, 30 000, 23 000, and 18 000. Continuous exposure of intact seedlings to this elevated temperature results in a depression in the synthesis of these hsps after 8 – 12 h and a shift in the pattern of the proteins synthesized to one that resembles those proteins synthesized by radicles from seedlings grown at 25 °C. The transient synthesis of hsp73 and the hsp18 family in radicles from seedlings exposed to, and maintained at, an elevated temperature correlates with the levels of hsp73 and hsp18 mRNAs associated with their polyribosomes. The heat shock induced accumulation of these hsp mRNAs occurs concomitantly with a fourfold increase in polyribosome-associated ubiquitin mRNAs. However, unlike the transient association of hsp73 and hsp18 mRNAs with polyribosomes in radicles from seedlings maintained at 42.5 °C (8 – 12 h), the level of uniquitin mRNAs associated with polyribosomes does not return to a steady-state control (25 °C) level for at least 24 h. The marked, rapid increase in the level of ubiquitin mRNAs associated with polyribosomes in radicles from heat-shocked seedlings provides the first evidence implicating ubiquitin as a heat shock protein of plants.Key words: heat Shock, heat shock proteins, ubiquitin, maize.

scholarly journals Genes encoding heat shock proteins in the endoparasitoid wasp, Cotesia chilonis, and their expression in response to temperatures

2018 ◽  
Vol 17 (5) ◽  
pp. 1012-1022 ◽  
Author(s):  
Dan-dan PAN ◽  
Shuang-shuang CAO ◽  
Ming-xing LU ◽  
San-bao HANG ◽  
Yu-zhou DU
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Genes Encoding ◽  
Shock Proteins ◽  
Cotesia Chilonis

The expression of temperature-stress proteins in a desert cactus (Opuntia ficus indica)

Genome ◽  
1991 ◽  
Vol 34 (6) ◽  
pp. 940-943 ◽  
Author(s):  
Daryl J. Somers ◽  
Randal W. Giroux ◽  
W. Gary Filion
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Stress Proteins ◽  
Protein S ◽  
Protein Families ◽  
Opuntia Ficus Indica ◽  
Stress Acclimation ◽  
Molecular Masses ◽  
Shock Proteins

Opuntia ficus indica roots grown hydroponically at 20 or 30 °C were subjected to a range of heat-shock temperatures as high as 50 °C for 2 h. Roots grown at 30 °C sustained a greater level of total protein synthesis than did 20 °C-grown roots following heat-shock treatments ≥ 45 °C. The 30 °C-grown roots synthesized 31 families of heat-shock proteins between 38 and 47 °C in comparison with 20 °C-grown roots, which synthesized 19 families of heat-shock proteins at 45 °C. In both groups of roots, the heat-shock response was dominated equally by the 71–75 and a 62 kDa heat-shock protein families. In addition, the 20 °C-grown roots expressed 11 families of cold-shock proteins following 2 h at 4 °C, five of which had similar relative molecular masses to heat-shock protein families. There were numerous qualitative differences in the heat shock protein profiles between the roots grown at 20 and 30 °C; the 30 °C-grown roots expressed several unique heat shock protein families.Key words: heat-shock protein(s), cactus, thermal stress, acclimation.

Mammalian lymphocytes: stress-induced synthesis of heat-shock proteins in vitro and in vivo

1985 ◽  
Vol 63 (7) ◽  
pp. 711-722 ◽  
Author(s):  
David Rodenhiser ◽  
Jack H. Jung ◽  
Burr G. Atkinson
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
White Blood Cells ◽  
Sodium Dodecyl ◽  
Molecular Masses ◽  
Febrile Episodes ◽  
Shock Proteins ◽  
Mouse Lymphocytes

Mammalian (human, mouse, and rabbit) white blood cells (lymphocytes) maintained in culture respond to a brief incubation at an elevated temperature (at or above 41 °C) by (i) the new and (or) enhanced synthesis of a small number of proteins (the so-called heat-shock proteins; HSPs) having molecular masses of approximately 110 000, 100 000, 90 000, 70 000, 65 000, and 26 000 daltons and (ii) the depressed synthesis of proteins normally made at 37 °C. The HSPs synthesized in culture by human, rabbit, and mouse (peripheral and splenic) lymphocytes are similar in number, molecular mass, and distribution on two-dimensional (isoelectric focusing and sodium dodecyl sulfate – polyacrylamide) electrophoretic gels to those synthesized in vivo by lymphocytes in hyperthermic mice. Since the level of hyperthermia used to induce HSP synthesis in mouse lymphocytes in vitro and in vivo is of a magnitude (41 °C) also used to promote thermotolerance in mice and is similar to temperatures attained during febrile episodes in rabbits and in humans, we suggest that the in vitro and in vivo synthesis of HSPs by mouse lymphocytes, demonstrated in this study, represents a relevant, physiological response which mammalian lymphocytes may normally use to survive periods of thermal stress.

Heat-shock response in Legionella pneumophila

1988 ◽  
Vol 34 (10) ◽  
pp. 1148-1153 ◽  
Author(s):  
Michael W. Lema ◽  
Arnold Brown ◽  
Charles A. Butler ◽  
Paul S. Hoffman
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Legionella Pneumophila ◽  
Heat Shock Response ◽  
Temperature Shift ◽  
Bacterial Cells ◽  
Groel Protein ◽  
Shock Response ◽  
Molecular Masses ◽  
Shock Proteins

The heat-shock response of Legionella pneumophila was examined by radiolabelling bacterial cell proteins with [35S]methionine following a temperature shift from 30 to 42 °C. Five heat-shock proteins were identified as having molecular masses of 17, 60, 70, 78, and 85 kilodaltons (kDa). The 85- and 60-kDa proteins were equally distributed between supernatant and pellet fractions following ultracentrifugation at 100 000 × g, the 70- and 78-kDa proteins were found primarily in the supernatant, and the 17-kDa protein was found primarily in the pellet. Synthesis of subsets of the heat-shock proteins could be stimulated by novobiocin, patulin, or puromycin. Ethanol, an effector of the heat-shock response in other microorganisms, had little effect on L. pneumophila, even at the highest concentration tolerated by the bacterial cells (1.9%). Finally, the 60-kDa heat-shock protein of L. pneumophila was immunologically cross-reactive with a polyclonal antibody prepared to the Escherichia coli groEL protein. However, a mouse monoclonal antibody reactive with the 60-kDa protein of all legionellae tested did not cross-react with the E. coli groEL protein, suggesting that the Legionella 60-kDa protein contains common and unique epitopes.

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