Temperature-stress response in maize: a comparison of several cultivars

1986 ◽  
Vol 28 (6) ◽  
pp. 1125-1131 ◽  
Author(s):  
Reza K. Yacoob ◽  
W. Gary Filion
Keyword(s):  
Molecular Weight ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cold Tolerance ◽  
Cold Shock ◽  
Polyclonal Antibodies ◽  
Cross Reactivity ◽  
Species Variation ◽  
Cold Shock Response ◽  
Shock Response

The protein synthetic response to a heat (28–41 °C) and a cold (28–4 °C) shock was studied in seedlings from 10 cultivars of maize with varying levels of cold tolerance. This response was compared by fluorography of one-dimensional polyacrylamide gels and immunoblot analysis. We utilized polyclonal antibodies against the 18 000 dalton (Da) heat-shock protein and the 73 000–89 000 Da heat-shock protein complex from Oh43 maize seedlings to ascertain antigenic similarity of these polypeptides. The heat-shock response varied in the numbers and relative molecular masses of the heat-shock proteins. Only three polypeptides appeared to be conserved across cultivars: a 93 000, 71 000, and 18 000 Da polypeptide. The cold-shock response varied from none to a dramatically altered pattern in a few cultivars. Thus, the heat- and cold-shock responses in these cultivars of corn differ in the types of polypeptides that are induced. All cultivars showed varying degrees of cross-reactivity when probed with the anti 18 000 Da heat-shock protein antibody. The inbred lines appeared to respond more to a cold shock than the hybrid lines but there was little relationship between the cold tolerance and the induction of a cold-shock response. Two of the cultivars demonstrated unique binding to a higher molecular weight polypeptide under control (28 °C) conditions. These data suggest that within species variation in both number and relative molecular weight of thermal stress polypeptides (heat and cold) is a function of genotype.Key words: heat shock, cold shock, cold tolerance, maize, gene expression.

The effects of cold-temperature stress on gene expression in maize

1987 ◽  
Vol 65 (2) ◽  
pp. 112-119 ◽  
Author(s):  
Reza K. Yacoob ◽  
W. Gary Filion
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cold Shock ◽  
Incubation Temperature ◽  
Polyclonal Antibodies ◽  
Cold Shock Response ◽  
Shock Response ◽  
Acclimation Response ◽  
Molecular Masses ◽  
Shock Proteins

A rapid decrease from the 28 °C incubation temperature of 5-day-old maize seedlings induced a response recorded as an altered synthesis of several polypeptides. The maximum response occurred at 4 °C and included cold-shock proteins with relative molecular masses of 94, 92, 90, 73, 70, 54, 50, 44, 38, 34, 33, 32, 24, 20, and 14 kilodaltons (kDa). Western bolt analysis (probed with polyclonal antibodies against maize heat-shock proteins) and fluorograms prepared from one-dimensional gel electrophoresis of maize heat-shock proteins revealed differences between the cold-induced polypeptides and the maize heat-shock proteins. The abundance of low molecular weight polypeptides and the absence of a marked depression in normal protein synthesis were the most noted differences from the heat-shock response. The cold-shock response, which was induced by as little as a 3 °C reduction in temperature, showed some transitory proteins, was separate from an acclimation response, and lasted up to 18 h (after returning the seedlings to 28 °C) before the normal protein synthetic pattern returned. Seedlings allowed to recover from a 4 °C shock for 4 h at 28 °C showed synthesis of a 250-kDa polypeptide, which lasted less than 2 h and was completely inhibited by actinomycin D.

scholarly journals Transcriptomic time-series analysis of cold- and heat-shock response in psychrotrophic lactic acid bacteria

2020 ◽  
Author(s):  
Ilhan Cem Duru ◽  
Anne Ylinen ◽  
Sergei Belanov ◽  
Alan Ávila Pulido ◽  
Lars Paulin ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Heat Shock ◽  
Lactic Acid Bacteria ◽  
Heat Shock Response ◽  
Network Inference ◽  
Cold Shock ◽  
Cold Shock Protein ◽  
Gene Network Inference ◽  
Cold Shock Response ◽  
Shock Response

Abstract Background: Psychrotrophic lactic acid bacteria (LAB) species are the dominant species in microbiota of cold-stored modified-atmosphere-packaged food products and they are the main cause of food spoilage. But still, the cold- and heat-shock response of the spoilage-related psychrotrophic lactic acid bacteria has not been studied. Here, to study cold- and heat-shock response of spoilage lactic acid bacteria, we performed time-series RNA-seq for Le. gelidum, Lc. piscium and P. oligofermentans using temperatures of 0 °C, 4 °C, 14 °C, 25 °C and 28 °C. Results: We showed that the cold-shock protein A (cspA) gene was the main cold-shock protein gene among cold-shock protein genes in all three species. Our results indicated DEAD-box RNA helicase genes (cshA, cshB) play a critical role in cold-shock response in psychrotrophic LAB. In addition, several RNase genes were also involved in cold-shock response in Lc. piscium and P. oligofermentans. Moreover, gene network inference analysis provided candidate genes involved in cold-shock response. Ribosomal proteins, tRNA modification, rRNA modification, and ABC and efflux MFS transporter genes clustered with cold-shock response genes in all three species, which was a strong indication that these genes would be part of cold-shock response machinery. Heat-shock treatment caused upregulation of Clp protease and chaperone genes in all three species and we were able to identify transcription binding site motifs for heat-shock response genes in Le. gelidum and Lc. piscium. Finally, we showed that food spoilage-related genes were upregulated at cold temperatures. Conclusions: The results of this study provide new insights into a better understanding of the cold- and heat-shock response in psychrotrophic LAB. In addition, candidate genes involved in cold- and heat-shock response predicted using gene network inference analysis could be used as a target for future studies.

Immunochemical analysis of heat-shock protein synthesis in maize (Zea mays L.)

1986 ◽  
Vol 28 (6) ◽  
pp. 1076-1087 ◽  
Author(s):  
Chris L. Baszczynski
Keyword(s):  
Molecular Weight ◽  
Heat Shock ◽  
Molecular Mass ◽  
High Molecular Weight ◽  
Polyclonal Antibodies ◽  
Cross Reactivity ◽  
Antigenic Determinants ◽  
Genetic Stocks ◽  
Young Leaves ◽  
Shock Proteins

Polyclonal antibodies to 18-kilodalton (kDa) heat-shock proteins (HSPs) and to the high molecular weight (73 000 – 89 000) HSPs from 5- day-old maize plumules have been produced in rabbits. The antisera to high molecular weight HSPs show minor cross-reactivity to proteins of similar molecular mass in not heat-shocked tissues, while antisera to 18-kDa HSPs react only with this 18-kDa HSP class. HSPs of similar molecular mass and isoelectric points in maize plumules, mesocotyls, radicles, and young leaves also have similar antigenic determinants based on positive reactions with antisera to plumule HSPs. Among 13 maize inbreds and genetic stocks tested, differences were noted in the amount of immunoprecipitable 18-kDa HSPs. Antisera to maize plumule HSPs also showed cross-reactivity with similar-sized HSPs from pea epicotyls and soybean hypocotyls but not with HSPs from several animal tissues.Key words: polyclonal antibodies, maize, heat-shock.

scholarly journals Transcriptomic time-series analysis of cold- and heat-shock response in psychrotrophic lactic acid bacteria

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Ilhan Cem Duru ◽  
Anne Ylinen ◽  
Sergei Belanov ◽  
Alan Avila Pulido ◽  
Lars Paulin ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Heat Shock ◽  
Lactic Acid Bacteria ◽  
Heat Shock Response ◽  
Network Inference ◽  
Cold Shock ◽  
Cold Shock Protein ◽  
Gene Network Inference ◽  
Cold Shock Response ◽  
Shock Response

Abstract Background Psychrotrophic lactic acid bacteria (LAB) species are the dominant species in the microbiota of cold-stored modified-atmosphere-packaged food products and are the main cause of food spoilage. Despite the importance of psychrotrophic LAB, their response to cold or heat has not been studied. Here, we studied the transcriptome-level cold- and heat-shock response of spoilage lactic acid bacteria with time-series RNA-seq for Le. gelidum, Lc. piscium, and P. oligofermentans at 0 °C, 4 °C, 14 °C, 25 °C, and 28 °C. Results We observed that the cold-shock protein A (cspA) gene was the main cold-shock protein gene in all three species. Our results indicated that DEAD-box RNA helicase genes (cshA, cshB) also play a critical role in cold-shock response in psychrotrophic LAB. In addition, several RNase genes were involved in cold-shock response in Lc. piscium and P. oligofermentans. Moreover, gene network inference analysis provided candidate genes involved in cold-shock response. Ribosomal proteins, tRNA modification, rRNA modification, and ABC and efflux MFS transporter genes clustered with cold-shock response genes in all three species, indicating that these genes could be part of the cold-shock response machinery. Heat-shock treatment caused upregulation of Clp protease and chaperone genes in all three species. We identified transcription binding site motifs for heat-shock response genes in Le. gelidum and Lc. piscium. Finally, we showed that food spoilage-related genes were upregulated at cold temperatures. Conclusions The results of this study provide new insights on the cold- and heat-shock response of psychrotrophic LAB. In addition, candidate genes involved in cold- and heat-shock response predicted using gene network inference analysis could be used as targets for future studies.

C-terminal heat shock protein 90 modulators produce desirable oncogenic properties

2015 ◽  
Vol 13 (16) ◽  
pp. 4627-4631 ◽  
Author(s):  
Y. Wang ◽  
S. R. McAlpine
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Response ◽  
Heat Shock Protein 90 ◽  
Cellular Protection ◽  
Protection Mechanism ◽  
C Terminus ◽  
N Terminus ◽  
Shock Response

The cellular protection mechanism, the heat shock response, is only activated by classical heat shock 90 inhibitors (Hsp90) that “target” the N-terminus of the protein, but not by those that modulate the C-terminus.

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