HSP Transcript and Protein Accumulation in Brassinosteroid Barley Mutants Acclimated to Low and High Temperatures
In temperature stress, the main role of heat-shock proteins (HSP) is to act as molecular chaperones for other cellular proteins. However, knowledge about the hormonal regulation of the production of the HSP is quite limited. Specifically, little is known about the role of the plant steroid hormones&...
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2020-03-01
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author | Iwona Sadura Marta Libik-Konieczny Barbara Jurczyk Damian Gruszka Anna Janeczko |
author_facet | Iwona Sadura Marta Libik-Konieczny Barbara Jurczyk Damian Gruszka Anna Janeczko |
author_sort | Iwona Sadura |
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description | In temperature stress, the main role of heat-shock proteins (HSP) is to act as molecular chaperones for other cellular proteins. However, knowledge about the hormonal regulation of the production of the HSP is quite limited. Specifically, little is known about the role of the plant steroid hormones—brassinosteroids (BR)—in regulating the HSP expression. The aim of our study was to answer the question of how a BR deficit or disturbances in its signaling affect the accumulation of the HSP90, HSP70, HSP18, and HSP17 transcripts and protein in barley growing at 20 °C (control) and during the acclimation of plants at 5 °C and 27 °C. In barley, the temperature of plant growth modified the expression of HSPs. Furthermore, the BR-deficient mutants (mutations in the <i>HvDWARF</i> or <i>HvCPD</i> genes) and BR-signaling mutants (mutation in the <i>HvBRI1</i> gene) were characterized by altered levels of the transcripts and proteins of the HSP group compared to the wild type. The BR-signaling mutant was characterized by a decreased level of the <i>HSP</i> transcripts and heat-shock proteins. In the BR-deficient mutants, there were temperature-dependent cases when the decreased accumulation of the <i>HSP70</i> and <i>HSP90</i> transcripts was connected to an increased accumulation of these HSP. The significance of changes in the accumulation of HSPs during acclimation at 27 °C and 5 °C is discussed in the context of the altered tolerance to more extreme temperatures of the studied mutants (i.e., heat stress and frost, respectively). |
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spelling | doaj.art-7ab266100faf4574b742cf4eb0e83dd22022-12-22T03:49:44ZengMDPI AGInternational Journal of Molecular Sciences1422-00672020-03-01215188910.3390/ijms21051889ijms21051889HSP Transcript and Protein Accumulation in Brassinosteroid Barley Mutants Acclimated to Low and High TemperaturesIwona Sadura0Marta Libik-Konieczny1Barbara Jurczyk2Damian Gruszka3Anna Janeczko4Polish Academy of Sciences, The Franciszek Górski Institute of Plant Physiology, Niezapominajek 21, 30-239 Kraków, PolandPolish Academy of Sciences, The Franciszek Górski Institute of Plant Physiology, Niezapominajek 21, 30-239 Kraków, PolandDepartment of Plant Physiology, University of Agriculture in Kraków, Podłużna 3, 30-239 Kraków, PolandInstitute of Biology, Biotechnology and Environmental Protection, Faculty of Natural Sciences, University of Silesia, Jagiellońska 28, 40-032 Katowice, PolandPolish Academy of Sciences, The Franciszek Górski Institute of Plant Physiology, Niezapominajek 21, 30-239 Kraków, PolandIn temperature stress, the main role of heat-shock proteins (HSP) is to act as molecular chaperones for other cellular proteins. However, knowledge about the hormonal regulation of the production of the HSP is quite limited. Specifically, little is known about the role of the plant steroid hormones—brassinosteroids (BR)—in regulating the HSP expression. The aim of our study was to answer the question of how a BR deficit or disturbances in its signaling affect the accumulation of the HSP90, HSP70, HSP18, and HSP17 transcripts and protein in barley growing at 20 °C (control) and during the acclimation of plants at 5 °C and 27 °C. In barley, the temperature of plant growth modified the expression of HSPs. Furthermore, the BR-deficient mutants (mutations in the <i>HvDWARF</i> or <i>HvCPD</i> genes) and BR-signaling mutants (mutation in the <i>HvBRI1</i> gene) were characterized by altered levels of the transcripts and proteins of the HSP group compared to the wild type. The BR-signaling mutant was characterized by a decreased level of the <i>HSP</i> transcripts and heat-shock proteins. In the BR-deficient mutants, there were temperature-dependent cases when the decreased accumulation of the <i>HSP70</i> and <i>HSP90</i> transcripts was connected to an increased accumulation of these HSP. The significance of changes in the accumulation of HSPs during acclimation at 27 °C and 5 °C is discussed in the context of the altered tolerance to more extreme temperatures of the studied mutants (i.e., heat stress and frost, respectively).https://www.mdpi.com/1422-0067/21/5/1889brassinosteroidsacclimation processsmall hsps (shsps)hsp70hsp90temperature stress |
spellingShingle | Iwona Sadura Marta Libik-Konieczny Barbara Jurczyk Damian Gruszka Anna Janeczko HSP Transcript and Protein Accumulation in Brassinosteroid Barley Mutants Acclimated to Low and High Temperatures International Journal of Molecular Sciences brassinosteroids acclimation process small hsps (shsps) hsp70 hsp90 temperature stress |
title | HSP Transcript and Protein Accumulation in Brassinosteroid Barley Mutants Acclimated to Low and High Temperatures |
title_full | HSP Transcript and Protein Accumulation in Brassinosteroid Barley Mutants Acclimated to Low and High Temperatures |
title_fullStr | HSP Transcript and Protein Accumulation in Brassinosteroid Barley Mutants Acclimated to Low and High Temperatures |
title_full_unstemmed | HSP Transcript and Protein Accumulation in Brassinosteroid Barley Mutants Acclimated to Low and High Temperatures |
title_short | HSP Transcript and Protein Accumulation in Brassinosteroid Barley Mutants Acclimated to Low and High Temperatures |
title_sort | hsp transcript and protein accumulation in brassinosteroid barley mutants acclimated to low and high temperatures |
topic | brassinosteroids acclimation process small hsps (shsps) hsp70 hsp90 temperature stress |
url | https://www.mdpi.com/1422-0067/21/5/1889 |
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