Genome-Wide Identification of <i>Hsp90</i> Gene Family in Perennial Ryegrass and Expression Analysis under Various Abiotic Stresses
The heat shock protein 90 (<i>Hsp90</i>) is a protein produced in plants in response to stress. This study identified and analyzed <i>Hsp90</i> gene family members in the perennial ryegrass genome. From the results, eight <i>Hsp90</i> proteins were obtained and th...
Guardado en:
| Autores principales: | , , , , , , , |
|---|---|
| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
MDPI AG
2021
|
| Materias: | |
| Acceso en línea: | https://doaj.org/article/d800e965dc53497db9de5ed77e0f91f0 |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| Sumario: | The heat shock protein 90 (<i>Hsp90</i>) is a protein produced in plants in response to stress. This study identified and analyzed <i>Hsp90</i> gene family members in the perennial ryegrass genome. From the results, eight <i>Hsp90</i> proteins were obtained and their MW, pI and number of amino acid bases varied. The amino acid bases ranged from 526 to 862. The CDS also ranged from 20 (<i>LpHsp0-4</i>) to 1 <i>(LpHsp90-5</i>). The least number of CDS regions was 1 (<i>LpHsp90-5</i>) with 528 kb amino acids, while the highest was 20 (<i>LpHsp90-4</i>) with 862 kb amino acids, which showed diversity among the protein sequences. The phylogenetic tree revealed that <i>Hsp90</i> genes in <i>Lolium perenne</i>, <i>Arabidopsis thaliana</i>, <i>Oryza sativa</i> and <i>Brachypodium distachyon</i> could be divided into two groups with five paralogous gene pairs and three orthologous gene pairs. The expression analysis after perennial ryegrass was subjected to heat, salt, chromium (Cr), cadmium (Cd), polyethylene glycol (PEG) and abscisic acid (ABA) revealed that <i>LpHsp90</i> genes were generally highly expressed under heat stress, but only two <i>LpHsp90</i> proteins were expressed under Cr stresses. Additionally, the expression of the <i>LpHsp90</i> proteins differed at each time point in all treatments. This study provides the basis for an understanding of the functions of <i>LpHsp90</i> proteins in abiotic stress studies and in plant breeding. |
|---|