AI Article Synopsis

  • Heat shock protein 90 (HSP90) plays a crucial role in various organisms, including plants, especially in response to environmental stresses like salt and drought.
  • Six and eight HSP90 genes were identified in two rose varieties, Wangxifeng and Sweet Avalanche, with phylogenetic analysis revealing distinct groups and subgroups based on their gene structures and evolutionary relationships.
  • The study identified regulatory roles for specific HSP90 genes in response to abiotic stresses and highlighted structural differences that may influence their function, providing insights for breeding stress-resistant rose varieties.

Article Abstract

Unlabelled: Heat shock protein 90 (HSP90) is important for many organisms, including plants. Based on the whole genome information, the gene number, gene structure, evolutionary relationship, protein structure, and active site of the HSP90 gene family in and were determined, and the expression of the gene under salt, and drought stresses in two rose varieties Wangxifeng and Sweet Avalanche were analyzed. Six and eight genes were identified from and , respectively. Phylogenetic analysis revealed that the analyzed genes were divided into two Groups and four subgroups (Classes 1a, 1b, 2a, and 2b). Although members within the same classes displayed highly similar gene structures, while the gene structures and conserved domains of Group 1 (Class 1a and 1b) and the Group 2 (Class 2a and 2b) are different. Tandem and segmental duplication genes were found in , but not in , perhaps explaining the difference in gene quantity in the two analyzed species. Analysis of cis-acting elements revealed abundant abiotic stress, photolight-response, and hormone-response elements in HSP90s. qRT-PCR analysis suggested that , and in Sweet Avalanche and Wangxifeng varieties played important regulatory roles under salt and drought stress. The analysis of protein structure and active sites indicate that the potential different roles of , , and in salt and drought stresses may come from the differences of corresponding protein structures and activation sites. These data will provide information for the breeding of rose varieties with high stress resistance.

Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-024-04052-0.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11330952PMC
http://dx.doi.org/10.1007/s13205-024-04052-0DOI Listing

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