Dataset of wheat HSP90.2 chaperome

Published: 8 May 2024| Version 3 | DOI: 10.17632/fmyrz84f65.3
, Yan Yan,
, Jin-Ying Gou


Wheat (Triticum aestivum L.) is one of the world’s most important staple crops, whose production is critical to feed the expanding population worldwide. The 90-kDa Heat Shock Protein 90 (HSP90) is a highly abundant chaperone protein involved in multiple cellular processes. It facilitates the folding of nascent preproteins for their maturation and functioning. This data described HSP90.2 clients identified from the whole genome of wheat. The HSP90.2 chaperome contains over 1500 proteins, most detected by the C terminus and full-length of HSP90.2. Over 60% of the clients reside in the cytosol, nucleus, and chloroplasts. Cytoskeleton-related proteins are enriched in the chaperome of the N terminus of HSP90.2. The clients of the middle part of HSP90.2 contains several factors involved in ethylene biosynthesis and extracellular vesicle or organelle-related activities. Some clients related to plant hypersensitive response are induced by stripe rust. The presented dataset could isolate proteins regulated by HSP90.2 at the post-translational level.


Steps to reproduce

The HSP90.2-FL, HSP90.2-N, HSP90.2-M, and HSP90.2-C (HSP90.2 fragments, next after) were incorporated into the pLAW10 vector for yeast two-hybrid screening by LR clonase II. Aureobasidin (AbA) (CAT: 60231ES03, Yeasen, Shanghai, China) at 125 ng/mL inhibited the autoactivation of different TaHSP90.2 fragments. Potential clients of HSP90.2 fragments were isolated from a high coverage cDNA two-hybrid library prepared with mixed RNAs from different tissues of a hexaploid wheat Fielder (OE Biotechnology, Shanghai, China). The plates were incubated at a 28°C incubator to collect the clones to extract the plasmids for the second-generation sequencing.


Fudan University


Cereal Crop


National Natural Science Foundation of China