Interaction Studies of Heat Shock Responsive Protein HSA32 and Heat Shock Protein HSP101: An In Silico Approach

Abstract

Research ArticleABSTRACT Heat shock responsive protein HSA32 is a good candidate responsible for heat stress tolerance in crop plants. It interacts with other proteins in a signaling pathway which results its regulation of gene expression in response to heat shock. HSP101 is such protein which in combination with HSA32 is essential to thermotolerance in crop plants. In this study, we constructed 3-D structures of the two proteins. Hypothetical point mutations were also induced in HSA32 protein at amino acid position 27, 91, 159 and 220 and their 3-D models were developed. Then, protein -protein interaction was studied between two proteins. Our results showed that HSA32 and HSP101 proteins interact with each other in the active binding sites. It was also found that mutants HSA32 E<Q at amino acid position 91 and HSA32 G<A at the position 159 were interacting with HSP101 protein while HSA32 E<G at position 27 and HSA32 K<R showed no interaction with HSP101 protein. So, it is concluded that HSA32 interacts with HSP101 protein and both in combination are responsible for the acquired thermotolerance in crop plants. It is also concluded that point mutations in the protein active binding sites results in loss of function and there is no positive interaction between two proteins.

Identification and functional analysis of new conserved microRNAs and their targets in potato (Solanum tuberosum L.)

“…One such important protein group is heat shock proteins (HSPs), which are targeted by stu-miR1320 and 5035. The fine-tuning of HSPs via plant miRNAs can enhance plant tolerance for cold, heat, salt, and drought stresses (Mahmood-ur-Rahman et al, 2013). This finding is in agreement with many other studies (Gao et al, 2011;Bai et al, 2012;Chen et al, 2012).…”