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PING Jun-Jiao, ZHANG Zhen, CAI Zhen-Feng, TANG Xian-Chun, QIAN Gang. Functional Roles of Heat Shock Proteins 90-3(Hsp90-3) in Senecio scandens Buch.-Ham.ex D.Don Based on Its Bioinformatics[J]. Plant Science Journal, 2012, 30(4): 385-393. DOI: 10.3724/SP.J.1142.2012.40385
Citation: PING Jun-Jiao, ZHANG Zhen, CAI Zhen-Feng, TANG Xian-Chun, QIAN Gang. Functional Roles of Heat Shock Proteins 90-3(Hsp90-3) in Senecio scandens Buch.-Ham.ex D.Don Based on Its Bioinformatics[J]. Plant Science Journal, 2012, 30(4): 385-393. DOI: 10.3724/SP.J.1142.2012.40385

Functional Roles of Heat Shock Proteins 90-3(Hsp90-3) in Senecio scandens Buch.-Ham.ex D.Don Based on Its Bioinformatics

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  • Received Date: February 23, 2012
  • Revised Date: June 26, 2012
  • Published Date: August 29, 2012
  • Heat shock proteins (Hsp),representing an important molecular chaperone in eukaryotic cells,is a common response to development,stress resistance,signal transduction and evolution of plants.The relationship between the structure and functional roles was elucidated in Hsp90 based on the generation of full-length cDNAs from Senecio scandens Buch.-Ham.ex D.Don.Sequence analysis of Hsp90-3 gene indicated that it shared 93.71% identity with Arabidopsis thaliana (GenBank accession: NP_200412.1),encoding a protein composed of 699 amino acid residues with the predicted molecular weight of 79.78 kD and theoretical isoelectric point of 5.08.Moreover,the distribution of Hsp90-3 was involved in the endomembrane system such as nuclei,peroxisomes,chloroplast thylakoid membranes,and chloroplast matrices in the present study.Three-dimensional measurement revealed that the Hsp90-3 protein was composed of three structural domains and one link region.These results suggested that Hsp90-3 played a critical role in molecular chaperone,signal transduction,transcriptional regulation and stress-response in higher plants.
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