Title :
Characterization of Chloroplast Hsp90 Homologue
Author :
Ratnayake, R. M Udayangani ; Kakinuma, Yoshimi ; Akita, Mitsuru
Author_Institution :
United Grad. Sch. of Agric. Sci. & Fac. of Agric., Ehime Univ., Matsuyama
Abstract :
Members of the 90-kDa heat shock protein (HSP90) family regulate diverse cellular processes acting as molecular chaperones from prokaryotes to eukaryotes interacting with various proteins, cochaperones and other chaperones. As there is little information available about the functions of organelle Hsp90s in higher plants, this research was designed to characterize chloroplast-targeted Arabidopsis homologues of Hsp90 (AtHsp90). We identified the respective Arabidopsis homologue from the Arabidopsis thaliana databases, which had the higher plastid localizing probability by in silico analysis. C-terminally modified precursor type of AtHsp90 was successfully imported in vitro into pea chloroplasts. The processed, mature AtHsp90 was recovered in the soluble stroma extracts after post-import protease treatments, confirming its localization at the stroma. Possible functions of stromal Hsp90s are discussed.
Keywords :
botany; cellular biophysics; molecular biophysics; proteins; 90 kDa heat shock protein; Arabidopsis thaliana; C terminally modified AtHsp90 precursor type; HSP90 family; cellular process regulation; chloroplast Hsp90 homologue characterization; chloroplast targeted Arabidopsis Hsp90 homologues; higher plants; in silico analysis; molecular chaperones; molecular cochaperones; organelle Hsp90 functions; pea chloroplasts; plastid localizing probability; proteins; Agriculture; Bioinformatics; Databases; Electric shock; Genomics; In vitro; Peptides; Proteins; Temperature; Web server;
Conference_Titel :
Bioinformatics and Biomedical Engineering, 2008. ICBBE 2008. The 2nd International Conference on
Conference_Location :
Shanghai
Print_ISBN :
978-1-4244-1747-6
Electronic_ISBN :
978-1-4244-1748-3
DOI :
10.1109/ICBBE.2008.41