千里光热激蛋白90-3(Hsp90-3)的生物信息学与功能分析  

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

作　　者：平军娇[1,2] 张珍[1] 蔡振锋[1] 汤贤春[1] 钱刚[1] 

机构地区：[1]遵义医学院细胞生物学与遗传学教研室,贵州遵义563099 [2]中山市第三人民医院,广东中山528400

出　　处：《植物科学学报》2012年第4期385-393,共9页Plant Science Journal

基　　金：贵州省优秀科技教育人才省长基金项目(黔省专合字2008-61号)

摘　　要：Hsp90是真核细胞重要的一类分子伴侣,与植物的生长发育、抗逆性、信号转导及生物进化等功能密切相关。为了深入理解高等植物Hsp90结构与功能的关系,该研究从千里光(Senecio scandens)全长cDNA文库中分离到Hsp90-3基因。序列分析结果表明,该基因编码699个氨基酸的多肽,与拟南芥(Arabidopsis thaliana)AtHsp90-3(登录号:NP_200412.1)的同源性最高,为93.71%;预测蛋白质的分子量为79.78 kD,理论等电点为5.08。信号序列分析结果发现,该蛋白主要定位于细胞的细胞核、过氧化物酶体、叶绿体类囊体膜及叶绿体基质中,提示作为分子伴侣,高等植物Hsp90-3参与细胞内膜系统蛋白质的转运。结构与功能分析发现,该蛋白有3个结构域及1个连接区,推测Hsp90-3在真核细胞的信号转导、转录调控及胁迫表达等过程中发挥重要功能。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 endomembrahe 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.

关 键 词：千里光 Hsp90-3基因 结构预测 序列分析 

分 类 号：Q7[生物学—分子生物学] Q943