The HSP90 family of genes in the human genome: Insights into their divergence and evolution

被引:300
作者
Chen, B [1 ]
Piel, WH
Gui, LM
Bruford, E
Monteiro, A
机构
[1] SUNY Buffalo, Dept Biol Sci, Buffalo, NY 14260 USA
[2] Southwest Univ, Coll Plant Protect, Chongqing 407716, Peoples R China
[3] Univ Leeds, Sch Biol, Leeds LS2 9JT, W Yorkshire, England
[4] UCL, Galton Lab, London NW1 2HE, England
基金
美国国家科学基金会;
关键词
HSP90; TRAP; gene; human; genuine; evolution; nomenclature; polymorphism;
D O I
10.1016/j.ygeno.2005.08.012
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
HSP90 proteins are important molecular chaperones. Transcriptome and genome analyses revealed that the human HSP90 family includes 17 genes that fall into four classes. A standardized nomenclature for each of these genes is presented here. Classes HSP90AA, HSP90AB, HSP90B, and TRAP contain 7, 6 3, and I genes, respectively. HSP90AA genes mapped onto chromosomes 1, 3, 4, and 11; HSP90AB genes mapped onto 3. 4, 6. 13 and 15; HSP90B genes mapped onto 1, 12, and 15; and the TRAP1 gene mapped onto 16. Six genes, HSP90AA1, HSP90AA2, HSP90N. HSP90AB1, HSP90B1 and TRAP1, were recognized as functional, and the remaining I I genes were considered putative pseudogenes. Amino acid polymorphic variants were detected for genes HSP90AA1, HSP90AA2, HSP90AB1, HSP90B1, and TRAP1. The structures of these genes and the functional motifs and polymorphic variants of their proteins were documented and the features and functions of their proteins were discussed. Phylogenetic analyses based on both nucleotide and protein data demonstrated that HSP90(AA + AB + B) formed a monophyletic clade, whereas TRAP is a relatively distant paralogue of this clade. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:627 / 637
页数:11
相关论文
共 53 条
[31]   Structural and functional analysis of the middle segment of Hsp90: Implications for ATP hydrolysis and client protein and cochaperone interactions [J].
Meyer, P ;
Prodromou, C ;
Hu, B ;
Vaughan, C ;
Roe, SM ;
Panaretou, B ;
Piper, PW ;
Pearl, LH .
MOLECULAR CELL, 2003, 11 (03) :647-658
[32]   Unique behavior of a Dictyostelium homologue of TRAP-1, coupling with differentiation of D-discoideum cells [J].
Morita, T ;
Amagai, A ;
Maeda, Y .
EXPERIMENTAL CELL RESEARCH, 2002, 280 (01) :45-54
[33]  
NADEAU K, 1993, J BIOL CHEM, V268, P1479
[34]   Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96 [J].
Nicchitta, CV .
CURRENT OPINION IN IMMUNOLOGY, 1998, 10 (01) :103-109
[35]   Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites [J].
Nielsen, H ;
Engelbrecht, J ;
Brunak, S ;
vonHeijne, G .
PROTEIN ENGINEERING, 1997, 10 (01) :1-6
[36]   In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis [J].
Obermann, WMJ ;
Sondermann, H ;
Russo, AA ;
Pavletich, NP ;
Hartl, FU .
JOURNAL OF CELL BIOLOGY, 1998, 143 (04) :901-910
[37]  
ORENGO C, 2003, BIOINFORMATICS GENES
[38]   MAPPING OF THE GENE FAMILY FOR HUMAN HEAT-SHOCK PROTEIN-90-ALPHA TO CHROMOSOME-1, CHROMOSOME-4, CHROMOSOME-11, AND CHROMOSOME-14 [J].
OZAWA, K ;
MURAKAMI, Y ;
EKI, T ;
SOEDA, E ;
YOKOYAMA, K .
GENOMICS, 1992, 12 (02) :214-220
[39]   NUCLEOTIDE-SEQUENCE OF A CDNA FOR A MEMBER OF THE HUMAN 90-KDA HEAT-SHOCK PROTEIN FAMILY [J].
REBBE, NF ;
WARE, J ;
BERTINA, RM ;
MODRICH, P ;
STAFFORD, DW .
GENE, 1987, 53 (2-3) :235-245
[40]   Hsp90 as a capacitor for morphological evolution [J].
Rutherford, SL ;
Lindquist, S .
NATURE, 1998, 396 (6709) :336-342