THE EXPANDING SMALL HEAT-SHOCK PROTEIN FAMILY, AND STRUCTURE PREDICTIONS OF THE CONSERVED ALPHA-CRYSTALLIN DOMAIN

被引:304
作者
CASPERS, GJ
LEUNISSEN, JAM
DEJONG, WW
机构
[1] CATHOLIC UNIV NIJMEGEN,DEPT BIOCHEM,6500 HB NIJMEGEN,NETHERLANDS
[2] UNIV NIJMEGEN,CAOS CAMM CTR,NIJMEGEN,NETHERLANDS
[3] UNIV AMSTERDAM,INT TAXONOM ZOOL,AMSTERDAM,NETHERLANDS
关键词
MOLECULAR CHAPERONES; MOLECULAR PHYLOGENY; MOLECULAR EVOLUTION; STRUCTURAL DOMAINS; STRUCTURE PREDICTION;
D O I
10.1007/BF00163229
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ever-increasing number of proteins identified as belonging to the family of small heat-shock proteins (shsps) and alpha-crystallins enables us to reassess the phylogeny of this ubiquitous protein family. While the prokaryotic and fungal representatives are not properly resolved, most of the plant and animal shsps and related proteins are clearly grouped in distinct clades, reflecting a history of repeated gene duplications. The members of the shsp family are characterized by the presence of a conserved homologous ''alpha-crystallin domain,'' which sometimes is present in duplicate. Predictions are made of secondary structure and solvent accessibility of this domain, which together with hydropathy profiles and intron positions support the presence of two similar hydrophobic beta-sheet-rich motifs, connected by a hydrophilic alpha-helical region. Together with an overview of the newly characterized members of the shsp family, these data help to define this family as being involved as stable structural proteins and as molecular chaperones during normal development and induced under pathological and stressful conditions.
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页码:238 / 248
页数:11
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