Why proteins without an α-crystallin domain should not be included in the human small heat shock protein family HSPB

被引：69
作者：
Kappe, Guido [1 ]
Boelens, Wilbert C. [1 ]
de Jong, Wilfried W. [1 ]
机构：
[1] Radboud Univ Nijmegen, Nijmegen Ctr Mol Life Sci, Dept Biomol Chem 271, NL-6500 HB Nijmegen, Netherlands
来源：
CELL STRESS & CHAPERONES | 2010年 / 15卷 / 04期
关键词：
Chaperone-like; alpha-crystallin; HSPB11; Phylogeny; Protein family; Protein nomenclature; Small heat shock protein; B-CRYSTALLIN; CELL-DEATH; SUPERFAMILY; EXPRESSION; DIVERSITY; NETWORK;
D O I：
10.1007/s12192-009-0155-4
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
The presence of an alpha-crystallin domain documents the evolutionary relatedness of the ubiquitous family of small heat shock proteins. Sequence and three-dimensional structure provide no evidence for the presence of such a domain in HSPC034, recently proposed as the 11th member of the human HSPB family. Also, phylogenetic analyses detect no relationship between HSPC034 and the human HSPB1-10 sequences. Arguments are provided as to why inclusion in the HSPB family of proteins like HSPC034, which resemble small heat shock proteins in being heat-inducible and having chaperone-like properties and a low monomeric mass, but are evolutionarily unrelated, is misleading and confusing.
引用
收藏
页码：457 / 461
页数：5
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