4.3 Article

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

Journal

CELL STRESS & CHAPERONES
Volume 15, Issue 4, Pages 457-461

Publisher

SPRINGER
DOI: 10.1007/s12192-009-0155-4

Keywords

Chaperone-like; alpha-crystallin; HSPB11; Phylogeny; Protein family; Protein nomenclature; Small heat shock protein

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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.

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