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- ********************************************
- * Heat shock hsp20 proteins family profile *
- ********************************************
-
- Prokaryotic and eukaryotic organisms respond to heat shock or other
- environmental stress by the induction of the synthesis of proteins
- collectively known as heat-shock proteins (hsp) [1]. Amongst them is a family
- of proteins with an average molecular weight of 20 Kd, known as the hsp20
- proteins [2,3,4] and which seem to act as chaperones that can protect other
- proteins against heat-induced denaturation and aggregation. The hsp20 proteins
- seem to to form large heterooligomeric aggregates. The hsp20 family is
- currently composed of the following members:
-
- - Vertebrate heat shock protein hsp27 (hsp25), which are induced by a variety
- of environmental stresses.
- - Drosophila heat shock proteins hsp22, hsp23, hsp26, hsp27, hsp67BA and BC.
- - Caenorhabditis elegans hsp16 multigene family.
- - Fungal HSP26 (budding yeast) and hsp30 (Neurospora crassa).
- - Plant small hsps. Plants have four classes of hsp20: class I and II which
- are cytoplasmic; class III which is in the chloroplast and class IV which
- is in the endomembrane.
- - Alpha-crystallin A and B chains. Alpha-crystallin is an abundant
- constituent of the eye lens of most vertebrate species. Its main function
- appears to be the maintenance of the correct refractive index of the lens.
- It is also found in other tissues where it seems to act as a chaperone.
- - Schistosoma mansoni major egg antigen p40. Structurally p40 is built of two
- tandem hsp20 domains.
- - A variety of prokaryotic proteins: ibpA and ibpB from Escherichia coli;
- hsp18 from Clostridium acetobutylicum; spore protein SP21 (hspA) from
- Stigmatella aurantiaca; Mycobacterium leprae 18 Kd antigen; Mycobacterium
- tuberculosis 14 Kd antigen.
-
- Structurally, this family is characterized by the presence of a conserved C-
- terminal domain of about 100 residues. The profile developed to detect members
- of the hsp20 family is based on an alignment of this domain.
-
- -Sequences known to belong to this class detected by the profile: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Note: this is the first profile entry to be integrated into PROSITE !
-
- -Expert(s) to contact by email: Leunissen J.A.M.
- jackl@caos.kun.nl
- de Jong W.W.
- u629000@hnykun11.bitnet
-
- -Last update: June 1994 / First entry.
-
- [ 1] Lindquist S., Craig E.A.
- Annu. Rev. Genet. 22:631-677(1988).
- [ 2] de Jong W.W., Leunissen J.A.M., Voorter C.E.M.
- Mol. Biol. Evol. 10:103-126(1993).
- [ 3] Jaenicke R., Creighton T.E.
- Curr. Biol. 3:234-235(1993).
- [ 4] Jakob U., Buchner J.
- Trends Biochem. Sci. 19:205-211(1994).
-