title: An N-terminal 33-amino-acid-deletion variant of hsp25 retains oligomerization and functional properties.
abstract: The mechanism(s) by which heat shock protein 25 (hsp25) protects cells from stress may involve one or more of the biochemical properties attributed to hsp25 and other small M(r) hsp. In this report, structural and functional properties of an N-terminal 33 amino acid deletion variant of hsp25 (termed hsp25.c) were considered by comparison with hsp25. 6-His tagged recombinant hsp25 and hsp25.c (termed (H6)hsp25.a and (H6)hsp25.c) were expressed and purified. Oligomeric proteins formed and possessed properties previously attributed to hsp25. The 33 amino acid deletion represented by hsp27.c did not affect the ability of the recombinant protein to act as an inhibitor of elastase, as a molecular chaperone in the refolding of denatured citrate synthase, or as an actin-binding protein. The overexpression of either hsp25 or hsp25.c, enhanced the stress resistance of stable transformed eukaryotic cells. This N-terminal variant protein may be used in further cellular and biochemical assessment of hsp25 oligomerization and function.
authors.affiliation: Dental Research Center, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
authors.forename: Z
authors.initials: Z
authors.lastname: Guo
authors.forename: L F
authors.initials: LF
authors.lastname: Cooper
mesh_terms: D000199:Actins / Q000378:metabolism; D002950:Citrate (si)-Synthase / Q000378:metabolism; D014644:Genetic Variation; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D011485:Protein Binding; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017384:Sequence Deletion
chemical_list: D000199:Actins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D009363:Neoplasm Proteins; D011994:Recombinant Proteins; D002950:Citrate (si)-Synthase; D010196:Pancreatic Elastase