title: A P39R mutation at the N-terminal domain of human αB-crystallin regulates its oligomeric state and chaperone-like activity.
abstract: Recent structure analyses of αB-crystallin have proposed some models of the N-terminal domain and the manner of oligomerization, whereas the effects of the significantly high content of Pro residues at the N-terminal domain remain unclear. We report the properties of a novel P39R mutant of αB-crystallin. The content of α-helix was increased, and the molecular size of the P39R mutant was larger than that of wild-type αB-crystallin. A slight loss of chaperone-like activity was observed using alcohol dehydrogenase (ADH), while a significant increase was detected by insulin assay. The Pro residue at the N-terminal domain of αB-crystallin is important for oligomerization and function.
authors.affiliation: Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka 590-0494, Japan.
authors.forename: Nobutaka
authors.initials: N
authors.lastname: Numoto
authors.forename: Akiko
authors.initials: A
authors.lastname: Kita
authors.forename: Noriko
authors.initials: N
authors.lastname: Fujii
authors.forename: Kunio
authors.initials: K
authors.lastname: Miki
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002942:Circular Dichroism; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D017354:Point Mutation; D011392:Proline / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D038203:alpha-Crystallin B Chain / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
chemical_list: D018832:Molecular Chaperones; D011994:Recombinant Proteins; D038203:alpha-Crystallin B Chain; D001120:Arginine; D011392:Proline