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  • Title: Maintenance of chaperone-like activity despite mutations in a conserved region of murine lens alphaB crystallin.
    Author: Hepburne-Scott HW, Crabbe MJ.
    Journal: Mol Vis; 1999 Aug 10; 5():15. PubMed ID: 10445957.
    Abstract:
    PURPOSE: To understand the relationship between certain conserved residues in alphaB crystallin and the chaperone-like function of the protein. METHODS: In alphaB crystallin, residues H101 to R120 are highly conserved between alphaB crystallin and alphaA crystallin (85% identity), and between alphaB crystallin and the small heat shock protein hsp 27 (80% identity). We made three substitution mutants of alphaB crystallin: the single mutant F118A, and the double mutants K103L/H104I, and E110H/H111E. RESULTS: Polyacrylamide gel electrophoresis revealed no decrease in aggregate size or measureable structural changes between them and the native structure. Using the insulin aggregation assay, all three mutants had identical chaperone-like activity to the wild-type recombinant alphaB crystallin. CONCLUSIONS: Despite the high conservation in this area of sequence between alphaB crystallin, alphaA crystallin, and the small heat shock protein hsp 27, mutations F118A, K103L/H104I, and E110H/H111E did not significantly alter chaperone-like activity.
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