English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

AlphaB-crystallin is a member of the small heat shock protein family and is known to have chaperone activity. Using a peptide scan approach, we previously determined that regions 42-57, 60-71, and 88-123 in alphaB-crystallin interact with alphaA-crystallin during heterooligomer formation. To further characterize the significance of the N-terminal domain of alphaB-crystallin, we prepared a deletion mutant that lacks residues (54)FLRAPSWF(61) (alphaBDelta54-61) and found that the absence of residues 54-61 in alphaB-crystallin significantly decreased the homooligomeric mass of alphaB-crystallin. The average oligomeric mass of wild-type alphaB-crystallin and of alphaBDelta54-61, calculated using multiangle light scattering, was 624 and 382 kDa, respectively. The mutant subunits aggregate to form smaller, less-compact oligomers with a 4-fold increase in subunit exchange rate. Deletion of the 54-61 region resulted in a 50% decrease in intrinsic tryptophan fluorescence. The alphaBDelta54-61 mutant showed a 2-fold increase in 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid (bis-ANS) binding as compared to the wild-type protein, suggesting increased hydrophobicity of the mutant protein. Accompanying the evidence of increased hydrophobicity in the deletion mutant was a 10-fold increase in antiaggregation activity. Homooligomers of 6HalphaA (750 kDa) readily exchanged subunits with alphaBDelta54-61 homooligomers at 37 degrees C, forming heterooligomers with an intermediate mass of 625 kDa. Our data suggest that residues (54)FLRAPSWF(61) contribute to the higher order assembly of alphaB-crystallin oligomers. Residues (54)FLRAPSWF(61) in alphaB-crystallin are not essential for target protein binding during chaperone action, but this region apparently has a role in the chaperone activity of native alphaB-crystallin.

Deletion of 54FLRAPSWF61 Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of αB-Crystallin

Deletion of ⁵⁴FLRAPSWF⁶¹ Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of αB-Crystallin