The lack of chaperonelike activity of Caenorhabditis elegans Hsp12.2 cannot be restored by domain swapping with human αB-crystallin

Cell Stress and Chaperones

Volumn 6, Issue 4, 2001, Pages 360-367

  Kokke, B P A ^a   Boelens, W C ^a   De Jong, W W ^a  

^a RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; ALPHA,BETA CRYSTALLIN; BETA CRYSTALLIN; CHAPERONE; CHIMERIC PROTEIN; CRYSTALLIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 12; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BIOENGINEERING; CAENORHABDITIS ELEGANS; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; COMPLEX FORMATION; GEL PERMEATION CHROMATOGRAPHY; HUMAN; MOLECULAR SIZE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; CIRCULAR DICHROISM; CLONING, MOLECULAR; CONSERVED SEQUENCE; CRYSTALLINS; HEAT; HEAT-SHOCK PROTEINS; HUMANS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT;

CAENORHABDITIS ELEGANS;

EID: 0035195006     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/1466-1268(2001)006<0360:TLOCAO>2.0.CO;2     Document Type: Article

References (28)

1. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α-crystallin
2. Genealogy of the α-crystallin-small heat-shock protein superfamily
3. Primary structures of the α-crystallin A chains of twenty-eight mammalian species, chicken and frog
4. Chaperone function of mutant versions of αA- and αB-crystallin prepared to pinpoint chaperone binding sites
5. HSP25, a small heat shock protein associated with dense bodies and M-lines of body wall muscle in Caenorhabditis elegans
6. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
7. Stabilization of proteins and peptides in diagnostic immunological assays by the molecular chaperone Hsp25
8. Interaction of α-crystallin with spin-labeled peptides
9. Functional characterization of Xenopus small heat shock protein, Hsp30C: The carboxyl end is required for stability and chaperone activity
10. Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
11. Hsp26: A temperature-regulated chaperone
12. α-crystallin can function as a molecular chaperone
13. Mutation of αB-crystallin: Effects on chaperone-like activity
14. Crystal structure of a small heat-shock protein
15. Caenorhabditis elegans small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like ability
16. Folding pattern of the α-crystallin domain in αA-crystallin determined by site-directed spin labeling
17. Domain swapping in human αA and αB crystallins affects oligomerization and enhances chaperonelike activity
18. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
19. Unique structural features of a novel class of small heat shock proteins
20. Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides
21. Mouse Hsp25, a small heat shock protein
22. Molten-globule state of carbonic anhydrase binds to the chaperone-like α-crystallin
23. Chaperone-like activity and quaternary structure of α-crystallin
24. Functional elements in molecular chaperone α-crystallin: Identification of binding sites in αB-crystallin
25. Synthesis and characterization of a peptide identified as a functional unit in αA-crystallin
26. Identification of possible regions of chaperone activity in lens α-crystallin
27. Immobilization of the C-terminal extension of bovine αA-crystallin reduces chaperone-like activity
28. Intermolecular exchange and stabilization of recombinant human αA- and αB-crystallin