A critical motif for oligomerization and chaperone activity of bacterial α-heat shock proteins

European Journal of Biochemistry

Volumn 269, Issue 14, 2002, Pages 3578-3586

  Studer, Sonja ^a   Obrist, Markus ^a   Lentze, Nicolas ^a   Narberhaus, Franz ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

crystallin; heat shock protein; Chaperone; Oligomerization; Small heat shock protein

Indexed keywords

ALPHA CRYSTALLIN; ALPHA HEAT SHOCK PROTEIN; CHAPERONE; CITRATE SYNTHASE; DIMER; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN A; HEAT SHOCK PROTEIN B; HEAT SHOCK PROTEIN C; HEAT SHOCK PROTEIN D; HEAT SHOCK PROTEIN E; HEAT SHOCK PROTEIN F; HEAT SHOCK PROTEIN H; ISOLEUCINE; PROTEIN IBPA; PROTEIN IBPB; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BRADYRHIZOBIUM JAPONICUM; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DIMERIZATION; ENZYME ASSAY; GEL FILTRATION; NONHUMAN; OLIGOMERIZATION; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PURIFICATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BRADYRHIZOBIUM; CITRATE (SI)-SYNTHASE; CRYSTALLINS; DIMERIZATION; HEAT-SHOCK PROTEINS; ISOLEUCINE; MACROMOLECULAR SUBSTANCES; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION MAPPING; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS); BRADYRHIZOBIUM; BRADYRHIZOBIUM JAPONICUM; NEGIBACTERIA; RHIZOBIUM;

EID: 0036375506     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03049.x     Document Type: Article

References (49)

1. Evolution, structure and function of the small heat shock proteins in plants
2. Expression and function of the low-molecular-weight heat shock proteins
3. Structure and function of small heat-shock proteins
4. Multiple small heat shock proteins in rhizobia
5. Genealogy of the α-crystallin - Small heat-shock protein superfamily
6. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
7. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
8. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
9. α-crystallin can function as a molecular chaperone
10. Small heat shock protein of Methanococcus jannaschii, a hyperthermophile
11. Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation
12. Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
13. Chaperone activity and homo- and hetero-oligomer formation of bacterial small heat shock proteins
14. Crystal structure of a small heat-shock protein
15. Purification and characterization of the 16-kDa heat-shock-responsive protein from the thermophilic cyanobacterium Synechococcus vulcanus, which is an α-crystallin-related, small heat shock protein
16. The unique chaperone operon of Thermotoga maritima: Cloning and initial characterization of a functional Hsp70 and small heat shock protein
17. The dynamics of Hsp25 quaternary structure - Structure and function of different oligomeric species
18. Structure and modifications of the junior chaperone α-crystallin. From lens transparency to molecular pathology
19. Subunit exchange of αA-crystallin
20. The small heat-shock protein, αB-crystallin, has a variable quaternary structure
21. Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
22. Biochemical characterization of the small heat shock protein IbpB from Escherichia coli
23. The expanding small heat-shock protein family, and structure predictions of the conserved 'α-crystallin domain'
24. Caenorhabditis elegans small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity
25. Unique structural features of a novel class of small heat shock proteins
26. Subunit exchange of small heat shock proteins - Analysis of oligomer formation of αA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations
27. Cloning, expression and chaperone-like activity of human αA-crystallin
28. Chaperone function of mutant versions of αA- and αB-crystallin prepared to pinpoint chaperone binding sites
29. Site-directed mutations within the core 'α-crystallin' domain of the small heat-shock protein, human αB-crystallin, decrease molecular chaperone functions
30. Mutations and modifications support a 'pitted-flexiball' model for α-crystallin
31. Effects of site-directed mutations on the chaperone-like activity of αB-crystallin
32. Expression and aggregation of recombinant αA-crystallin and its two domains
33. Immobilization of the C-terminal extension of bovine αA-crystallin reduces chaperone-like activity
34. Crystal structure and assembly of a eukaryotic small heat shock protein
35. Functional characterization of Xenopus small heat shock protein, Hsp30C: The carboxyl end is required for stability and chaperone activity
36. Transient expression and heat-stress-induced co-aggregation of endogenous and heterologous small heat-stress proteins in tobacco protoplasts
37. Proteome analysis of heat shock protein expression in Bradyrhizobium japonicum
38. ROSE elements occur in disparate rhizobia and are functionally interchangeable between species
39. Folding pattern of the α-crystallin domain in αA-crystallin determined by site-directed spin labeling
40. Evolution and diversity of prokaryotic small heat shock proteins
41. α-crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
42. The mammalian small heat-shock protein Hsp20 forms dimers and is a poor chaperone
43. A novel quaternary structure of the dimeric α-crystallin domain with chaperone-like activity
44. Hsp26: A temperature-regulated chaperone
45. Site-directed spin labeling study of subunit interactions in the α-crystallin domain of small heat-shock proteins - Comparison of the oligomer symmetry in αA-crystallin, HSP 27, and HSP 16.3
46. Expression and native structure of cytosolic class II small heat-shock proteins
47. Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides
48. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
49. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa