Type II chaperonins, prefoldin, and the tubulin-specific chaperones

Advances in Protein Chemistry

Volumn 59, Issue , 2001, Pages 73-104

  Cowan, Nicholas J ^a   Lewis, Sally A ^a  

^a NEW YORK UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA ACTIN; CHAPERONE; CHAPERONIN; PREFOLDIN; PROTEIN SUBUNIT; TUBULIN; UNCLASSIFIED DRUG;

ALLOSTERISM; ARCHAEBACTERIUM; BINDING AFFINITY; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; EUKARYOTE; MOLECULAR GENETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES POMBE; SEQUENCE HOMOLOGY;

ARCHAEA; EUKARYOTA; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE;

EID: 0035715785     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(01)59003-8     Document Type: Review

References (109)

1. Formation and function of the Rbl2p-beta-tubulin complex
2. Rbl2p, a yeast protein that binds to beta-tubulin and participates in microtubule function in vivo
3. ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin
4. Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein
5. Getting newly synthesized proteins into shape
6. Growing up in a dangerous environment: A network of multiple targeting and folding pathways for nascent polypeptides in the cytosol
7. The Hsp70 and Hsp60 chaperone machines
8. Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo
9. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
10. Isolation of separate mRNAs for alpha- and beta-tubulin and characterization of the corresponding in vitro translation products
11. Mammalian cytosolic chaperonin
12. A chaperone with a hydrophilic surface
13. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
14. Evidence that beta-tubulin induces a conformation change in the cytosolic chaperonin which stabilizes binding: Implications for the mechanism of action
15. Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
16. Disruption of six open reading frames on chromosome X of Saccharomyces cerevisiae reveals a cluster of four essential genes
17. Regulated expression of p14 (cofactor A) during spermatogenesis
18. Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms
19. AlF1p, a CLIP-170 domain-containing protein, is functionally and physically associated with alpha-tubulin
20. Protein folding in vivo: The importance of molecular chaperones
21. Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC
22. Incorporation of tubulin subunits into dimers requires GTP hydrolysis
23. Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
24. Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
25. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
26. Group II chaperonin in a thermophilic methanogen. Methanococcus thermolithotrophicus. Chaperone activity and filament-forming ability
27. A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin
28. A cytoplasmic chaperonin that catalyzes beta-actin folding
29. Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin
30. A novel protein complex promoting formation of functional alpha- and gamma-tubulin
31. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
32. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
33. Sto 1p, a fission yeast protein similar to tubulin folding cofactor E, plays an essential role in mitotic microtubule assembly
34. The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro
35. Sequence and structural homology between a mouse T-complex protein TCP-1 and the 'chaperonin' family of bacterial (GroEL, 60-65 kDa heat shock antigen) and eukaryotic proteins
36. Group II chaperonins: New TRiC(k)s and turns of a protein folding machine
37. Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins
38. Homologous plant and bacterial proteins chaperone oligomeric protein assembly
39. Purification and properties of groE, a host protein involved in bacteriophage assembly
40. Essential role of tubulin-folding cofactor D in microtubule assembly and its association with microtubules in fission yeast
41. Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly
42. Protein folding in the cell: Functions of two families of molecular chaperone, hsp 60 and TF55-TCP1
43. Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability
44. Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes
45. Peptide mass fingerprinting of chaperonin-containing TCP-1 (CCT) and copurifying proteins
46. Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of beta-actin
47. Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
48. Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
49. Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin
50. The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol
51. The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic chaperonin containing TCP-1
52. Transcriptional activation of mouse cytosolic chaperonin CCT subunit genes by heat shock factors HSF1 and HSF2
53. Structures and co-regulated expression of the genes encoding mouse cytosolic chaperonin CCT subunits
54. Transcriptional regulation of the mouse cytosolic chaperonin subunit gene Ccta/Tcp-1 by Staf family zinc finger proteins
55. MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin
56. The alpha and beta tubulin folding pathways
57. T-Complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
58. Analysis of mutationally altered forms of the Cct6 subunit of the chaperonin from Saccharomyces cerevisiae
59. The chaperonin containing TCP-1 (CCT) displays a single-ring mediated disassembly and reassembly cycle
60. Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT microcomplexes
61. Eukaryotic type II chaperonin CCT interacts with actin through specific subunits
62. 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin
63. ATP binding induces large conformational changes in the apical and equatorial domains of the eukaryotic chaperonin containing TCP-1 complex
64. A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo
65. Identification of a groES-like chaperonin in mitochondria that facilitates protein folding
66. Reversible interaction of beta-actin along the channel of the TCP-1 cytoplasmic chaperonin
67. Tubulin folding cofactor D is a microtubule destabilizing protein
68. The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking
69. Cytoplasmic chaperonin containing TCP-1: Structural and functional characterization
70. Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates
71. Cofactor A is a molecular chaperone required for beta-tubulin folding: Functional and structural characterization
72. Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta
73. Beyond self-assembly: From microtubules to morphogenesis
74. Novel isolation method and structural stability of a eukaryotic chaperonin: The TCP-1 ring complex from rabbit reticulocytes
75. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
76. Functional dissection and hierarchy of tubulin-folding cofactors in fission yeasts
77. Characterisation of fission yeast alp 11 mutants defines three functional domains within tubulin-folding cofactor B
78. A conserved small GTP-binding protein Alp41 is essential for the cofactor-dependent biogenesis of microtubules in fission yeast
79. The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins
80. Subunits of the eukaryotic cytosolic chaperonin CCT do not always behave as components of a uniform hetero-oligomeric particle
81. + and ATP
82. Cytoplasmic chaperonin complexes enter neurites developing in vitro and differ in subunit composition within single cells
83. Thermal unfolding of G-actin monitored with the DNase 1-inhibition assay stabilities of actin isoforms
84. Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
85. Myosin II folding is mediated by a molecular chaperonin
86. Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function
87. Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p
88. Review: The Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts
89. Use of T7 RNA polymerase to direct expression of cloned genes
90. In vivo newly translated polypeptides are sequestered in a protected folding environment
91. Tubulin folding cofactors as GTPase activating proteins: GTP hydrolysis and the assembly of the alpha/beta tubulin heterodimer
92. Pathway leading to correctly folded beta-tubulin
93. Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
94. Quasi-native chaperonin-bound intermediates in facilitated protein folding
95. Specificity in chaperonin-mediated protein folding
96. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
97. The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes
98. The essential yeast Tcp1 protein affects actin and microtubules
99. Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
100. Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring
101. + dependent
102. A yeast TCP-1-like protein is required for actin function in vivo
103. The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC
104. Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT
105. TCP1 complex is a molecular chaperone in tubulin biogenesis
106. Cytosolic chaperonin is up-regulated during cell growth. Preferential expression and binding to tubulin at G(1)/S transition through early S phase
107. Upregulation of cytosolic chaperonin CCT subunits during recovery from chemical stress that causes accumulation of unfolded proteins
108. Tubulin dimer formation via the release of alpha- and beta-tubulin monomers from multimolecular complexes
109. Tubulin folding is altered by mutations in a putative GTP binding motif