Archaeal-like chaperonins in bacteria

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 47, 2010, Pages 20269-20274

  Techtmann, Stephen M ^a,b,c   Robb, Frank T ^a,b  

^a UNIVERSITY OF MARYLAND CENTER FOR ENVIRONMENTAL SCIENCE   (United States)

^b UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

^c UNIFORMED SERVICES UNIVERSITY OF THE HEALTH SCIENCES   (United States)

Author keywords

Evolution; Protein folding; Thermophilic

Indexed keywords

CHAPERONIN; GLUTAMATE DEHYDROGENASE; HEAT SHOCK PROTEIN 70; MALATE DEHYDROGENASE; MESSENGER RNA; PROTEIN DNAK;

ARCHAEBACTERIUM; CARBOXYDOTHERMUS HYDROGENOFORMANS; CONFERENCE PAPER; CONTROLLED STUDY; DESULFOTOMACULUM; ENZYME ACTIVITY; FIRMICUTES; GEOBACILLUS; GRAM POSITIVE BACTERIUM; HELIOBACTERIUM; HORIZONTAL GENE TRANSFER; NONHUMAN; OPERON; PHYLOGENETIC TREE; PHYLOGENY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; SYNTROPHOMONAS WOLFEI;

ARCHAEA; BACTERIA (MICROORGANISMS); CARBOXYDOTHERMUS HYDROGENOFORMANS; EUKARYOTA;

EID: 78650542648     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1004783107     Document Type: Article

References (49)

1. Laksanalamai P, Robb FT (2004) Small heat shock proteins from extremophiles: a review. Extremophiles 8:1-11.
2. Laksanalamai P, Whitehead TA, Robb FT (2004) Minimal protein-folding systems in hyperthermophilic archaea. Nat Rev Microbiol 2:315-324.
3. Large AT, Goldberg MD, Lund PA (2009) Chaperones and protein folding in the archaea. Biochem Soc Trans 37:46-51.
4. Large AT, Lund PA (2009) Archaeal chaperonins. Front Biosci 14:1304-1324.
5. Macario AJ, Conway De Macario E (2001) The molecular chaperone system and other anti-stress mechanisms in archaea. Front Biosci 6:D262-283.
6. Macario AJ, MalzM, Conway de Macario E (2004) Evolution of assisted protein folding: the distribution of the main chaperoning systems within the phylogenetic domain archaea. Front Biosci 9:1318-1332.
7. Hartl FU, Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858.
8. Saibil HR (2008) Chaperone machines in action. Curr Opin Struct Biol 18:35-42.
9. Saibil HR, Ranson NA (2002) The chaperonin folding machine. Trends Biochem Sci 27:627-632.
10. Spiess C, Meyer AS, Reissmann S, Frydman J (2004) Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol 14:598-604.
11. Farr GW, et al. (2000) Multivalent binding of nonnative substrate proteins by the chaperonin GroEL. Cell 100:561-573.
12. Horwich AL, Fenton WA, Chapman E, Farr GW (2007) Two families of chaperonin: physiology and mechanism. Annu Rev Cell Dev Biol 23:115-145.
13. Brinker A, et al. (2001) Dual function of protein confinement in chaperonin-assisted protein folding. Cell 107:223-233.
14. Lin Z, Rye HS (2006) GroEL-mediated protein folding: making the impossible, possible. Crit Rev Biochem Mol Biol 41:211-239.
15. Jewett AI, Shea JE (2009) Reconciling theories of chaperonin accelerated folding with experimental evidence. Cell Mol Life Sci 67:255-276.
16. Agard DA (1993) To fold or not to fold. Science 260:1903-1904.
17. Ellis RJ (2003) Protein folding: importance of the Anfinsen cage. Curr Biol 13:R881-883.
18. Horwich AL, Apetri AC, Fenton WA (2009) The GroEL/GroES cis cavity as a passive anti-aggregation device. FEBS Lett 583:2654-2662.
19. Betancourt MR, Thirumalai D (1999) Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity. J Mol Biol 287:627-644.
20. Sfatos CD, Gutin AM, Abkevich VI, Shakhnovich EI (1996) Simulations of chaperoneassisted folding. Biochemistry 35:334-339.
21. Weissman JS, Kashi Y, Fenton WA, Horwich AL (1994) GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell 78:693-702.
22. Booth CR, et al. (2008) Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT. Nat Struct Mol Biol 15:746-753.
23. Ditzel L, et al. (1998) Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93:125-138.
24. Reissmann S, Parnot C, Booth CR, Chiu W, Frydman J (2007) Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins. Nat Struct Mol Biol 14:432-440.
25. Meyer AS, et al. (2003) Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell 113:369-381.
26. Zhang J, et al. (2010) Mechanism of folding chamber closure in a Group II chaperonin. Nature 463:379-383.
27. Ballard SA, Go M, Segers RP, Adler B (1998) Molecular analysis of the dnaK locus of Leptospira interrogans serovar Copenhageni. Gene 216:21-29.
28. Grandvalet C, Rapoport G, Mazodier P (1998) hrcA, encoding the repressor of the groEL genes in Streptomyces albus G, is associated with a second dnaJ gene. J Bacteriol 180:5129-5134.
29. Schulz A, Schumann W (1996) hrcA, the first gene of the Bacillus subtilis dnaK operon encodes a negative regulator of class I heat shock genes. J Bacteriol 178:1088-1093.
30. Wilson AC, Tan M (2002) Functional analysis of the heat shock regulator HrcA of Chlamydia trachomatis. J Bacteriol 184:6566-6571.
31. Svetlitchnyi V, et al. (1991) Carboxydothermus hydrogenoformans gen. nov., sp. nov., a CO-utilizing thermophilic anaerobic bacterium from hydrothermal environments of Kunashir Island. Syst Appl Microbiol 14:254-260.
32. Wu M, et al. (2005) Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901. PLoS Genet 1:e65.
33. Laksanalamai P, Maeder DL, Robb FT (2001) Regulation and mechanism of action of the small heat shock protein from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol 183:5198-5202.
34. Laksanalamai P, Narayan S, Luo H, Robb FT (2009) Chaperone action of a versatile small heat shock protein from Methanococcoides burtonii, a cold adapted archaeon. Proteins 75:275-281.
35. Luo H, Laksanalamai P, Robb FT (2009) An exceptionallystable Group II chaperonin from the hyperthermophile Pyrococcus furiosus. Arch Biochem Biophys 486:12-18.
36. Figueiredo L, et al. (2004) Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation. J Biol Chem 279:1090-1099.
37. Hongo K, et al. (2006) A novel ATP/ADP hydrolysis activity of hyperthermostable Group II chaperonin in the presence of cobalt or manganese ion. FEBS Lett 580:34-40.
38. Quaite-Randall E, Trent JD, Josephs R, Joachimiak A (1995) Conformational cycle of the archaeosome, a TCP1-like chaperonin from Sulfolobus shibatae. J Biol Chem 270:28818-28823.
39. Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: semiautomated software for highresolution single-particle reconstructions. J Struct Biol 128:82-97.
40. Williams TA, Codoner FM, Toft C, Fares MA (2010) Two chaperonin systems in bacterial genomes with distinct ecological roles. Trends Genet 26:47-51.
41. Macario AJ, Brocchieri L, Shenoy AR, de Macario EC (2006) Evolution of a proteinfolding machine: genomic and evolutionary analyses reveal three lineages of the archaeal hsp70(dnaK) gene. J Mol Evol 63:74-86.
42. Hirtreiter AM, et al. (2009) Differential substrate specificity of Group I and Group II chaperonins in the archaeon Methanosarcina mazei. Mol Microbiol 74:1152-1168.
43. Cuellar J, et al. (2008) The structure of CCT-Hsc70 NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin. Nat Struct Mol Biol 15:858-864.
44. Guindon S, Gascuel O (2003) A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst Biol 52:696-704.
45. Studier FW (2005) Protein production by auto-induction in high density shaking cultures. Protein Expres Purif 41:207-234.
46. Hayer-Hartl M () Chaperonin protocols: methods in molecular biology. (Humana Press, Totowa, NJ), Vol 140, pp 127-132.
47. Schagger H (2001) Blue-native gels to isolate protein complexes from mitochondria. Methods Cell Biol 65:231-244.
48. Schagger H, von Jagow G (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 199:223-231.
49. Pettersen EF, et al. (2004) UCSF Chimera-a visualization system for exploratory research and analysis. J Comput Chem 25:1605-1612.