Two chaperonin systems in bacterial genomes with distinct ecological roles

Trends in Genetics

Volumn 26, Issue 2, 2010, Pages 47-51

  Williams, Tom A ^a   Codoñer, Francisco M ^b   Toft, Christina ^c   Fares, Mario A ^a  

^a TRINITY COLLEGE DUBLIN   (Ireland)

^b HOSPITAL UNIVERSITARI GERMANS TRIAS I PUJOL   (Spain)

^c UPPSALA UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONIN; PROTEIN MTHSP60; UNCLASSIFIED DRUG;

BACTERIAL GENOME; CELL VIABILITY; ECOLOGICAL NICHE; ENVIRONMENTAL CHANGE; EVOLUTIONARY ADAPTATION; GENETIC SCREENING; GENETIC VARIABILITY; HUMAN; MOLECULAR ECOLOGY; NONHUMAN; NUCLEIC ACID BASE SUBSTITUTION; PHYLOGENY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STRUCTURE; SHORT SURVEY;

BACTERIA; CHAPERONINS; ECOSYSTEM; EVOLUTION, MOLECULAR; GENOME, BACTERIAL; HUMANS; MICROBIAL VIABILITY;

ARCHAEA; BACTERIA (MICROORGANISMS);

EID: 75149177236     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tig.2009.11.009     Document Type: Short Survey

References (29)

1. Anfinsen C.B. Principles that govern the folding of protein chains. Science 181 (1973) 223-230
2. Hartl F.U., and Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 16 (2009) 574-581
3. Fayet O., et al. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol 171 (1989) 1379-1385
4. Kerner M., et al. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 122 (2005) 209-220
5. Lund P.A. Multiple chaperonins in bacteria--why so many?. FEMS Microbiol. Rev. 33 (2009) 785-800
6. Gupta R.S. Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells. Mol. Microbiol. 15 (1995) 1-11
7. Lund P., et al. The chaperonins: perspectives from the Archaea. Biochem. Soc. Trans 31 (2003) 681-685
8. Hirtreiter A.M., et al. Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei. Mol. Microbiol. 74 (2009) 1152-1168
9. Kondrashov F.A., and Kondrashov A.S. Role of selection in fixation of gene duplications. J. Theor. Biol. 239 (2006) 141-151
10. Karlin S., et al. Predicted highly expressed genes in archaeal genomes. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 7303-7308
11. Klunker D., et al. Coexistence of group I and group II chaperonins in the Archaeon Methanosarcina mazei. J. Biol. Chem. 278 (2003) 33256-33267
12. Taoka M., et al. Only a small subset of the horizontally transferred chromosomal genes in Escherichia coli are translated into proteins. Mol. Cell. Proteomics 3 (2004) 780-787
13. Toft, C. et al (2009) Genome-wide functional divergence after the symbiosis of proteobacteria with insects unraveled through a novel computational approach. PLoS Comput Biol. 5, e1000344, doi:10.1371/journal.pcbi.1000344.
14. Morrison R.P., et al. Chlamydial disease pathogenesis. The 57-kD chlamydial hypersensitivity antigen is a stress response protein. J. Exp. Med 170 (1989) 1271-1283
15. Hughes A.L. Contrasting evolutionary rates in the duplicate chaperonin genes of Mycobacterium tuberculosis and M. leprae. Mol. Biol. Evol 10 (1993) 1343-1359
16. Fares M., et al. GroEL and the maintenance of bacterial endosymbiosis. Trends Genet. 20 (2004) 413-416
17. Moran N.A., et al. Genomics and evolution of heritable bacterial symbionts. Annu Rev Genet 42 (2008) 165-190
18. Henderson B., et al. Stress wars: the direct role of host and bacterial molecular chaperones in bacterial infection. Infect. Immun. 74 (2006) 3693-3706
19. Wong P., and Houry W.A. Chaperone networks in bacteria: analysis of protein homeostasis in minimal cells. J. Struct. Biol. 146 (2004) 79-89
20. Foster J., et al. The Wolbachia genome of Brugia malayi: endosymbiont evolution within a human pathogenic nematode. PLoS Biol. 3 (2005) e121
21. Nielsen K.L., and Cowan N.J. A single ring is sufficient for productive chaperonin-mediated folding in vivo. Mol. Cell 2 (1998) 93-99
22. Weissman J.S., et al. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell 83 (1995) 577-587
23. Sigler P.B., et al. Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem. 67 (1998) 581-608
24. Levy-Rimler G., et al. The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60. Eur. J. Biochem. 268 (2001) 3465-3472
25. Sun Z., et al. Isolation and characterisation of mutants of GroEL that are fully functional as single rings. J. Mol. Biol. 332 (2003) 715-728
26. Zheng W., et al. Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations. Biophys. J. 93 (2007) 2289-2299
27. Sot B., et al. GroEL stability and function: contribution of the ionic interactions at the inter-ring contact sites. J. Biol. Chem. 278 (2003) 32083-32090
28. Rutherford S., and Lindquist S. Hsp90 as a capacitor for morphological evolution. Nature 396 (1998) 336-342
29. Xu Z., et al. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388 (1997) 741-750