Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells - PubMed (original) (raw)
Review
Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells
R S Gupta. Mol Microbiol. 1995 Jan.
Abstract
The members of the 10 kDa and 60 kDa heat-shock chaperonin proteins (Hsp10 and Hsp60 or Cpn10 and Cpn60), which form an operon in bacteria, are present in all eubacteria and eukaryotic cell organelles such as mitochondria and chloroplasts. In archaebacteria and eukaryotic cell cytosol, no close homologues of Hsp10 or Hsp60 have been identified. However, these species (or cell compartments) contain the Tcp-1 family of proteins (distant homologues of Hsp60). Phylogenetic analysis based on global alignments of Hsp60 and Hsp10 sequences presented here provide some evidence regarding the evolution of mitochondria from a member of the alpha-subdivision of Gram-negative bacteria and chloroplasts from cyanobacterial species, respectively. This interference is strengthened by the presence of sequence signatures that are uniquely shared between Hsp60 homologues from alpha-purple bacteria and mitochondria on one hand, and the chloroplasts and cyanobacterial hsp60s on the other. Within the alpha-purple subdivision, species such as Rickettsia and Ehrlichia, which live intracellularly within eukaryotic cells, are indicated to be the closest relatives of mitochondrial homologues. In the Hsp60 evolutionary tree, rooted using the Tcp-1 homologue, the order of branching of the major groups was as follows: Gram-positive bacteria--cyanobacteria and chloroplasts--chlamydiae and spirochaetes--beta- and gamma-Gram-negative purple bacteria--alpha-purple bacteria--mitochondria. A similar branching order was observed independently in the Hsp10 tree. Multiple Hsp60 homologues, when present in a group of species, were found to be clustered together in the trees, indicating that they evolved by independent gene-duplication events. This review also considers in detail the evolutionary relationship between Hsp60 and Tcp-1 families of proteins based on two different models (viz. archaebacterial and chimeric) for the origin of eukaryotic cell nucleus. Some predictions of the chimeric model are also discussed.
Comment in
- GroEL (Hsp60)-based eubacterial and organellar phylogenies.
Viale A. Viale A. Mol Microbiol. 1995 Sep;17(5):1013. doi: 10.1111/j.1365-2958.1995.mmi_17051013.x. Mol Microbiol. 1995. PMID: 8596429 No abstract available.
Similar articles
- Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.
Kubota H, Hynes G, Carne A, Ashworth A, Willison K. Kubota H, et al. Curr Biol. 1994 Feb 1;4(2):89-99. doi: 10.1016/s0960-9822(94)00024-2. Curr Biol. 1994. PMID: 7953530 - Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus.
Gupta RS, Singh B. Gupta RS, et al. Curr Biol. 1994 Dec 1;4(12):1104-14. doi: 10.1016/s0960-9822(00)00249-9. Curr Biol. 1994. PMID: 7704574 - Origin and evolution of eukaryotic chaperonins: phylogenetic evidence for ancient duplications in CCT genes.
Archibald JM, Logsdon JM Jr, Doolittle WF. Archibald JM, et al. Mol Biol Evol. 2000 Oct;17(10):1456-66. doi: 10.1093/oxfordjournals.molbev.a026246. Mol Biol Evol. 2000. PMID: 11018153 - Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains.
Kim S, Willison KR, Horwich AL. Kim S, et al. Trends Biochem Sci. 1994 Dec;19(12):543-8. doi: 10.1016/0968-0004(94)90058-2. Trends Biochem Sci. 1994. PMID: 7846767 Review. - The phylogeny of proteobacteria: relationships to other eubacterial phyla and eukaryotes.
Gupta RS. Gupta RS. FEMS Microbiol Rev. 2000 Oct;24(4):367-402. doi: 10.1111/j.1574-6976.2000.tb00547.x. FEMS Microbiol Rev. 2000. PMID: 10978543 Review.
Cited by
- Mitochondrial DNA Missense Mutations ChrMT: 8981A > G and ChrMT: 6268C > T Identified in a Caucasian Female with Myalgic Encephalomyelitis/Chronic Fatigue Syndrome (ME/CFS) Triggered by the Epstein-Barr Virus.
Tang-Siegel GG, Maughan DW, Frownfelter MB, Light AR. Tang-Siegel GG, et al. Case Rep Genet. 2024 May 9;2024:6475425. doi: 10.1155/2024/6475425. eCollection 2024. Case Rep Genet. 2024. PMID: 38756740 Free PMC article. - Heat Shock Response and Heat Shock Proteins: Current Understanding and Future Opportunities in Human Diseases.
Singh MK, Shin Y, Ju S, Han S, Choe W, Yoon KS, Kim SS, Kang I. Singh MK, et al. Int J Mol Sci. 2024 Apr 10;25(8):4209. doi: 10.3390/ijms25084209. Int J Mol Sci. 2024. PMID: 38673794 Free PMC article. Review. - A peptide derived from HSP60 reduces proinflammatory cytokines and soluble mediators: a therapeutic approach to inflammation.
Domínguez-Horta MDC, Serrano-Díaz A, Hernández-Cedeño M, Martínez-Donato G, Guillén-Nieto G. Domínguez-Horta MDC, et al. Front Immunol. 2023 Apr 28;14:1162739. doi: 10.3389/fimmu.2023.1162739. eCollection 2023. Front Immunol. 2023. PMID: 37187739 Free PMC article. Review. - Crystal structures of dimeric and heptameric mtHsp60 reveal the mechanism of chaperonin inactivation.
Lai MC, Cheng HY, Lew SH, Chen YA, Yu CH, Lin HY, Lin SM. Lai MC, et al. Life Sci Alliance. 2023 Mar 27;6(6):e202201753. doi: 10.26508/lsa.202201753. Print 2023 Jun. Life Sci Alliance. 2023. PMID: 36973006 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous