A dnaK homolog in the archaebacterium Methanosarcina mazei S6

Macario, Alberto J. L.; Dugan, Charles B.; Macario, Everly Conway de

doi:10.1016/0378-1119(91)90498-z

Cited by 62 publications

(36 citation statements)

References 19 publications

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“…After submission of this manuscript, the sequence of HSP70 from a methanogenic archaebacterium, M. mazei, was also reported (30). These reports provide definitive identification and characterization of HSP70 homologs in species belonging to the archaebacterium domain, and they establish the ubiquity of both HSP70 as well as the heat shock response in all forms of life.…”

Section: Discussionmentioning

confidence: 88%

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Cloning of the HSP70 gene from Halobacterium marismortui: relatedness of archaebacterial HSP70 to its eubacterial homologs and a model for the evolution of the HSP70 gene

1992

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Heat shock induces the synthesis of a set of proteins in Halobacterium marismortui whose molecular sizes correspond to the known major heat shock proteins. By using the polymerase chain reaction and degenerate oligonucleotide primers for conserved regions of the 70-kDa heat shock protein (HSP70) family, we All bacterial and eukaryotic species studied to date exhibit increased synthesis of a set of proteins referred to as stress or heat shock proteins (HSPs) in response to a sudden increase in physiological temperature as well as exposure to other stressors (e.g., hypoxia, amino acid analogs, ethanol, etc.) (27,34). One of the proteins whose synthesis is greatly induced under these conditions has an apparent molecular mass of 70 kDa (HSP70; bacterial homolog known as the DnaK protein). Although the synthesis of HSP70 is greatly enhanced by various physiological stressors, it also constitutes a major protein under normal growth conditions and has been shown to be essential for cellular growth. Gene cloning and sequencing studies on HSP70 show that the primary structure of this protein has been highly conserved during evolution in species ranging from bacteria to plants to humans (27,34).In recent years, although HSP70 homologs have been cloned from numerous bacterial and eukaryotic species (1,2,4,6,12,14,18,21,32,37,38,41,42)

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Section: Discussionmentioning

confidence: 88%

“…4) showed extensive similarity throughout its length, confirming its identity as an HSP70 homolog. Recently (after original submission of this paper), the sequence of HSP70 from the archaebacterium Methanosarcina mazei was also reported (30), and it is included in the comparison shown in Fig. 4.…”

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confidence: 99%

Cloning of the HSP70 gene from Halobacterium marismortui: relatedness of archaebacterial HSP70 to its eubacterial homologs and a model for the evolution of the HSP70 gene

1992

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“…Org., organism; perm., permease; RNAP, RNA polymerase; k-ase, kinase; RNaseP, RNaseP RNA. The sequence sources were the genome Web sites (see Web Site References in Supplemental Material, Table S3, online) and Conway de Macario et al 1994, Gupta and Singh 1993, Macario et al 1991, 1993, 1995, Hoffman-Bang et al 1999, Deppenmeir et al 2002, Galagan et al 2002, Smith et al 1997 , and A.S. Kazi and C.K.K. Nair, Bombay, India (accession number AF069527; gi, 10798841; H. mediterranei).…”

Section: Dnak Locus I Types and Dnak Phylogenymentioning

confidence: 99%

Evolution of a Protein-Folding Machine: Genomic and Evolutionary Analyses Reveal Three Lineages of the Archaeal hsp70(dnaK) Gene

et al. 2006

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Abstract. The stress chaperone protein Hsp70 (DnaK) (abbreviated DnaK) and its co-chaperones Hsp40(DnaJ) (or DnaJ) and GrpE are universal in bacteria and eukaryotes but occur only in some archaea clustered in the order 5¢-grpE-dnaK-dnaJ-3¢ in a locus termed Locus I. Three structural varieties of Locus I, termed Types I, II, and III, were identified, respectively, in Methanosarcinales, in Thermoplasmatales and Methanothermobacter thermoautotrophicus, and in Halobacteriales. These Locus I types corresponded to three groups identified by phylogenetic trees of archaeal DnaK proteins including the same archaeal subdivisions. These archaeal DnaK groups were not significantly interrelated, clustering instead with DnaKs from three bacterial lineages, Methanosarcinales with Firmicutes, Thermoplasmatales and M. thermoautotrophicus with Thermotoga, and Halobacteriales with Actinobacteria, suggesting that the three archaeal types of Locus I were acquired by independent events of lateral gene transfer. These associations, however, lacked strong bootstrap support and were sensitive to dataset choice and treereconstruction method. Structural features of dnaK loci in bacteria revealed that Methanosarcinales and Firmicutes shared a similar structure, also common to most other bacterial groups. Structural differences were observed instead in Thermotoga compared to Thermoplasmatales and M. thermoautotrophicus, and in Actinobacteria compared to Halobacteriales. It was also found that the association between the DnaK sequences from Halobacteriales and Actinobacteria likely reflects common biases in their amino acid compositions. Although the loci structural features and the DnaK trees suggested the possibility of lateral gene transfer between Firmicutes and Methanosarcinales, the similarity between the archaeal and the ancestral bacterial loci favors the more parsimonious hypothesis that all archaeal sequences originated from a unique prokaryotic ancestor.

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“…the HSP70 (DnaK), HSP90 and HSP40 (DnaJ) families, in M. jannaschii is particularly striking as these proteins are universally conserved in other genomes and appeared to be indispensable for any cell . These molecular chaperones are encoded by at least some archaea (Macario et al, 1991;1993;Gupta and Singh, 1994), including the dnaK gene in the methanogen Methanosarcina mazei (Macario et al, 1991). We performed a reverse search of the M. jannaschii protein and nucleotide sequences with the sequences of known molecular chaperones, in order to detect putative distant homologues.…”

Section: ¹7mentioning

confidence: 99%

Comparison of archaeal and bacterial genomes: computer analysis of protein sequences predicts novel functions and suggests a chimeric origin for the archaea

Galperin

et al. 1997

Molecular Microbiology

285

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SummaryProtein sequences encoded in three complete bacterial genomes, those of Haemophilus influenzae, Mycoplasma genitalium and Synechocystis sp., and the first available archaeal genome sequence, that of Methanococcus jannaschii, were analysed using the BLAST 2 algorithm and methods for amino acid motif detection. Between 75% and 90% of the predicted proteins encoded in each of the bacterial genomes and 73% of the M. jannaschii proteins showed significant sequence similarity to proteins from other species. The fraction of bacterial and archaeal proteins containing regions conserved over long phylogenetic distances is nearly the same and close to 70%. Functions of 70-85% of the bacterial proteins and about 70% of the archaeal proteins were predicted with varying precision. This contrasts with the previous report that more than half of the archaeal proteins have no homologues and shows that, with more sensitive methods and detailed analysis of conserved motifs, archaeal genomes become as amenable to meaningful interpretation by computer as bacterial genomes. The analysis of conserved motifs resulted in the prediction of a number of previously undetected functions of bacterial and archaeal proteins and in the identification of novel protein families. In spite of the generally high conservation of protein sequences, orthologues of 25% or less of the M. jannaschii genes were detected in each individual completely sequenced genome, supporting the uniqueness of archaea as a distinct domain of life. About 53% of the M. jannaschii proteins belong to families of paralogues, a fraction similar to that in bacteria with larger genomes, such as Synechocystis sp. and Escherichia coli, but higher than that in H. influenzae, which has approximately the same number of genes as M. jannaschii. Certain groups of proteins, e.g. molecular chaperones and DNA repair enzymes, thought to be ubiquitous and represented in the minimal gene set derived by bacterial genome comparison, are missing in M. jannaschii, indicating massive non-orthologous displacement of genes responsible for essential functions. An unexpectedly large fraction of the M. jannaschii gene products, 44%, shows significantly higher similarity to bacterial than to eukaryotic proteins, compared with 13% that have eukaryotic proteins as their closest homologues (the rest of the proteins show approximately the same level of similarity to bacterial and eukaryotic homologues or have no homologues). Proteins involved in translation, transcription, replication and protein secretion are most closely related to eukaryotic proteins, whereas metabolic enzymes, metabolite uptake systems, enzymes for cell wall biosynthesis and many uncharacterized proteins appear to be 'bacterial'. A similar prevalence of proteins of apparent bacterial origin was observed among the currently available sequences from the distantly related archaeal genus, Sulfolobus. It is likely that the evolution of archaea included at least one major merger between ancestral cells from the bacterial lineage and the ...

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A dnaK homolog in the archaebacterium Methanosarcina mazei S6

Cited by 62 publications

References 19 publications

Cloning of the HSP70 gene from Halobacterium marismortui: relatedness of archaebacterial HSP70 to its eubacterial homologs and a model for the evolution of the HSP70 gene

Cloning of the HSP70 gene from Halobacterium marismortui: relatedness of archaebacterial HSP70 to its eubacterial homologs and a model for the evolution of the HSP70 gene

Evolution of a Protein-Folding Machine: Genomic and Evolutionary Analyses Reveal Three Lineages of the Archaeal hsp70(dnaK) Gene

Comparison of archaeal and bacterial genomes: computer analysis of protein sequences predicts novel functions and suggests a chimeric origin for the archaea

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