Ying Xu

Free University of Brussels, Brussels, BRU, Belgium

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Publications (18)68.92 Total impact

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    ABSTRACT: Contrary to a widespread opinion, horizontal gene transfer (HGT) between distantly related microorganisms (such as Bacteria and Archaea) has not been demonstrated to occur on a large scale. Except for transfer of mobile elements between closely related organisms, most alleged HGT events reflect phylogenetic discrepancies that can be explained by a variety of artefacts or by the differential loss of paralogous gene copies either originally present in the Last Universal Common Ancestor (LUCA) to the three Domains (a sophisticated, genetically redundant and promiscuous community of protoeukaryotes), or created by duplications having occurred at later times. Besides, (i) there is no experimental evidence for the facile acquisition of foreign DNA between distant taxa and (ii) important biological constraints operate on the phenotypic success of genetic exchange at several levels, including protein-protein interactions involved in metabolic channelling; stable integration and expression of foreign DNA is, therefore, expected to require strong selection. Explaining phylogenetic discrepancies by artefacts or loss of paralogs does not eliminate difficulties in retracing species genealogy but maintains the picture of a universal tree of life, HGT between distant organisms being reduced to a trickle. We illustrate our thesis by the phylogenetic analysis of carbamoyltransferases, a family of paralogous proteins. Among higher eukaryotes HGT appears of limited scope except in asexual organisms. We suggest that meiotic sexuality (a hallmark of eukaryotes) emerged in the genetically redundant and protoeukaryotic LUCA as a molecular identity check providing a defence mechanism against the deleterious effects of HGT.
    Journal of Molecular Evolution 09/2009; 69(5):470-80. · 2.15 Impact Factor
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    ABSTRACT: A complete tree with roots, trunk and crown remains an appropriate model to represent all steps of life's development, from the emergence of a unique genetic code up to the last universal common ancestor and its further radiation. Catalytic closure of a mixture of prebiotic polymers is a heuristic alternative to the RNA world. Conjectures about emergence of life in an infinite multiverse should not confuse probability with possibility.
    Research in Microbiology 07/2009; 160(7):522-8. · 2.89 Impact Factor
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    ABSTRACT: Since the reclassification of all life forms in three Domains (Archaea, Bacteria, Eukarya), the identity of their alleged forerunner (Last Universal Common Ancestor or LUCA) has been the subject of extensive controversies: progenote or already complex organism, prokaryote or protoeukaryote, thermophile or mesophile, product of a protracted progression from simple replicators to complex cells or born in the cradle of "catalytically closed" entities? We present a critical survey of the topic and suggest a scenario. LUCA does not appear to have been a simple, primitive, hyperthermophilic prokaryote but rather a complex community of protoeukaryotes with a RNA genome, adapted to a broad range of moderate temperatures, genetically redundant, morphologically and metabolically diverse. LUCA's genetic redundancy predicts loss of paralogous gene copies in divergent lineages to be a significant source of phylogenetic anomalies, i.e. instances where a protein tree departs from the SSU-rRNA genealogy; consequently, horizontal gene transfer may not have the rampant character assumed by many. Examining membrane lipids suggest LUCA had sn1,2 ester fatty acid lipids from which Archaea emerged from the outset as thermophilic by "thermoreduction," with a new type of membrane, composed of sn2,3 ether isoprenoid lipids; this occurred without major enzymatic reconversion. Bacteria emerged by reductive evolution from LUCA and some lineages further acquired extreme thermophily by convergent evolution. This scenario is compatible with the hypothesis that the RNA to DNA transition resulted from different viral invasions as proposed by Forterre. Beyond the controversy opposing "replication first" to metabolism first", the predictive arguments of theories on "catalytic closure" or "compositional heredity" heavily weigh in favour of LUCA's ancestors having emerged as complex, self-replicating entities from which a genetic code arose under natural selection. Life was born complex and the LUCA displayed that heritage. It had the "body "of a mesophilic eukaryote well before maturing by endosymbiosis into an organism adapted to an atmosphere rich in oxygen. Abundant indications suggest reductive evolution of this complex and heterogeneous entity towards the "prokaryotic" Domains Archaea and Bacteria. The word "prokaryote" should be abandoned because epistemologically unsound. This article was reviewed by Anthony Poole, Patrick Forterre, and Nicolas Galtier.
    Biology Direct 08/2008; 3:29. · 2.72 Impact Factor
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    ABSTRACT: Major aspects of the pathway of de novo arginine biosynthesis via acetylated intermediates in microorganisms must be revised in light of recent enzymatic and genomic investigations. The enzyme N-acetylglutamate synthase (NAGS), which used to be considered responsible for the first committed step of the pathway, is present in a limited number of bacterial phyla only and is absent from Archaea. In many Bacteria, shorter proteins related to the Gcn5-related N-acetyltransferase family appear to acetylate l-glutamate; some are clearly similar to the C-terminal, acetyl-coenzyme A (CoA) binding domain of classical NAGS, while others are more distantly related. Short NAGSs can be single gene products, as in Mycobacterium spp. and Thermus spp., or fused to the enzyme catalyzing the last step of the pathway (argininosuccinase), as in members of the Alteromonas-Vibrio group. How these proteins bind glutamate remains to be determined. In some Bacteria, a bifunctional ornithine acetyltransferase (i.e., using both acetylornithine and acetyl-CoA as donors of the acetyl group) accounts for glutamate acetylation. In many Archaea, the enzyme responsible for glutamate acetylation remains elusive, but possible connections with a novel lysine biosynthetic pathway arose recently from genomic investigations. In some Proteobacteria (notably Xanthomonadaceae) and Bacteroidetes, the carbamoylation step of the pathway appears to involve N-acetylornithine or N-succinylornithine rather than ornithine. The product N-acetylcitrulline is deacetylated by an enzyme that is also involved in the provision of ornithine from acetylornithine; this is an important metabolic function, as ornithine itself can become essential as a source of other metabolites. This review insists on the biochemical and evolutionary implications of these findings.
    Microbiology and Molecular Biology Reviews 04/2007; 71(1):36-47. · 16.42 Impact Factor
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    ABSTRACT: Avast number of prokaryotic and eukaryotic microorganisms can synthesize arginine de novo from glutamate. The first committed step of this pathway is acetylation of l-glutamate at the N-position. Asurprising variety of proteins were found to catalyze this reaction in prokaryotes: (i) the classical, two-domain N-acetylglutamate synthase (NAGS) originally found in γ-Proteobacteria, (ii) shorter NAGS of the GNAT acetyltransferase family, either independent or fused with the ArgH protein (argininosuccinase), (iii) bifunctional ornithine acetyltransferases (OAT), i.e. able to acetylate glutamate with both acetyl-CoA and acetylornithine. In many organisms, including most Archaea, the enzyme acetylating glutamate remains elusive; possible connections with lysine biosynthesis may be envisaged. In fungi, NAGS appears only distantly related to its prokaryotic analog and requires association with acetylglutamate kinase (NAGK) to be functional. In most organisms, the acetyl group of acetylornithine is either split by an acetylornithinase (AO) or recycled on glutamate by OAT; in both cases, one of the products is ornithine which is carbamoylated into citrulline. In some Proteobacteria however, acetylornithine is carbamoylated into acetylcitrulline. These discoveries on arginine precursor acetylation have important metabolic and evolutionary implications. Among Bacteria, regulation of arginine biosynthetic genes was analyzed intensively in Escherichia coli, Salmonella typhimurium, Bacilli and more recently in Pseudomonas sp. Archaea remain to be investigated. Among Eukarya, the yeast Saccharomyces cerevisiae was studied in great detail. The comparison of the mechanisms found to operate in these very different organisms is interesting from several points of view: (i) the occurrence of repressor-operator interactions on both sides of the prokaryote/eukaryote divide and the first evidence for aJacob-Monod regulatory mechanism in eukaryotes, (ii) the coordination of carbamoyl phosphate synthesis with the two pathways that depend on this metabolite (arginine and pyrimidine biosyntheses), (iii) the coordination of arginine biosynthesis with arginine catabolism and the first indication ever that arepressor (the E.coli ArgR protein) may also function as agene activator, (iv) the extensive conservation of the ArgR/AhrC transcription control system throughout the bacterial domain with the notable exception of Pseudomonas sp. and related Bacteria, (v) the functional and possible evolutionary relationship between proteins involved in arginine metabolic control systems and proteins controlling DNA replication and partition. Arginine is an important “nutraceutical”. Knowledge of the regulatory mechanisms controlling the function or synthesis of arginine biosynthetic enzymes in prokaryotes has been used to engineer arginine-overproducing strains amenable to industrial exploitation.
    11/2006: pages 219-257;
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    ABSTRACT: The N-acetylation of L-glutamate is regarded as a universal metabolic strategy to commit glutamate towards arginine biosynthesis. Until recently, this reaction was thought to be catalyzed by either of two enzymes: (i) the classical N-acetylglutamate synthase (NAGS, gene argA) first characterized in Escherichia coli and Pseudomonas aeruginosa several decades ago and also present in vertebrates, or (ii) the bifunctional version of ornithine acetyltransferase (OAT, gene argJ) present in Bacteria, Archaea and many Eukaryotes. This paper focuses on a new and surprising aspect of glutamate acetylation. We recently showed that in Moritella abyssi and M. profunda, two marine gamma proteobacteria, the gene for the last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of NAGS and is able to complement an argA mutant of E. coli. Very recently, other authors identified in Mycobacterium tuberculosis an independent gene corresponding to this short C-terminal domain and coding for a new type of NAGS. We have investigated the two prokaryotic Domains for patterns of gene-enzyme relationships in the first committed step of arginine biosynthesis. The argH-A fusion, designated argH(A), and discovered in Moritella was found to be present in (and confined to) marine gamma proteobacteria of the Alteromonas- and Vibrio-like group. Most of them have a classical NAGS with the exception of Idiomarina loihiensis and Pseudoalteromonas haloplanktis which nevertheless can grow in the absence of arginine and therefore appear to rely on the arg(A) sequence for arginine biosynthesis. Screening prokaryotic genomes for virtual argH-X 'fusions' where X stands for a homologue of arg(A), we retrieved a large number of Bacteria and several Archaea, all of them devoid of a classical NAGS. In the case of Thermus thermophilus and Deinococcus radiodurans, the arg(A)-like sequence clusters with argH in an operon-like fashion. In this group of sequences, we find the short novel NAGS of the type identified in M. tuberculosis. Among these organisms, at least Thermus, Mycobacterium and Streptomyces species appear to rely on this short NAGS version for arginine biosynthesis. The gene-enzyme relationship for the first committed step of arginine biosynthesis should now be considered in a new perspective. In addition to bifunctional OAT, nature appears to implement at least three alternatives for the acetylation of glutamate. It is possible to propose evolutionary relationships between them starting from the same ancestral N-acetyltransferase domain. In M. tuberculosis and many other bacteria, this domain evolved as an independent enzyme, whereas it fused either with a carbamate kinase fold to give the classical NAGS (as in E. coli) or with argH as in marine gamma proteobacteria. Moreover, there is an urgent need to clarify the current nomenclature since the same gene name argA has been used to designate structurally different entities. Clarifying the confusion would help to prevent erroneous genomic annotation.
    BMC Genomics 02/2006; 7:4. · 4.40 Impact Factor
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    Microbiology 01/2005; 150(Pt 12):3908-11. · 2.85 Impact Factor
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    ABSTRACT: Annotating genomes remains an hazardous task. Mistakes or gaps in such a complex process may occur when relevant knowledge is ignored, whether lost, forgotten or overlooked. This paper exemplifies an approach which could help to ressucitate such meaningful data.
    09/2004;
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    ABSTRACT: Annotating genomes remains an hazardous task. Mistakes or gaps in such a complex process may occur when relevant knowledge is ignored, whether lost, forgotten or overlooked. This paper exemplifies an approach which could help to resuscitate such meaningful data. We show that a set of closely related sequences which have been annotated as ornithine carbamoyltransferases are actually putrescine carbamoyltransferases. This demonstration is based on the following points : (i) use of enzymatic data which had been overlooked, (ii) rediscovery of a short NH2-terminal sequence allowing to reannotate a wrongly annotated ornithine carbamoyltransferase as a putrescine carbamoyltransferase, (iii) identification of conserved motifs allowing to distinguish unambiguously between the two kinds of carbamoyltransferases, and (iv) comparative study of the gene context of these different sequences. We explain why this specific case of misannotation had not yet been described and draw attention to the fact that analogous instances must be rather frequent. We urge to be especially cautious when high sequence similarity is coupled with an apparent lack of biochemical information. Moreover, from the point of view of genome annotation, proteins which have been studied experimentally but are not correlated with sequence data in current databases qualify as "orphans", just as unassigned genomic open reading frames do. The strategy we used in this paper to bridge such gaps in knowledge could work whenever it is possible to collect a body of facts about experimental data, homology, unnoticed sequence data, and accurate informations about gene context.
    BMC Genomics 09/2004; 5(1):52. · 4.40 Impact Factor
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    ABSTRACT: Many evolutionary scenarios describing the history of proteins are based solely on phylogenetic studies. We have designed a new approach that allows ascertainment of such questionable scenarios by taking into account quaternary structures: we used aspartate carbamoyltransferase (ATCase) as a case study. Prokaryotic ATCases correspond to different classes of quaternary structures according to the mode of association of the catalytic PyrB subunit with other polypeptides, either the PyrI regulatory subunit (class B) or a dihydroorotase (class A), which may be active (PyrC, subclass A1) or inactive (PyrC', subclass A2). Class C is uniquely made up of trimers of PyrB. The PyrB phylogenetic tree is not congruent with the tree of life, but it became coherent when we recognized the existence of two families of ATCases, ATC I and ATC II. Remarkably, a very strong correlation was found between the pattern of PyrB phylogenetic clustering and the different classes of quaternary structures of ATCases. All class B ATCases form a clade in family ATC II, which also contains all eukaryotic sequences. In contrast, family ATC I is made up of classes A and C. These results suggest unexpected common ancestry for prokaryotic B and eukaryotic ATCases on the one hand, and for A and C on the other. Thus, the emergence of specific quaternary structures appears to have been a more recent event than the separation into the ATC I and ATC II families. We propose that different evolutionary constraints, depending on the identity of the partners interacting in the different kinds of holoenzymes, operated in a concerted way on the ancestral pyrB genes and the respective associated genes pyrI or pyrC, so as to maintain appropriate inter-polypeptides interactions at the level of quaternary structure. The process of coevolution of genes encoding proteins interacting in various holoenzymes has been assessed by calculating the correlation coefficient between their respective phylogenetic trees. Our approach integrating data obtained from the separate fields of structural biology and molecular evolution could be useful in other cases where pure statistical data need to receive independent confirmation.
    Molecular Biology and Evolution 03/2004; 21(2):364-73. · 14.31 Impact Factor
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    ABSTRACT: Adapting metabolic enzymes of microorganisms to low temperature environments may require a difficult compromise between velocity and affinity. We have investigated catalytic efficiency in a key metabolic enzyme (dihydrofolate reductase) of Moritella profunda sp. nov., a strictly psychrophilic bacterium with a maximal growth rate at 2 degrees C or less. The enzyme is monomeric (Mr=18,291), 55% identical to its Escherichia coli counterpart, and displays Tm and denaturation enthalpy changes much lower than E. coli and Thermotoga maritima homologues. Its stability curve indicates a maximum stability above the temperature range of the organism, and predicts cold denaturation below 0 degrees C. At mesophilic temperatures the apparent Km value for dihydrofolate is 50- to 80-fold higher than for E. coli, Lactobacillus casei, and T. maritima dihydrofolate reductases, whereas the apparent Km value for NADPH, though higher, remains in the same order of magnitude. At 5 degrees C these values are not significantly modified. The enzyme is also much less sensitive than its E. coli counterpart to the inhibitors methotrexate and trimethoprim. The catalytic efficiency (kcat/Km) with respect to dihydrofolate is thus much lower than in the other three bacteria. The higher affinity for NADPH could have been maintained by selection since NADPH assists the release of the product tetrahydrofolate. Dihydrofolate reductase adaptation to low temperature thus appears to have entailed a pronounced trade-off between affinity and catalytic velocity. The kinetic features of this psychrophilic protein suggest that enzyme adaptation to low temperature may be constrained by natural limits to optimization of catalytic efficiency.
    Journal of Bacteriology 10/2003; 185(18):5519-26. · 3.19 Impact Factor
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    ABSTRACT: The enzyme ornithine carbamoyltransferase (OTCase) of Moritella abyssi (OTCase(Mab)), a new, strictly psychrophilic and piezophilic bacterial species, was purified. OTCase(Mab) displays maximal activity at rather low temperatures (23 to 25 degrees C) compared to other cold-active enzymes and is much less thermoresistant than its homologues from Escherichia coli or thermophilic procaryotes. In vitro the enzyme is in equilibrium between a trimeric state and a dodecameric, more stable state. The melting point and denaturation enthalpy changes for the two forms are considerably lower than the corresponding values for the dodecameric Pyrococcus furiosus OTCase and for a thermolabile trimeric mutant thereof. OTCase(Mab) displays higher K(m) values for ornithine and carbamoyl phosphate than mesophilic and thermophilic OTCases and is only weakly inhibited by the bisubstrate analogue delta-N-phosphonoacetyl-L-ornithine (PALO). OTCase(Mab) differs from other, nonpsychrophilic OTCases by substitutions in the most conserved motifs, which probably contribute to the comparatively high K(m) values and the lower sensitivity to PALO. The K(m) for ornithine, however, is substantially lower at low temperatures. A survey of the catalytic efficiencies (k(cat)/K(m)) of OTCases adapted to different temperatures showed that OTCase(Mab) activity remains suboptimal at low temperature despite the 4.5-fold decrease in the K(m) value for ornithine observed when the temperature is brought from 20 to 5 degrees C. OTCase(Mab) adaptation to cold indicates a trade-off between affinity and catalytic velocity, suggesting that optimization of key metabolic enzymes at low temperatures may be constrained by natural limits.
    Journal of Bacteriology 05/2003; 185(7):2161-8. · 3.19 Impact Factor
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    ABSTRACT: A psychropiezophilic bacterium, strain 2825T (=LMG 21260T =JCM 11437T), isolated from deep Atlantic sediments at a depth of 2770 m and a temperature of 2 degrees C, was found by polyphasic analysis to represent a novel species of the genus Psychromonas, Psychromonas profunda sp. nov. It is a strict psychrophile and a moderate piezophile, whose degree of piezophily is increased markedly when the temperature is raised to 10 degrees C. The piezophily of P. profunda is intermediate between that of the type species, Psychromonas antarctica, which is not piezophilic, and that of Psychromonas kaikoae, which is an obligate piezophile.
    International journal of systematic and evolutionary microbiology 04/2003; 53(Pt 2):527-32. · 2.11 Impact Factor
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    ABSTRACT: Strains 2674T (=LMG 21259T =JCM 11435T) and 2693T (=LMG 21258T =JCM 11436T) were isolated from Atlantic sediments at a temperature of 2 degrees C and a depth of 2815 m off the West African coast. Polyphasic evidence indicates that the two strains belong to the genus Moritella and represent distinct species, for which the names Moritella profunda sp. nov. (for strain 2674T) and Moritella abyssi sp. nov. (for strain 2693T) are proposed. The moderate piezophily of the two organisms is intermediate between that of the type species, Moritella marina, which is not piezophilic, and Moritella yayanosii, an obligate piezophile. Both are strict psychrophiles with slightly different cardinal temperatures: at 0.1 MPa, maximal growth rates are observed at 2 degrees C (M. profunda) and 4 degrees C (M. abyssi) with maximum temperatures of 12 degrees C (M. profunda) or 14 degrees C (M. abyssi). The optimal pressure is lower than that at the site of isolation, and raising the temperature to 10 degrees C makes the organisms more piezophilic.
    International journal of systematic and evolutionary microbiology 04/2003; 53(Pt 2):533-8. · 2.11 Impact Factor
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    ABSTRACT: We report the cloning of the arginine repressor gene from the psychropiezophilic Gram-negative bacterium Moritella profunda, the purification of its product (ArgR(Mp)), the identification of the operator in the bipolar argECBFGH(A) operon, in vivo repressibility studies, and an in vitro analysis of the repressor-operator interaction, including binding to mutant and heterologous arginine operators. The ArgR(Mp) subunit shows about 70% amino acid sequence identity with Escherichia coli ArgR (ArgR(Ec)). Binding of purified hexameric ArgR(Mp) to the control region of the divergent operon proved to be arginine-dependent, sequence-specific, and significantly more sensitive to heat than complex formation with ArgR(Ec). ArgR(Mp) binds E.coli arginine operators very efficiently, but hardly recognizes the operator from Bacillus stearothermophilus or Thermotoga maritima. ArgR(Mp) binds to a single site overlapping the -35 element of argC(P), but not argE(P). Therefore, the arrangement of promoter and operator sites in the bipolar argECBFGH(A) operon of M.profunda is very different from the organization of control elements in the bipolar argECBH operon of E.coli, where both promoters overlap the common operator and are equally repressible. We demonstrate that M.profunda argC(P) is about 44-fold repressible, whereas argE(P) is fully constitutive. A high-resolution contact map of the ArgR(Mp)-operator interaction was established by enzymatic and chemical footprinting, missing contact and base-specific premodification binding interference studies. The results indicate that the argC operator consists of two ARG box-like sequences (18bp imperfect palindromes) separated by 3bp. ArgR(Mp) binds to one face of the DNA helix and establishes contacts with two major groove segments and the intervening minor groove of each ARG box, whereas the minor groove segment facing the repressor at the center of the operator remains largely uncontacted. This pattern is reminiscent of complex formation with the repressors of E.coli and B.stearothermophilus, and suggests that each ARG box is contacted by two ArgR subunits belonging to opposite trimers. Moreover, the premodification interference patterns and mutant studies clearly indicate that the inner, center proximal halves of each ARG box in the M.profunda argC operator are more important for complex formation and repression than the outermost halves. A close inspection of sequence conservation and of single base-pair O(c)-type mutations indicate that the same conclusion can be generalized to E.coli operators.
    Journal of Molecular Biology 03/2003; 326(2):353-69. · 3.91 Impact Factor
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    ABSTRACT: Strains 2674 T (=LMG 21259 T =JCM 11435 T) and 2693 T (=LMG 21258 T =JCM 11436 T) were isolated from Atlantic sediments at a temperature of 2 uC and a depth of 2815 m off the West African coast. Polyphasic evidence indicates that the two strains belong to the genus Moritella and represent distinct species, for which the names Moritella profunda sp. nov. (for strain 2674 T) and Moritella abyssi sp. nov. (for strain 2693 T) are proposed. The moderate piezophily of the two organisms is intermediate between that of the type species, Moritella marina, which is not piezophilic, and Moritella yayanosii, an obligate piezophile. Both are strict psychrophiles with slightly different cardinal temperatures: at 0?1 MPa, maximal growth rates are observed at 2 uC (M. profunda) and 4 uC (M. abyssi) with maximum temperatures of 12 uC (M. profunda) or 14 uC (M. abyssi). The optimal pressure is lower than that at the site of isolation, and raising the temperature to 10 uC makes the organisms more piezophilic. Below 2000 m depth, the temperature of the ocean usually does not rise above 2–3 uC (Yayanos, 1995). The deep sea is thus a habitat favourable to psychrophilic micro-organisms (highest growth temperature below 20 uC; Morita, 1975). From the analysis of sediments collected from the tropical Atlantic off West Africa between 1500 and 4500 m depth, Rüger & Tan (1992) concluded that psychrophiles with maximum growth temperatures below 12 uC were predo-minant among cultivable bacteria. Since the hydrostatic pressure increases by 0?1 MPa every 10 m down the water column, deep-sea resident organisms are expected to display various levels of piezophily or piezotolerance (Yayanos, 1995). Since the isolation of the first pure culture of a true piezophilic bacterium, collected at a depth of 5700 m (Yayanos et al., 1979), several psychropiezophilic species have been described (Kato et al., 1995, 1996; Nogi et al., 1998). Obligate piezophiles, i.e. unable to grow at atmos-pheric pressure, have been isolated from the deepest Pacific trenches (Yayanos, 1995; Kato et al., 2000; Bartlett, 2000). Most cultivable psychropiezophiles have been found to belong to a few genera of the c-Proteobacteria, Colwellia, Moritella, Photobacterium and Shewanella (DeLong et al., 1997), and more recently, Psychromonas, a genus that also includes non-piezophilic organisms (Nogi et al., 2002, Xu et al., 2003).
    International journal of systematic and evolutionary microbiology 01/2003; 53(2). · 2.11 Impact Factor
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    ABSTRACT: In this paper we critically review the 'classical' model for the emergence of the three domains (Archaea, Bacteria, Eucarya), which presents hyperthermophilic procaryotes as the ancestors of all life on this planet. We come to the conclusion that our last common ancestor is likely to have been rather a non-hyperthermophilic protoeucaryote endowed with sn-1,2 glycerol ester lipids (as in modern Bacteria and Eucarya), from which Archaea emerged by streamlining under pressure for adapting to heat, a process which involved an important molecular innovation: the advent of sn-2,3 glycerol ether lipids. The nature of the primeval bacterial lines of descent is less clear; it would appear, nevertheless, that the first extreme- and hyperthermophilic Bacteria emerged by converging mechanisms; lateral gene transfer from Archaea may have played a role in this adaptation.
    Comparative Biochemistry and Physiology - Part A Molecular & Integrative Physiology 12/2002; 133(3):677-88. · 2.17 Impact Factor

Publication Stats

332 Citations
68.92 Total Impact Points

Institutions

  • 2002–2009
    • Free University of Brussels
      • Laboratorium voor Erfelijkheidsleer en Microbiologie
      Brussels, BRU, Belgium
  • 2004–2007
    • Université Paris-Sud 11
      • Institut de Génétique et Microbiologie (IGMORS)
      Paris, Ile-de-France, France
  • 2006
    • Stony Brook University
      • Marine Sciences Research Center
      Stony Brook, NY, United States