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Environmental Adaptation (environmental + adaptation)
Selected AbstractsCrystal structures and enzymatic properties of three formyltransferases from archaea: Environmental adaptation and evolutionary relationshipPROTEIN SCIENCE, Issue 9 2002Björn Mamat Abstract Formyltransferase catalyzes the reversible formation of formylmethanofuran from N5 -formyltetrahydromethanopterin and methanofuran, a reaction involved in the C1 metabolism of methanogenic and sulfate-reducing archaea. The crystal structure of the homotetrameric enzyme from Methanopyrus kandleri (growth temperature optimum 98°C) has recently been solved at 1.65 Å resolution. We report here the crystal structures of the formyltransferase from Methanosarcina barkeri (growth temperature optimum 37°C) and from Archaeoglobus fulgidus (growth temperature optimum 83°C) at 1.9 Å and 2.0 Å resolution, respectively. Comparison of the structures of the three enzymes revealed very similar folds. The most striking difference found was the negative surface charge, which was ,32 for the M. kandleri enzyme, only ,8 for the M. barkeri enzyme, and ,11 for the A. fulgidus enzyme. The hydrophobic surface fraction was 50% for the M. kandleri enzyme, 56% for the M. barkeri enzyme, and 57% for the A. fulgidus enzyme. These differences most likely reflect the adaptation of the enzyme to different cytoplasmic concentrations of potassium cyclic 2,3-diphosphoglycerate, which are very high in M. kandleri (>1 M) and relatively low in M. barkeri and A. fulgidus. Formyltransferase is in a monomer/dimer/tetramer equilibrium that is dependent on the salt concentration. Only the dimers and tetramers are active, and only the tetramers are thermostable. The enzyme from M. kandleri is a tetramer, which is active and thermostable only at high concentrations of potassium phosphate (>1 M) or potassium cyclic 2,3-diphosphoglycerate. Conversely, the enzyme from M. barkeri and A. fulgidus already showed these properties, activity and stability, at much lower concentrations of these strong salting-out salts. [source] Is natural selection a plausible explanation for the distribution of Idh- 1 alleles in the cricket Allonemobius socius?ECOLOGICAL ENTOMOLOGY, Issue 1 2006Diana L. Huestis Abstract., 1.,Allozyme alleles in natural populations have been proposed as either neutral markers of genetic diversity or the product of natural selection on enzyme function, as amino acid substitutions that change electrophoretic mobility may also alter enzyme performance. To address these possibilities, researchers have used both correlative analyses and empirical studies. 2.,Here, geographically structured variation of the enzyme isocitrate dehydrogenase (Idh- 1) in the striped ground cricket Allonemobius socius Scudder (Orthoptera: Gryllidae) is examined. The distributions of Idh- 1 alleles appear to be related to environmental gradients, as allele frequencies showed significant relationships with mean annual temperature and precipitation. Specifically, the slowest mobility allele was more frequent at colder temperatures, while the converse occurred for the fastest mobility allele. 3.,An exploratory experiment was performed to examine fitness effects of possessing different Idh- 1 alleles at two temperatures to test the hypothesis that the geographic structure of this locus may reflect environmental adaptation. Results showed that a significant interaction between temperature and Idh- 1 genotype affected the number of eggs laid, with success of homozygous individuals matching environmental expectations. 4.,The above results show that (1) variation in the frequency of Idh- 1 alleles is significantly related to environmental gradients in the eastern U.S.A. and (2) alternative alleles of Idh- 1 appear to influence the egg-laying ability of individuals differently depending on environmental temperature. Together, these results suggest that natural selection is a plausible mechanism underlying the distribution of Idh- 1 alleles in this species, although more detailed studies are needed. [source] Metagenomic and stable isotopic analyses of modern freshwater microbialites in Cuatro Ciénegas, MexicoENVIRONMENTAL MICROBIOLOGY, Issue 1 2009Mya Breitbart Summary Ancient biologically mediated sedimentary carbonate deposits, including stromatolites and other microbialites, provide insight into environmental conditions on early Earth. The primary limitation to interpreting these records is our lack of understanding regarding microbial processes and the preservation of geochemical signatures in contemporary microbialite systems. Using a combination of metagenomic sequencing and isotopic analyses, this study describes the identity, metabolic potential and chemical processes of microbial communities from living microbialites from Cuatro Ciénegas, Mexico. Metagenomic sequencing revealed a diverse, redox-dependent microbial community associated with the microbialites. The microbialite community is distinct from other marine and freshwater microbial communities, and demonstrates extensive environmental adaptation. The microbialite metagenomes contain a large number of genes involved in the production of exopolymeric substances and the formation of biofilms, creating a complex, spatially structured environment. In addition to the spatial complexity of the biofilm, microbial activity is tightly controlled by sensory and regulatory systems, which allow for coordination of autotrophic and heterotrophic processes. Isotopic measurements of the intracrystalline organic matter demonstrate the importance of heterotrophic respiration of photoautotrophic biomass in the precipitation of calcium carbonate. The genomic and stable isotopic data presented here significantly enhance our evolving knowledge of contemporary biomineralization processes, and are directly applicable to studies of ancient microbialites. [source] Temperature- and pH-dependent accumulation of heat-shock proteins in the acidophilic green alga Chlamydomonas acidophilaFEMS MICROBIOLOGY ECOLOGY, Issue 3 2006Antje Gerloff-Elias Abstract Chlamydomonas acidophila, a unicellular green alga, is a dominant phytoplankton species in acidic water bodies, facing severe environmental conditions such as low pH and high heavy metal concentrations. We examined the pH-, and temperature-dependent accumulation of heat-shock proteins in this alga to determine whether heat-shock proteins play a role in adaptation to their environment. Our results show increased heat-shock proteins accumulation at suboptimal pHs, which were not connected with any change in intracellular pH. In comparison to the mesophilic Chlamydomonas reinhardtii, the acidophilic species exhibited significantly higher accumulations of heat-shock proteins under control conditions, indicating an environmental adaptation of increased basal levels of heat-shock proteins. The results suggest that heat-shock proteins might play a role in the adaptation of C. acidophila, and possibly other acidophilic algae, to their extreme environment. [source] Extreme changes to gene expression associated with homoploid hybrid speciationMOLECULAR ECOLOGY, Issue 5 2009MATTHEW J. HEGARTY Abstract Hybridization is an important cause of abrupt speciation. Hybrid speciation without a change in ploidy (homoploid hybrid speciation) is well-established in plants but has also been reported in animals and fungi. A notable example of recent homoploid hybrid speciation is Senecio squalidus (Oxford ragwort), which originated in the UK in the 18th Century following introduction of hybrid material from a hybrid zone between S. chrysanthemifolius and S. aethnensis on Mount Etna, Sicily. To investigate genetic divergence between these taxa, we used complementary DNA microarrays to compare patterns of floral gene expression. These analyses revealed major differences in gene expression between the parent species and wild and resynthesized S. squalidus. Comparisons of gene expression between S. aethnensis, S. chrysanthemifolius and natural S. squalidus identified genes potentially involved in local environmental adaptation. The analysis also revealed non-additive patterns of gene expression in the hybrid relative to its progenitors. These expression changes were more dramatic and widespread in resynthesized hybrids than in natural S. squalidus, suggesting that a unique expression pattern may have been fixed during the allopatric divergence of British S. squalidus. We speculate that hybridization-induced gene-expression change may provide an immediate source of novel phenotypic variation upon which selection can act to facilitate homoploid hybrid speciation in plants. [source] Threonine phosphorylation prevents promoter DNA binding of the Group B Streptococcus response regulator CovRMOLECULAR MICROBIOLOGY, Issue 6 2009Wan-Jung Lin Summary All living organisms communicate with the external environment for their survival and existence. In prokaryotes, communication is achieved by two-component systems (TCS) comprising histidine kinases and response regulators. In eukaryotes, signalling is accomplished by serine/threonine and tyrosine kinases. Although TCS and serine/threonine kinases coexist in prokaryotes, direct cross-talk between these families was first described in Group B Streptococcus (GBS). A serine/threonine kinase (Stk1) and a TCS (CovR/CovS) co-regulate toxin expression in GBS. Typically, promoter binding of regulators like CovR is controlled by phosphorylation of the conserved active site aspartate (D53). In this study, we show that Stk1 phosphorylates CovR at threonine 65. The functional consequence of threonine phosphorylation of CovR in GBS was evaluated using phosphomimetic and silencing substitutions. GBS encoding the phosphomimetic T65E allele are deficient for CovR regulation unlike strains encoding the non-phosphorylated T65A allele. Further, compared with wild-type or T65A CovR, the T65E CovR is unable to bind promoter DNA and is decreased for phosphorylation at D53, similar to Stk1-phosphorylated CovR. Collectively, we provide evidence for a novel mechanism of response regulator control that enables GBS (and possibly other prokaryotes) to fine-tune gene expression for environmental adaptation. [source] Welcome to new editors , development, eco-devo and environmental adaptationNEW PHYTOLOGIST, Issue 1 2003Jonathan Ingram Editorial & Development Manager No abstract is available for this article. [source] The first structure of a cold-adapted superoxide dismutase (SOD): biochemical and structural characterization of iron SOD from Aliivibrio salmonicidaACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 2 2009Hege Lynum Pedersen Superoxide dismutases (SODs) are metalloenzymes that catalyse the dismutation of the superoxide radical anion into O2 and H2O2 in a two-step reaction. The crystal structure of the iron superoxide dismutase from the cold-adapted and fish-pathogenic bacterium Aliivibrio salmonicida (asFeSOD) has been determined and refined to 1.7,Å resolution. The protein has been characterized and compared with the closely related homologous iron superoxide dismutase from the mesophilic Escherichia coli (ecFeSOD) in an attempt to rationalize its environmental adaptation. ecFeSOD shares 75% identity with asFeSOD. Compared with the mesophilic FeSOD, the psychrophilic FeSOD has distinct temperature differences in residual activity and thermostability that do not seem to be related to structural differences such as intramolecular or intermolecular ion bonds, hydrogen bonds or cavity sizes. However, an increased net negative charge on the surface of asFeSOD may explain its lower thermostability compared with ecFeSOD. Activity measurements and differential scanning calorimetry measurements revealed that the psychrophilic asFeSOD had a thermostability that was significantly higher than the optimal growth temperature of the host organism. [source] Managing the environmental adaptation process in supplier,customer relationshipsBUSINESS STRATEGY AND THE ENVIRONMENT, Issue 4 2001Louise Canning This paper details the results and managerial implications from four case studies, which examine how the environmental adaptation process (EAP) is managed within business-to-business relationships. The research uses models of supplier,customer interaction and inter-organization cooperation in order to explore inter-firm relationships and the process of adaptation. The research findings show that either party might pursue adaptations and also establishes features of the process itself as well as identifying factors that can facilitate or hinder the introduction of environmental changes. Arriving at a satisfactory outcome to the adaptation process can be determined by individual company and relationship characteristics, as well as the behaviour and experience of those managers involved in the process. Guidelines for the management of the process of environmental adaptation are proposed. Copyright © 2001 John Wiley & Sons, Ltd and ERP Environment [source] | |||||||||||||