Species 2000 & ITIS Catalogue of Life, 2013 Annual Checklist

This release of the Catalogue of Life contains contributions from 132 databases with information on 1,352,112 species, 114,069 infraspecific taxa and also includes 928,147 synonyms and 408,689 common names covering the following groups: Viruses • Viruses and Subviral agents from ICTV_MSL UPDATED! Bacteria and Archaea from BIOS Chromista • Chromistan fungi from Species Fungorum Protozoa • Major groups from ITIS Regional, • Ciliates from CilCat, • Polycystines from WoRMS Polycystina UPDATED!, • Protozoan fungi from Species Fungorum and Trichomycetes database • Slime moulds from Nomen.eumycetozoa.com Fungi • Various taxa in whole or in part from CABI Bioservices databases (Species Fungorum, Phyllachorales, Rhytismatales, Saccharomycetes and Zygomycetes databases) and from three other databases covering Xylariaceae, Glomeromycota, Trichomycetes, Dothideomycetes • Lichens from LIAS UPDATED! Plantae (Plants) • Mosses from MOST • Liverworts and hornworts from ELPT • Conifers from Conifer Database • Cycads and 6 flowering plant families from IOPI-GPC, and 99 families from WCSP • Plus individual flowering plants families from AnnonBase, Brassicaceae, ChenoBase, Droseraceae Database, EbenaBase, GCC UPDATED!, ILDIS UPDATED!, LecyPages, LHD, MELnet UPDATED!, RJB Geranium, Solanaceae Source, Umbellifers. Animalia (Animals) • Marine groups from URMO, ITIS Global, Hexacorals, ETI WBD (Euphausiacea), WoRMS: WoRMS Asteroidea UPDATED!, WoRMS Bochusacea UPDATED!, WoRMS Brachiopoda UPDATED!, WoRMS Brachypoda UPDATED!, WoRMS Brachyura UPDATED!, WoRMS Bryozoa UPDATED!, WoRMS Cestoda NEW!, WoRMS Chaetognatha UPDATED!, WoRMS Cumacea UPDATED!, WoRMS Echinoidea UPDATED!, WoRMS Gastrotricha NEW!, WoRMS Gnathostomulida NEW!, WoRMS Holothuroidea UPDATED!, WoRMS Hydrozoa UPDATED!, WoRMS Isopoda UPDATED!, WoRMS Leptostraca UPDATED!, WoRMS Monogenea NEW!, WoRMS Mystacocarida UPDATED!, WoRMS Myxozoa NEW!, WoRMS Nemertea UPDATED!, WoRMS Oligochaeta UPDATED!, WoRMS Ophiuroidea UPDATED!, WoRMS Phoronida UPDATED!, WoRMS Placozoa NEW!, WoRMS Polychaeta UPDATED!, WoRMS Polycystina UPDATED!, WoRMS Porifera UPDATED!, WoRMS Priapulida NEW!, WoRMS Proseriata and Kalyptorhynchia UPDATED!, WoRMS Remipedia UPDATED!, WoRMS Scaphopoda UPDATED!, WoRMS Tanaidacea UPDATED!, WoRMS Tantulocarida UPDATED!, WoRMS Thermosbaenacea UPDATED!, WoRMS Trematoda NEW!, WoRMS Xenoturbellida UPDATED! • Rotifers, mayflies, freshwater hairworms, planarians from FADA databases: FADA Rotifera UPDATED!, FADA Ephemeroptera NEW!, FADA Nematomorpha NEW! & FADA Turbellaria NEW! • Entoprocts, water bears from ITIS Global • Spiders, scorpions, ticks & mites from SpidCat via ITIS UPDATED!, SalticidDB , ITIS Global, TicksBase, SpmWeb BdelloideaBase UPDATED! & Mites GSDs: OlogamasidBase, PhytoseiidBase, RhodacaridBase & TenuipalpidBase • Diplopods, centipedes, pauropods and symphylans from SysMyr UPDATED! & ChiloBase • Dragonflies and damselflies from Odonata database • Stoneflies from PlecopteraSF UPDATED! • Cockroaches from BlattodeaSF UPDATED! • Praying mantids from MantodeaSF UPDATED! • Stick and leaf insects from PhasmidaSF UPDATED! • Grasshoppers, locusts, katydids and crickets from OrthopteraSF UPDATED! • Webspinners from EmbiopteraSF UPDATED! • Bark & parasitic lices from PsocodeaSF NEW! • Some groups of true bugs from ScaleNet, FLOW, COOL, Psyllist, AphidSF UPDATED! , MBB, 3i Cicadellinae, 3i Typhlocybinae, MOWD & CoreoideaSF NEW!• Twisted-wing parasites from Strepsiptera Database UPDATED! • Lacewings, antlions, owlflies, fishflies, dobsonflies & snakeflies from LDL Neuropterida • Some beetle groups from the Scarabs UPDATED!, TITAN, WTaxa & ITIS Global • Fleas from Parhost • Flies, mosquitoes, bots, midges and gnats from Systema Dipterorum, CCW & CIPA • Butterflies and moths from LepIndex UPDATED!, GloBIS (GART) UPDATED!, Tineidae NHM, World Gracillariidae • Bees & wasps from ITIS Bees, Taxapad Ichneumonoidea, UCD, ZOBODAT Vespoidea & HymIS Rhopalosomatidae NEW!• Molluscs from WoRMS Mollusca NEW!, FADA Bivalvia NEW!, MolluscaFW NEW! & AFD (Pulmonata) • Fishes from FishBase UPDATED! • Reptiles from TIGR Reptiles • Amphibians, birds and mammals from ITIS Global PLUS additional species of many groups from ITIS Regional, NZIB and CoL China NEW!

How the double spherules of infectious bronchitis virus impact our understanding of RNA virus replicative organelles

Powered by advances in electron tomography, recent studies have extended our understanding of how viruses construct "replication factories" inside infected cells. Their function, however, remains an area of speculation with important implications for human health. It is clear from these studies that whatever their purpose, organelle structure is dynamic (M. Ulasli, M. H. Verheije, C. A. de Haan, and F. Reggiori, Cell. Microbiol. 12:844-861, 2010) and intricate (K. Knoops, M. Kikkert, S. H. Worm, J. C. Zevenhoven-Dobbe, Y. van der Meer, et al., PLOS Biol. 6:e226, 2008). But by concentrating on medically important viruses, these studies have failed to take advantage of the genetic variation inherent in a family of viruses that is as diverse as the archaea, bacteria, and eukaryotes combined (C. Lauber, J. J. Goeman, M. del Carmen Parquet, P. T. Nga, E. J. Snijder, et al., PLOS Pathog. 9:e1003500, 2013). In this climate, Maier et al. (H. J. Maier, P. C. Hawes, E. M. Cottam, J. Mantell, P. Verkade, et al., mBio 4:e00801-13, 2013) explored the replicative structures formed by an avian coronavirus that appears to have diverged at an early point in coronavirus evolution and shed light on controversial aspects of viral biology.

Replacement of the arginine biosynthesis operon in Xanthomonadales by ateral gene transfer

The role of lateral gene transfer (LGT) in prokaryotes has been shown to rapidly change the genome content, providing new gene tools for environmental adaptation. Features related to pathogenesis and resistance to strong selective conditions have been widely shown to be products of gene transfer between bacteria. The genomes of the gamma-proteobacteria from the genus Xanthomonas, composed mainly of phytopathogens, have potential genomic islands that may represent imprints of such evolutionary processes. In this work, the evolution of genes involved in the pathway responsible for arginine biosynthesis in Xanthomonadales was investigated, and several lines of evidence point to the foreign origin of the arg genes clustered within a potential operon. Their presence inside a potential genomic island, bordered by a tRNA gene, the unusual ranking of sequence similarity, and the atypical phylogenies indicate that the metabolic pathway for arginine biosynthesis was acquired through LGT in the Xanthomonadales group. Moreover, although homologues were also found in Bacteroidetes (Flavobacteria group), for many of the genes analyzed close homologues are detected in different life domains (Eukarya and Archaea), indicating that the source of these arg genes may have been outside the Bacteria clade. The possibility of replacement of a complete primary metabolic pathway by LGT events supports the selfish operon hypothesis and may occur only under very special environmental conditions. Such rare events reveal part of the history of these interesting mosaic Xanthomonadales genomes, disclosing the importance of gene transfer modifying primary metabolism pathways and extending the scenario for bacterial genome evolution.

Oxidative stress protection of Trypanosomes requires selenophosphate synthase

Selenoproteins are characterized by the incorporation of at least one amino acid selenocysteine (Sec-U) encoded by in-frame UGA stop codons. These proteins, as well as the components of the Sec synthesis pathway, are present in members of the bacteria, archaea and eukaryote domains. Although not a ubiquitous pathway in all organisms, it was also identified in several protozoa, including the Kinetoplastida. Genetic evidence has indicated that the pathway is non-essential to the survival of Trypanosoma growing in non-stressed conditions. By analyzing the effects of RNA interference of the Trypanosoma brucei selenophosphate synthetase SPS2, we found a requirement under sub-optimal growth conditions. The present work shows that SPS2 is involved in oxidative stress protection of the parasite and its absence severely hampers the parasite survival in the presence of an oxidizing environment that results in an apoptotic-like phenotype and cell death. (C) 2011 Elsevier B.V. All rights reserved.

Insights into the mechanism of progressive RNA degradation by the archaeal exosome

Initially identified in yeast, the exosome has emerged as a central component of the RNA maturation and degradation machinery both in Archaea and eukaryotes. Here we describe a series of high-resolution structures of the RNase PH ring from the Pyrococcus abyssi exosome, one of them containing three 10-mer RNA strands within the exosome catalytic chamber, and report additional nucleotide interactions involving positions N5 and N7. Residues from all three Rrp41-Rrp42 heterodimers interact with a single RNA molecule, providing evidence for the functional relevance of exosome ring-like assembly in RNA processivity. Furthermore, an ADP-bound structure showed a rearrangement of nucleotide interactions at site N1, suggesting a rationale for the elimination of nucleoside diphosphate after catalysis. In combination with RNA degradation assays performed with mutants of key amino acid residues, the structural data presented here provide support for a model of exosome-mediated RNA degradation that integrates the events involving catalytic cleavage, product elimination, and RNA translocation. Finally, comparisons between the archaeal and human exosome structures provide a possible explanation for the eukaryotic exosome inability to catalyze phosphate-dependent RNA degradation.

Structure, Dynamics, and RNA Interaction Analysis of the Human SBDS Protein

Shwachman-Bodian-Diamond syndrome is an autosomal recessive genetic syndrome with pleiotropic phenotypes, including pancreatic deficiencies, bone marrow dysfunctions with increased risk of myelodysplasia or leukemia, and skeletal abnormalities. This syndrome has been associated with mutations in the SBDS gene, which encodes a conserved protein showing orthologs in Archaea and eukaryotes. The Shwachman-Bodian-Diamond syndrome pleiotropic phenotypes may be an indication of different cell type requirements for a fully functional SBDS protein. RNA-binding activity has been predicted for archaeal and yeast SBDS orthologs, with the latter also being implicated in ribosome biogenesis. However, full-length SBDS orthologs function in a species-specific manner, indicating that the knowledge obtained from model systems may be of limited use in understanding major unresolved issues regarding SBDS function, namely, the effect of mutations in human SBDS on its biochemical function and the specificity of RNA interaction. We determined the solution structure and backbone dynamics of the human SBDS protein and describe its RNA binding site using NMR spectroscopy. Similarly to the crystal structures of Archaea, the overall structure of human SBDS comprises three well-folded domains. However, significant conformational exchange was observed in NMR dynamics experiments for the flexible linker between the N-terminal domain and the central domain, and these experiments also reflect the relative motions of the domains. RNA titrations monitored by heteronuclear correlation experiments and chemical shift mapping analysis identified a classic RNA binding site at the N-terminal FYSH (fungal, Yhr087wp, Shwachman) domain that concentrates most of the mutations described for the human SBDS. (C) 2010 Elsevier Ltd. All rights reserved.

Sdo1p, the yeast orthologue of Shwachman-Bodian-Diamond syndrome protein, binds RNA and interacts with nuclear rRNA-processing factors

The Shwachman-Bodian-Diamond syndrome protein (SBDS) is a member of a highly conserved protein family of not well understood function, with putative orthologues found in different organisms ranging from Archaea, yeast and plants to vertebrate animals. The yeast orthologue of SBDS, Sdo1p, has been previously identified in association with the 60S ribosomal subunit and is proposed to participate in ribosomal recycling. Here we show that Sdo1p interacts with nucleolar rRNA processing factors and ribosomal proteins, indicating that it might bind the pre-60S complex and remain associated with it during processing and transport to the cytoplasm. Corroborating the protein interaction data, Sdo1p localizes to the nucleus and cytoplasm and co-immunoprecipitates precursors of 60S and 40S subunits, as well as the mature rRNAs. Sdo1p binds RNA directly, suggesting that it may associate with the ribosomal subunits also through RNA interaction. Copyright (C) 2009 John Wiley & Sons, Ltd.

Características das células procarióticas e eucarióticas

Apresenta a definição e descrição de células procarióticas e eucarióticas com o auxílio de figuras ilustrativas. Inicialmente detalha-se a célula procariótica e suas estruturas: parede celular, membrana celular, citoplasma, ribossomos, estruturas externas, região nuclear, plasmídeo, endósporo, morfologia celular e divisão celular. A seguir apresenta-se a célula eucariótica e suas estruturas: organelas, retículo endoplasmático, ribossomos, lisossomos, núcleo celular, mitocôndrias, cloroplasto e complexo de Golgi. No decorrer da descrição enfatizam-se as semelhanças e diferenças entre as células procarióticas e eucarióticas, apresenta-se a Teoria endossimbiótica e a árvore filogenética (Bacteria, Archaea e Eucarya).

Análise metagenômica da microbiota de ambientes aquáticos do estado do Rio Grande do Norte - Brasil

The screening for genes in metagenomic libraries from soil creates opportunities to explore the enormous genetic and metabolic diversity of microorganisms. Rivers are ecosystems with high biological diversity, but few were examined using the metagenomic approach. With this objective, a metagenomic library was constructed from DNA soil samples collected at three different points along the Jundiaí-river (Rio Grande do Norte-Brazil). The points sampled are from open area, rough terrain and with the direct incidence of sunlight. This library was analyzed functionally and based in sequence. For functional analysis Luria-Bertani solid medium (LB) with NaCl concentration varied from 0.17M to 0.85M was used for functional analysis. Positives clones resistant to hypersaline medium were obtained. The recombinant DNAs were extracted and transformed into Escherichia coli strain DH10B and survival curves were obtained for quantification of abiotic stress resistance. The sequences of clones were obtained and submitted to the BLASTX tool. Some clones were found to hypothetical proteins of microorganisms from both Archaea and Bacteria division. One of the clones showed a complete ORF with high similarity to glucose-6-phosphate isomerase which participates in the synthesis of glycerol pathway and serves as a compatible solute to balance the osmotic pressure inside and outside of cells. Subsequently, in order to identify genes encoding osmolytes or enzymes related halotolerance, environmental DNA samples from the river soil, from the water column of the estuary and ocean were collected and pyrosequenced. Sequences of osmolytes and enzymes of different microorganisms were obtained from the UniProt and used as RefSeqs for homology identification (TBLASTN) in metagenomic databases. The sequences were submitted to HMMER for the functional domains identification. Some enzymes were identified: alpha-trehalose-phosphate synthase, L-ectoina synthase (EctC), transaminase L-2 ,4-diaminobutyric acid (EctB), L-2 ,4-diaminobutyric acetyltransferase (EctA), L-threonine 3 dehydrogenase (sorbitol pathway), glycerol-3-phosphate dehydrogenase, inositol 3-phosphate dehydrogenase, chaperones, L-proline, glycine betaine binding ABC transporter, myo-inositol-1-phosphate synthase protein of proline simportadora / PutP sodium-and trehalose-6-phosphate phosphatase These proteins are commonly related to saline environments, however the identification of them in river environment is justified by the high salt concentration in the soil during prolonged dry seasons this river. Regarding the richness of the microbiota the river substrate has an abundance of halobacteria similar to the sea and more than the estuary. These data confirm the existence of a specialized response against salt stress by microorganisms in the environment of the Jundiaí river

Molecular characterization of bacterial populations of different soils

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Synthetic lethality between eIF5A and Ypt1 reveals a connection between translation and the secretory pathway in yeast

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Functional significance of eIF5A and its hypusine modification in eukaryotes

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Production of active recombinant eIF5A: reconstitution in E.coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes

Eukaryotic translation initiation factor 5A (eIF5A) is the only cellular protein that contains the polyamine-modified lysine, hypusine [N(epsilon)-(4-amino-2-hydroxybutyl)lysine]. Hypusine occurs only in eukaryotes and certain archaea, but not in eubacteria. It is formed post-translationally by two consecutive enzymatic reactions catalyzed by deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). Hypusine modification is essential for the activity of eIF5A and for eukaryotic cell proliferation. eIF5A binds to the ribosome and stimulates translation in a hypusine-dependent manner, but its mode of action in translation is not well understood. Since quantities of highly pure hypusine-modified eIF5A is desired for structural studies as well as for determination of its binding sites on the ribosome, we have used a polycistronic vector, pST39, to express eIF5A alone, or to co-express human eIF5A-1 with DHS or with both DHS and DOHH in Escherichia coli cells, to engineer recombinant proteins, unmodified eIF5A, deoxyhypusine- or hypusine-modified eIF5A. We have accomplished production of three different forms of recombinant eIF5A in high quantity and purity. The recombinant hypusine-modified eIF5A was as active in methionyl-puromycin synthesis as the native, eIF5A (hypusine form) purified from mammalian tissue. The recombinant eIF5A proteins will be useful tools in future structure/function and the mechanism studies in translation.

eIF5A interacts functionally with eEF2

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Evolução do reparo por excisão de nucleotídeo

The phylogeny is one of the main activities of the modern taxonomists and a way to reconstruct the history of the life through comparative analysis of these sequences stored in their genomes aimed find any justification for the origin or evolution of them. Among the sequences with a high level of conservation are the genes of repair because it is important for the conservation and maintenance of genetic stability. Hence, variations in repair genes, as the genes of the nucleotide excision repair (NER), may indicate a possible gene transfer between species. This study aimed to examine the evolutionary history of the components of the NER. For this, sequences of UVRA, UVRB, UVRC and XPB were obtained from GenBank by Blast-p, considering 10-15 as cutoff to create a database. Phylogenetic studies were done using algorithms in PAUP programs, BAYES and PHYLIP package. Phylogenetic trees were build with protein sequences and with sequences of 16S ribosomal RNA for comparative analysis by the methods of parsimony, likelihood and Bayesian. The XPB tree shows that archaeal´s XPB helicases are similar to eukaryotic helicases. According to this data, we infer that the eukaryote nucleotide excision repair system had appeared in Archaea. At UVRA, UVRB and UVRC trees was found a monophyletic group formed by three species of epsilonproteobacterias class, three species of mollicutes class and archaeabacterias of Methanobacteria and Methanococci classes. This information is supported by a tree obtained with the proteins, UVRA, UVRB and UVRC concatenated. Thus, although there are arguments in the literature defending the horizontal transfer of the system uvrABC of bacteria to archaeabacterias, the analysis made in this study suggests that occurred a vertical transfer, from archaeabacteria, of both the NER genes: uvrABC and XPs. According the parsimony, this is the best way because of the occurrence of monophyletic groups, the time of divergence of classes and number of archaeabacterias species with uvrABC system