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This paper was characterized by a bibliometric and systematic review on the database ISI Web of Science, aiming to provide an update of the main points addressed regarding the Temporary Immersion Systems (TIS) for micropropagation of tree species. It was pointed out that the frequency and time of immersion were one of the main parameters studied in the papers and 35% these papers worked with eucalyptus species. The main problem reported in the papers was the hyperhydricity, but it was overcome via procedures such as: a) air injection into the system, b) increasing the immersion intervals and decreasing the immersion time and c) decreasing concentration of cytokinin. Most papers reported that TIS produced plants that were more successful in surviving the ex-vitro acclimation stage than those produced on semi-solid media or continuous immersion systems. Few studies compared different types of temporary immersion bioreactors on micropropagation of plants and within the established criteria, papers with TIS tree species represented only 15% of the total. This system has presented promising results for most of the tree species, and although some gaps have been identified and few are the works with tree species, this process has been taking an increasingly larger space in the propagation of plants.

sporamin ABSTRACT. Zinc in xylem and phloem of the citrus rootstock, rough lemon (Citrus jambhiri (L.)) was associated with a Zn- binding protein, designated citrus vascular Zn-binding protein (CVZBP). The apparent molecular mass of the CVZBP was 19.5 kDa after nondenaturing size exclusion chromatography and 21.8 kDa after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Ion exchange chromatography demonstrated that CVZBP was anionic, requiring 0.43 N NaCl for elution from quaternary aminoethyl Sepharose. Antiserum to the protein cross-reacted more with total protein extracts from leaf midveins than with total protein from the rest of the leaf lamina, further suggesting a vascular location of the Zn-binding protein. Quantitative analysis indicated that ≈2 to 3 mol of Zn were associated with 1 mol of native protein. Binding studies with the partially purified CVZBP demonstrated a capacity to bind several divalent cations: Cd, Ni, Pb, and Zn. Reaction with Ellman's reagent suggested that the protein has significant sulfhydryl group content that may be involved in metal binding. N-terminal sequencing demonstrates identity with papaya latex trypsin inhibitor, sporamin, or other Kunitz soybean proteinase inhibitors. samples were collected from healthy or blight affected trees of Citrus jambhiri grown in a quarantine greenhouse facility on the campus of University of Arizona, Tucson, during 1996. Xylem evacuate was collected by applying 4 mL of 10 mM Tris-Cl, pH 7.4 to one end of a 10 cm root piece >1 cm diameter while a vacuum was pulled at the other end. Bark was removed from the root piece down to the cambium before evacuation. Before purification, xylem evacuate was stored at -80 °C. Phloem tissue was sampled as a bark patch taken 15 to 30 cm above the soil line. Contaminants on the bark surface were removed by scraping away the brown-green outer layer to a 5 × 10 cm rectangle of clean whitish phloem tissue. The patch was scored through the scraped bark to the wood and separated from the tree at the cambial layer. The samples were taken from convex surfaces of healthy and blight-affected trees in active growth. ISOLATION AND PURIFICATION OF CVZBP. To quantitate recov- ery of CVZBP, three independent purifications were performed. Three separate xylem evacuates (Derrick et al., 1990) were lyophilized and adjusted to 1 mL each with deionized water. Xylem evacuate was fractionated by ion exchange chromatogra- phy (IEC) (Taylor et al., 1996) over quaternary aminoethyl Sepharose (QAE) (Pharmacia, Piscataway, N.J.). Total Zn was determined for aliquots of each fraction by determination of A213.9 by atomic absorption spectrometry (model 3100, Perkin-Elmer, Shelton, Conn.) and for 254 nm absorbance (A254) by ultraviolet (UV)- spectrophotometry. Fractions with elevations of A254 and coincident elevated Zn were pooled and the volume reduced in a centrifugal vacuum concentrator (model RC 10. 10; Jouan, Win- chester, Va.). Concentrated Zn-containing eluant from QAE chromatography was separated using a 2.5 × 14 cm gel filtration (GF) column of Bio-Gel P-30 (Bio-Rad, Hercules, Calif.) in 10 mM Tris-Cl buffer, pH 8.0 (4 °C) in 3 mL fractions. Fractions within the peaks of A254 and elevated Zn content were pooled, trichloroacetic acid precipitated (Deutscher, 1990), and further purified by sodium dodecyl sulfate-polyacrylamide gel electro- phoresis (SDS-PAGE) (Laemmli, 1970). For all isolation steps, total protein was determined at A595 with Quantigold (Diversified Biotech, Newton Centre, Mass.) or with the Bradford assay (Bio- Rad), depending upon protein concentration with each stage of purification.

Made available in DSpace on 2013-09-27T14:53:33Z (GMT). No. of bitstreams: 1 WOS000289620100009.pdf: 394055 bytes, checksum: 9a23eb5b1d44e130bf137337fc894796 (MD5) Previous issue date: 2011-04-18 Made available in DSpace on 2013-09-30T18:01:03Z (GMT). No. of bitstreams: 1 WOS000289620100009.pdf: 394055 bytes, checksum: 9a23eb5b1d44e130bf137337fc894796 (MD5) Previous issue date: 2011-04-18 Submitted by Vitor Silverio Rodrigues (vitorsrodrigues@reitoria.unesp.br) on 2014-05-20T13:17:54Z No. of bitstreams: 1 WOS000289620100009.pdf: 394055 bytes, checksum: 9a23eb5b1d44e130bf137337fc894796 (MD5) Made available in DSpace on 2014-05-20T13:17:54Z (GMT). No. of bitstreams: 1 WOS000289620100009.pdf: 394055 bytes, checksum: 9a23eb5b1d44e130bf137337fc894796 (MD5) Previous issue date: 2011-04-18 Fundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG) NIH (National Institutes of Health) - Fogarty Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Background: Corynebacterium pseudotuberculosis, a Gram-positive, facultative intracellular pathogen, is the etiologic agent of the disease known as caseous lymphadenitis (CL). CL mainly affects small ruminants, such as goats and sheep; it also causes infections in humans, though rarely. This species is distributed worldwide, but it has the most serious economic impact in Oceania, Africa and South America. Although C. pseudotuberculosis causes major health and productivity problems for livestock, little is known about the molecular basis of its pathogenicity.Methodology and Findings: We characterized two C. pseudotuberculosis genomes (Cp1002, isolated from goats; and CpC231, isolated from sheep). Analysis of the predicted genomes showed high similarity in genomic architecture, gene content and genetic order. When C. pseudotuberculosis was compared with other Corynebacterium species, it became evident that this pathogenic species has lost numerous genes, resulting in one of the smallest genomes in the genus. Other differences that could be part of the adaptation to pathogenicity include a lower GC content, of about 52%, and a reduced gene repertoire. The C. pseudotuberculosis genome also includes seven putative pathogenicity islands, which contain several classical virulence factors, including genes for fimbrial subunits, adhesion factors, iron uptake and secreted toxins. Additionally, all of the virulence factors in the islands have characteristics that indicate horizontal transfer.Conclusions: These particular genome characteristics of C. pseudotuberculosis, as well as its acquired virulence factors in pathogenicity islands, provide evidence of its lifestyle and of the pathogenicity pathways used by this pathogen in the infection process. All genomes cited in this study are available in the NCBI Genbank database (http://www.ncbi.nlm.nih.gov/genbank/) under accession numbers CP001809 and CP001829. Fundação Oswaldo Cruz, Res Ctr Rene Rachou, Ctr Excellence Bioinformat, Natl Inst Sci & Technol, Belo Horizonte, MG, Brazil Universidade Federal de Minas Gerais (UFMG), Dept Gen Biol, Belo Horizonte, MG, Brazil Fed Univ Para, Dept Genet, BR-66059 Belem, Para, Brazil Univ Fed Sao Joao del Rei, Hlth Sci Ctr, Divinopilis, MG, Brazil Univ Estadual Ceara, Dept Vet Med, Fortaleza, Ceara, Brazil Univ Bielefeld, Dept Genet, CeBiTech, Bielefeld, Nordrhein Westf, Germany Max Planck Inst Informat, Dept Comp Sci, Saarbrucken, Saarlan, Germany Univ Fed Ouro Preto, Dept Pharmaceut Sci, Ouro Preto, MG, Brazil Univ Fed Ouro Preto, Dept Phis, Ouro Preto, MG, Brazil Univ Fed Triangulo Mineiro, Dept Biol Sci, Uberaba, MG, Brazil Universidade Federal de Uberlândia (UFU), Dept Biochem & Genet, BR-38400 Uberlandia, MG, Brazil Brazilian Agr Res Corp Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA), Sete Lagoas, MG, Brazil Universidade Federal de Minas Gerais (UFMG), Dept Biochem & Immunol, Belo Horizonte, MG, Brazil Universidade Federal de Minas Gerais (UFMG), Dept Parasitol, Belo Horizonte, MG, Brazil Univ Fed Ouro Preto, Dept Pharm, Ouro Preto, MG, Brazil State Univ São Paulo, Dept Technol, Jaboticabal, SP, Brazil Universidade Federal de Lavras (UFLA), Dept Chem, Lavras, MG, Brazil Brazilian Agr Res Corp Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA), Campinas, SP, Brazil Universidade Federal de Viçosa (UFV), Dept Plant Pathol, Vicosa, MG, Brazil Universidade Federal da Bahia (UFBA), Dept Biointeract Sci, Salvador, BA, Brazil CSIRO Livestock Ind, Clayton, Vic, Australia State Univ São Paulo, Dept Technol, Jaboticabal, SP, Brazil FAPEMIG: CBB-1181/0 FAPEMIG: REDE-186/08 NIH - Fogarty: TW007012