DOCSLIB.ORG

University of Groningen Genome Sequencing and Analysis of The

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
University of Groningen Genome Sequencing and Analysis of The University of Groningen Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88 Pel, Herman J.; de Winde, Johannes H.; Archer, David B.; Dyer, Paul S.; Hofmann, Gerald; Schaap, Peter J.; Turner, Geoffrey; Albang, Richard; Albermann, Kaj; Andersen, Mikael R. Published in: Nature Biotechnology DOI: 10.1038/nbt1282 IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 2007 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Pel, H. J., de Winde, J. H., Archer, D. B., Dyer, P. S., Hofmann, G., Schaap, P. J., Turner, G., Albang, R., Albermann, K., Andersen, M. R., Bendtsen, J. D., Benen, J. A. E., van den Berg, M., Breestraat, S., Caddick, M. X., Contreras, R., Cornell, M., Coutinho, P. M., Danchin, E. G. J., ... de Vries, R. P. (2007). Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88. Nature Biotechnology, 25(2), 221-231. https://doi.org/10.1038/nbt1282 Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license. More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne- amendment. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 30-09-2021 Supplementary Table 7 A. niger CBS 513.88 gene expression Gene name day3 day3 day3_Detection day5 day5_ day5_Detection Descriptions Signal Detection p-value Signal Detection p-value An01e00180 3.9 A 0.216384 15.7 P 0.04219 trnaKctt An01e00230 42.2 P 0.02493 51.1 P 0.001437 trnaDgtc An01e01100 10 A 0.07897 24.1 P 0.001851 5S ribosomal RNA An01e01100 58.8 P 0.001109 61.1 P 0.001437 trnaPagg An01e01570 14.2 A 0.406973 6.8 A 0.437665 trnaItat An01e01910 4.4 A 0.759912 3.8 A 0.5 trnaAtgc An01e02450 56.6 P 0.017085 65.3 P 0.017085 trnaDgtc An01e02580 38 A 0.085938 61.5 P 0.009766 trnaMcat An01e02710 44.7 P 0.011455 35.7 P 0.02987 transposon Vader - Aspergillus niger An01e03830 14.9 A 0.173261 16.7 A 0.240088 trnaEttc An01e03890 8.8 A 0.376842 17 A 0.265142 trnaEttc An01e04290 4.8 A 0.173261 1.3 A 0.406973 trnaMcat An01e04780 127.9 P 0.001437 84.9 P 0.001109 trnaVcac An01e05430 184.6 P 0.00302 98.6 P 0.001851 trnaVaac An01e05550 3.9 A 0.70854 0.5 A 0.805907 trnaTagt An01e06590 3 A 0.652557 0.6 A 0.95781 trnaFgaa An01e06680 131.4 P 0.001109 86.6 P 0.001109 trnaVcac An01e07610 90.6 P 0.04974 68.1 P 0.02987 trnaLaag An01e07880 62 P 0.000977 55.4 P 0.000977 trnaEctc An01e08320 25.9 A 0.173261 22 A 0.265142 trnaSgct An01e08330 22.9 A 0.194093 15.8 A 0.318935 trnaSgct An01e08340 17.8 A 0.194093 7.4 A 0.623158 trnaSgct An01e08350 19.1 A 0.318935 7.8 A 0.437665 trnaSgct An01e08940 36.6 P 0.014028 30.9 P 0.017085 trnaHgtg An01e09990 9.1 A 0.437665 11.7 A 0.562335 trnaSaga An01e10260 18.4 P 0.04219 18.4 A 0.173261 trnaAtgc An01e11040 115.3 P 0.001109 81.9 P 0.001109 trnaQctg An01e11050 30 A 0.27417 21.8 A 0.19458 trnaQttg An01e11060 39.6 P 0.002371 27.4 P 0.004816 trnaQctg An01e11230 104 P 0.003825 121 P 0.001109 transposon Vader - Aspergillus niger An01e11460 6.9 A 0.531264 3.4 A 0.468736 trnaCgca An01e11490 31.9 M 0.058332 39.1 P 0.02987 trnaSaga An01e11980 99.3 P 0.011455 50.7 P 0.035595 trnaYgta An01e12140 141.4 P 0.001109 117.5 P 0.001109 trnaGgcc An01e12510 36.3 A 0.136048 20.2 A 0.07897 trnaScga An01e12650 41.5 P 0.009301 47.7 P 0.007511 trnaVcac An01e12870 88.2 P 0.004816 70.7 P 0.014028 trnaLaag An01e12900 78 P 0.017085 67.9 P 0.02493 trnaLaag An01e12930 14.4 A 0.29146 13.1 A 0.376842 trnaSaga An01e13800 66.3 P 0.000977 63.3 P 0.000977 trnaEctc An01e15090 5 A 0.468736 2.2 A 0.562335 probable transposon Tndm3 - Aspergillus niger An01g00010 2 A 0.863952 8.1 A 0.652557 hypothetical protein [truncated ORF] An01g00020 23.3 A 0.318935 29.8 A 0.406973 weak similarity to nucleotide binding protein phnN - Escherichia coli An01g00030 394.2 P 0.002371 381.5 P 0.002371 strong similarity to HGH1 - Saccharomyces cerevisiae An01g00040 192.6 P 0.014028 285.4 P 0.006032 strong similarity to alpha subunit of transcription initiation factor TFIIF TFG1 - Saccharomyces cerevisiae [truncated ORF] An01g00050 57.3 M 0.058332 168.7 P 0.004816 similarity to fatty-acyl-CoA synthase beta chain FAS1 - Saccharomyces cerevisiae [truncated orf] An01g00060 776.2 P 0.001109 791.8 P 0.001109 strong similarity to fatty acid synthase, subunit alpha FAS2 - Schizosaccharomyces pombe An01g00070 73.9 P 0.020695 73.5 P 0.006032 strong similarity to N2,N2-dimethylguanosine tRNA methyltransferase trm1 - Schizosaccharomyces pombe An01g00080 98.7 P 0.001437 84.8 P 0.001437 weak similarity to probable membrane protein YOR228c - Saccharomyces cerevisiae An01g00090 35.3 A 0.437665 45.3 A 0.376842 weak similarity to hypothetical protein F21E10.7 - Arabidopsis thaliana An01g00100 950.1 P 0.001109 1046.6 P 0.001109 strong similarity to pyruvate dehydrogenase beta chain precursor PDB1 - Saccharomyces cerevisiae An01g00110 251.5 P 0.011455 272.5 P 0.007511 strong similarity to hypothetical protein SPAC1039.02 - Schizosaccharomyces pombe An01g00120 268.7 P 0.001109 295.1 P 0.001109 similarity to mitochondrial respiratory function protein MRF1 - Saccharomyces cerevisiae An01g00130 83.8 P 0.002371 81.3 P 0.001437 strong similarity to glutamyl-tRNA (Gln) amidotransferase chain A gatA - Bacillus subtilis An01g00140 22.4 A 0.173261 16 A 0.104713 weak similarity to trithorax protein ash2 - Drosophila melanogaster An01g00150 258.9 P 0.001109 288.2 P 0.001437 strong similarity to nuclear protein ENP1 - Saccharomyces cerevisiae An01g00160 1373.5 P 0.001109 1319.3 P 0.001437 similarity to regulator of unfolded protein response (UPR) Hac1p - Saccharomyces cerevisiae An01g00170 223.1 P 0.011455 208.9 P 0.014028 similarity to FTI1 protein - Saccharomyces cerevisiae An01g00190 3.5 A 0.931951 7.8 A 0.941668 similarity to PRIB protein - Lentinus edodes An01g00200 129 P 0.002371 108.7 P 0.002371 strong similarity to succinyl-CoA:3-ketoacid-CoA transferase SCOT - Homo sapiens An01g00210 40.7 A 0.136048 46.6 A 0.136048 hypothetical protein An01g00220 36.8 A 0.29146 62 A 0.136048 strong similarity to hypothetical membrane protein YJR124c - Saccharomyces cerevisiae [truncated] An01g00240 13.6 A 0.759912 22.6 A 0.531264 strong similarity to cytochrome P450 protein 4F5 - rattus norvegicus An01g00250 2.5 A 0.964405 3.2 A 0.95781 strong similarity to nitrate reductase NR2 - Arabidopsis thaliana An01g00260 1.4 A 0.783616 1.5 A 0.805907 strong similarity to hypothetical transcription activator SPAC139.03 - Schizosaccharomyces pombe An01g00270 32.4 A 0.240088 30.2 A 0.194093 similarity to fluconazole resistance protein FLU1 - Candida albicans [putative frameshift] An01g00280 123.6 P 0.003825 226.4 P 0.001437 strong similarity to hypothetical protein PAC823.14 - Schizosaccharomyces pombe An01g00290 102.4 P 0.017085 38.7 A 0.153911 similarity to the hypothetical protein encoded by An17g00430 - Aspergillus niger An01g00310 1.1 A 0.783616 2.5 A 0.805907 strong similarity to the hypothetical protein encoded by An02g10090 - Aspergillus niger An01g00320 11.5 A 0.406973 10.1 A 0.468736 similarity to the hypothetical protein encoded by An08g08380 - Aspergillus niger An01g00330 8 A 0.376842 24.3 A 0.136048 alpha-l-arabinofuranosidase a precursor abfA - Aspergillus niger An01g00340 384.5 P 0.001437 354.3 P 0.001109 strong similarity to hypothetical protein SPCC320.08 - Schizosaccharomyces pombe An01g00360 4.3 A 0.92103 3 A 0.95781 hypothetical protein An01g00370 60.9 A 0.216384 193.2 P 0.011455 strong similarity to aspergillopepsin apnS - Aspergillus phoenicis An01g00380 15.6 A 0.29146 11 A 0.29146 similarity to monocarboxylate transporter MCT3 - Homo sapiens An01g00390 116 P 0.04219 107.6 A 0.068049 hypothetical protein An01g00400 69.6 P 0.04974 67.5 P 0.04219 strong similarity to hypothetical protein SPBC12C2.09c - Schizosaccharomyces pombe An01g00420 36.9 A 0.29146 33.8 A 0.136048 strong similarity to the hypothetical protein encoded by An01g01580 - Aspergillus niger An01g00430 133 P 0.011455 50.6 P 0.04219 similarity to heterokaryon incompatibility protein het-6 - Neurospora crassa An01g00450 5.1 A 0.652557 3.7 A 0.562335 similarity to 3-hydroxyisobutyrate dehydrogenase mmsB - Pseudomonas aeruginosa An01g00460 102.8 P 0.001109 179.3 P 0.001109 hypothetical protein An01g00470 4.9 A 0.468736 19.4 A 0.194093 strong similarity to hypothetical protein jhp0584 - Helicobacter pylori An01g00480 72.5 P 0.001437 24.7 P 0.006032 strong similarity to the hypothetical protein encoded by An08g06260 - Aspergillus niger An01g00490 4.8 A 0.681065 24.7 A 0.562335 strong similarity to isoamyl alcohol oxidase mreA - Aspergillus oryzae An01g00500 21.5 A 0.07897 11 A 0.347443 hypothetical protein An01g00510 29.4 P 0.035595 19.2
Load more

Recommended publications
  • METACYC ID Description A0AR23 GO:0004842 (Ubiquitin-Protein Ligase
    Electronic Supplementary Material (ESI) for Integrative Biology This journal is © The Royal Society of Chemistry 2012 Heat Stress Responsive Zostera marina Genes, Southern Population (α=0.
    [Show full text]
  • Heterologous Expression and Identification of the Genes Involved
    Heterologous Expression and Identification of the Genes Involved in Anaerobic Degradation of 1,3-Dihydroxybenzene (Resorcinol) in Azoarcus anaerobiusᰔ Paula I. Darley,1† Jutta A. Hellstern,1†‡ Javier I. Medina-Bellver,2 Silvia Marque´s,2 Bernhard Schink,1 and Bodo Philipp1* Fachbereich Biologie, Universita¨t Konstanz, D-78457 Constance, Germany,1 and Estacio´n Experimental del Zaidı´n, C/. Profesor Albareda 1, E-18008 Granada, Spain2 Received 9 November 2006/Accepted 9 March 2007 Azoarcus anaerobius, a strictly anaerobic, gram-negative bacterium, utilizes resorcinol as a sole carbon and energy source with nitrate as an electron acceptor. Previously, we showed that resorcinol degradation by this bacterium is initiated by two oxidative steps, both catalyzed by membrane-associated enzymes that lead to the formation of hydroxyhydroquinone (HHQ; 1,2,4-benzenetriol) and 2-hydroxy-1,4-benzoquinone (HBQ). This study presents evidence for the further degradation of HBQ in cell extracts to form acetic and malic acids. To identify the A. anaerobius genes required for anaerobic resorcinol catabolism, a cosmid library with genomic DNA was constructed and transformed into the phylogenetically related species Thauera aromatica, which cannot grow with resorcinol. By heterologous complementation, a transconjugant was identified that gained the ability to metabolize resorcinol. Its cosmid, designated R؉, carries a 29.88-kb chromosomal DNA fragment containing 22 putative genes. In cell extracts of T. aromatica transconjugants, resorcinol was degraded to HHQ, HBQ, and acetate, suggesting that cosmid R؉ carried all of the genes necessary for resorcinol degradation. On the basis of the physiological characterization of T. aromatica transconjugants carrying transposon insertions -in different genes of cosmid R؉, eight open reading frames were found to be essential for resorcinol miner alization.
    [Show full text]
  • Metaproteogenomic Insights Beyond Bacterial Response to Naphthalene
    ORIGINAL ARTICLE ISME Journal – Original article Metaproteogenomic insights beyond bacterial response to 5 naphthalene exposure and bio-stimulation María-Eugenia Guazzaroni, Florian-Alexander Herbst, Iván Lores, Javier Tamames, Ana Isabel Peláez, Nieves López-Cortés, María Alcaide, Mercedes V. del Pozo, José María Vieites, Martin von Bergen, José Luis R. Gallego, Rafael Bargiela, Arantxa López-López, Dietmar H. Pieper, Ramón Rosselló-Móra, Jesús Sánchez, Jana Seifert and Manuel Ferrer 10 Supporting Online Material includes Text (Supporting Materials and Methods) Tables S1 to S9 Figures S1 to S7 1 SUPPORTING TEXT Supporting Materials and Methods Soil characterisation Soil pH was measured in a suspension of soil and water (1:2.5) with a glass electrode, and 5 electrical conductivity was measured in the same extract (diluted 1:5). Primary soil characteristics were determined using standard techniques, such as dichromate oxidation (organic matter content), the Kjeldahl method (nitrogen content), the Olsen method (phosphorus content) and a Bernard calcimeter (carbonate content). The Bouyoucos Densimetry method was used to establish textural data. Exchangeable cations (Ca, Mg, K and 10 Na) extracted with 1 M NH 4Cl and exchangeable aluminium extracted with 1 M KCl were determined using atomic absorption/emission spectrophotometry with an AA200 PerkinElmer analyser. The effective cation exchange capacity (ECEC) was calculated as the sum of the values of the last two measurements (sum of the exchangeable cations and the exchangeable Al). Analyses were performed immediately after sampling. 15 Hydrocarbon analysis Extraction (5 g of sample N and Nbs) was performed with dichloromethane:acetone (1:1) using a Soxtherm extraction apparatus (Gerhardt GmbH & Co.
    [Show full text]
  • Genome-Wide Transcriptional Changes and Lipid Profile
    G C A T T A C G G C A T genes Article Genome-Wide Transcriptional Changes and Lipid Profile Modifications Induced by Medicago truncatula N5 Overexpression at an Early Stage of the Symbiotic Interaction with Sinorhizobium meliloti Chiara Santi 1, Barbara Molesini 1, Flavia Guzzo 1, Youry Pii 2 ID , Nicola Vitulo 1 and Tiziana Pandolfini 1,* ID 1 Department of Biotechnology, University of Verona, 37134 Verona, Italy; [email protected] (C.S.); [email protected] (B.M.); fl[email protected] (F.G.); [email protected] (N.V.) 2 Faculty of Science and Technology, Free University of Bozen-Bolzano, 39100 Bolzano BZ, Italy; [email protected] * Correspondence: tiziana.pandolfi[email protected]; Tel.: +39-045-8027918 Received: 30 October 2017; Accepted: 11 December 2017; Published: 19 December 2017 Abstract: Plant lipid-transfer proteins (LTPs) are small basic secreted proteins, which are characterized by lipid-binding capacity and are putatively involved in lipid trafficking. LTPs play a role in several biological processes, including the root nodule symbiosis. In this regard, the Medicago truncatula nodulin 5 (MtN5) LTP has been proved to positively regulate the nodulation capacity, controlling rhizobial infection and nodule primordia invasion. To better define the lipid transfer protein MtN5 function during the symbiosis, we produced MtN5-downregulated and -overexpressing plants, and we analysed the transcriptomic changes occurring in the roots at an early stage of Sinorhizobium meliloti infection. We also carried out the lipid profile analysis of wild type (WT) and MtN5-overexpressing roots after rhizobia infection. The downregulation of MtN5 increased the root hair curling, an early event of rhizobia infection, and concomitantly induced changes in the expression of defence-related genes.
    [Show full text]
  • Table S1-Final.Xlsx
    Table S1. Functional gene families covered on the GeoChip 5.0. No. of sequence‐ No. of group‐ No. of total No. of covered No. of total Category Subcategory Subcategory 2 Gene Encoded Enzyme specific probesa specific probesa probes on 5M CDSa probes on 5S Categories for Geochemical Cycling Carbon Cycling Carbon Degradation Agar beta_agarase Agarase 42 79 217 121 Agar Total 42 79 0 217 121 Alginate alginase Alginase 45 200 512 245 Alginate Total 45 200 0 512 245 Cellulose Endoglucanase Endoglucanase 198 248 446 740 343 Cellulose Total 198 248 446 740 343 Chitin Acetylglucosaminidase Acetylglucosaminidase 119 976 1095 3088 1116 Chitinase Chitinase 649 1231 1880 3285 1411 endochitinase Endochitinase 213 334 1104 547 exochitinase Exochitinase 14 55 259 69 Chitin Total 995 2596 2975 7736 3143 Glyoxylate cycle AceA Isocitrate lyase 69 373 442 887 0 AceB Malate synthase A 90 610 700 1457 0 Glyoxylate cycle Total 159 983 1142 2344 0 Hemicellulose Ara Arabinofuranosidase 172 543 715 1367 827 Mannanase Mannanase 159 238 397 639 478 Xylanase Xylanase 150 653 803 1739 858 Hemicellulose Total 481 1434 1915 3745 2163 Heparin heparinase Heparinase 7 53 166 60 Heparin Total 7 53 0 166 60 Hyaluronic acid hyaluronidase Hyaluronidase 880 383 88 Hyaluronidase Total 8 80 0 383 88 Lignin Glx Glyoxal oxidase 103 40 143 178 125 Mnp Manganese peroxidase 50 13 63 74 66 Phenol_oxidase Laccase or phenol oxidase 188 372 560 1009 677 Lignin Total 341 425 766 1261 868 Pectin Pectinase (pectate_lyase) Pectate lyase 53 252 305 827 321 Pme Pectin methylesterase 25 240 265
    [Show full text]
  • Association Between the Gut Microbiota and Blood Pressure in a Population Cohort of 6953 Individuals
    Journal of the American Heart Association ORIGINAL RESEARCH Association Between the Gut Microbiota and Blood Pressure in a Population Cohort of 6953 Individuals Joonatan Palmu , MD; Aaro Salosensaari , MSc; Aki S. Havulinna , DSc (Tech); Susan Cheng , MD, MPH; Michael Inouye, PhD; Mohit Jain, MD, PhD; Rodolfo A. Salido , BSc; Karenina Sanders , BSc; Caitriona Brennan, BSc; Gregory C. Humphrey, BSc; Jon G. Sanders , PhD; Erkki Vartiainen , MD, PhD; Tiina Laatikainen , MD, PhD; Pekka Jousilahti, MD, PhD; Veikko Salomaa , MD, PhD; Rob Knight , PhD; Leo Lahti , DSc (Tech); Teemu J. Niiranen , MD, PhD BACKGROUND: Several small-scale animal studies have suggested that gut microbiota and blood pressure (BP) are linked. However, results from human studies remain scarce and conflicting. We wanted to elucidate the multivariable-adjusted as- sociation between gut metagenome and BP in a large, representative, well-phenotyped population sample. We performed a focused analysis to examine the previously reported inverse associations between sodium intake and Lactobacillus abun- dance and between Lactobacillus abundance and BP. METHODS AND RESULTS: We studied a population sample of 6953 Finns aged 25 to 74 years (mean age, 49.2±12.9 years; 54.9% women). The participants underwent a health examination, which included BP measurement, stool collection, and 24-hour urine sampling (N=829). Gut microbiota was analyzed using shallow shotgun metagenome sequencing. In age- and sex-adjusted models, the α (within-sample) and β (between-sample) diversities of taxonomic composition were strongly re- lated to BP indexes (P<0.001 for most). In multivariable-adjusted models, β diversity was only associated with diastolic BP (P=0.032).
    [Show full text]
  • Phosphodiesterase 1B Knock-Out Mice Exhibit Exaggerated Locomotor Hyperactivity and DARPP-32 Phosphorylation in Response to Dopa
    The Journal of Neuroscience, June 15, 2002, 22(12):5188–5197 Phosphodiesterase 1B Knock-Out Mice Exhibit Exaggerated Locomotor Hyperactivity and DARPP-32 Phosphorylation in Response to Dopamine Agonists and Display Impaired Spatial Learning Tracy M. Reed,1,3 David R. Repaske,2* Gretchen L. Snyder,4 Paul Greengard,4 and Charles V. Vorhees1* Divisions of 1Developmental Biology and 2Endocrinology, Children’s Hospital Research Foundation, Cincinnati, Ohio 45229, 3Department of Biology, College of Mount St. Joseph, Cincinnati, Ohio 45233, and 4Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, New York 10021 Using homologous recombination, we generated mice lack- maze spatial-learning deficits. These results indicate that en- ing phosphodiesterase-mediated (PDE1B) cyclic nucleotide- hancement of cyclic nucleotide signaling by inactivation of hydrolyzing activity. PDE1B Ϫ/Ϫ mice showed exaggerated PDE1B-mediated cyclic nucleotide hydrolysis plays a signifi- hyperactivity after acute D-methamphetamine administra- cant role in dopaminergic function through the DARPP-32 and tion. Striatal slices from PDE1B Ϫ/Ϫ mice exhibited increased related transduction pathways. levels of phospho-Thr 34 DARPP-32 and phospho-Ser 845 Key words: phosphodiesterases; DARPP-32; dopamine- GluR1 after dopamine D1 receptor agonist or forskolin stimu- stimulated locomotor activity; spatial learning and memory; lation. PDE1B Ϫ/Ϫ and PDE1B ϩ/Ϫ mice demonstrated Morris Morris water maze; methamphetamine; SKF81297; forskolin Calcium/calmodulin-dependent phosphodiesterases (CaM- (CaMKII) and calcineurin and have the potential to activate PDEs) are members of one of 11 families of PDEs (Soderling et CaM-PDEs. Dopamine D1 or D2 receptor activation leads to al., 1999;Yuasa et al., 2001) and comprise the only family that acts adenylyl cyclase activation or inhibition, respectively (Traficante ϩ as a potential point of interaction between the Ca 2 and cyclic et al., 1976; Monsma et al., 1990; Cunningham and Kelley, 1993; nucleotide signaling pathways.
    [Show full text]
  • N-Glycan Trimming in the ER and Calnexin/Calreticulin Cycle
    Neurotransmitter receptorsGABA and A postsynapticreceptor activation signal transmission Ligand-gated ion channel transport GABAGABA Areceptor receptor alpha-5 alpha-1/beta-1/gamma-2 subunit GABA A receptor alpha-2/beta-2/gamma-2GABA receptor alpha-4 subunit GABAGABA receptor A receptor beta-3 subunitalpha-6/beta-2/gamma-2 GABA-AGABA receptor; A receptor alpha-1/beta-2/gamma-2GABA receptoralpha-3/beta-2/gamma-2 alpha-3 subunit GABA-A GABAreceptor; receptor benzodiazepine alpha-6 subunit site GABA-AGABA-A receptor; receptor; GABA-A anion site channel (alpha1/beta2 interface) GABA-A receptor;GABA alpha-6/beta-3/gamma-2 receptor beta-2 subunit GABAGABA receptorGABA-A receptor alpha-2receptor; alpha-1 subunit agonist subunit GABA site Serotonin 3a (5-HT3a) receptor GABA receptorGABA-C rho-1 subunitreceptor GlycineSerotonin receptor subunit3 (5-HT3) alpha-1 receptor GABA receptor rho-2 subunit GlycineGlycine receptor receptor subunit subunit alpha-2 alpha-3 Ca2+ activated K+ channels Metabolism of ingested SeMet, Sec, MeSec into H2Se SmallIntermediateSmall conductance conductance conductance calcium-activated calcium-activated calcium-activated potassium potassium potassiumchannel channel protein channel protein 2 protein 1 4 Small conductance calcium-activatedCalcium-activated potassium potassium channel alpha/beta channel 1 protein 3 Calcium-activated potassiumHistamine channel subunit alpha-1 N-methyltransferase Neuraminidase Pyrimidine biosynthesis Nicotinamide N-methyltransferase Adenosylhomocysteinase PolymerasePolymeraseHistidine basic
    [Show full text]
  • Reduction of Pectinesterase Activity in a Commercial Enzyme Preparation
    Journal of the Science of Food and Agriculture J Sci Food Agric 85:1613–1621 (2005) DOI: 10.1002/jsfa.2154 Reduction of pectinesterase activity in a commercial enzyme preparation by pulsed electric fields: comparison of inactivation kinetic models Joaquın´ Giner, Pascal Grouberman, Vicente Gimeno and Olga Martın´ ∗ Department of Food Technology, University of Lleida, CeRTA-UTPV, ETSEA, Avda Alcalde Rovira Roure 191, 25198-Lleida, Spain Abstract: The inactivation of pectinesterase (PE) in a commercial enzyme preparation (CEP) under high intensity pulsed electric fields (HIPEF) was studied. After desalting and water dilution of the raw CEP, samples were exposed to exponentially decay waveform pulses for up to 463 µs at electric field intensities ranging from 19 to 38 kV cm−1. Pulses were applied in monopolar mode. Experimental data were fitted to a first-order kinetic model as well as to models based on Fermi, Hulsheger¨ or Weibull equations to describe PE inactivation kinetics. Characteristic parameters for each model were calculated. Relationships between some of the parameters and process variables were obtained. The Weibull model yielded the best accuracy factor. The relationship between residual PE and input of electrical energy density was found to be that of exponential decay. 2005 Society of Chemical Industry Keywords: pulsed electric fields; kinetics; pectinesterase; model; inactivation INTRODUCTION It has become customary to use CEPs in fruit and Pectinesterase (PE; EC 3.1.1.11) is a pectic enzyme vegetable juice technology. Depending
    [Show full text]
  • Regulation of Calmodulin-Stimulated Cyclic Nucleotide Phosphodiesterase (PDE1): Review
    95-105 5/6/06 13:44 Page 95 INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE 18: 95-105, 2006 95 Regulation of calmodulin-stimulated cyclic nucleotide phosphodiesterase (PDE1): Review RAJENDRA K. SHARMA, SHANKAR B. DAS, ASHAKUMARY LAKSHMIKUTTYAMMA, PONNIAH SELVAKUMAR and ANURAAG SHRIVASTAV Department of Pathology and Laboratory Medicine, College of Medicine, University of Saskatchewan, Cancer Research Division, Saskatchewan Cancer Agency, 20 Campus Drive, Saskatoon SK S7N 4H4, Canada Received January 16, 2006; Accepted March 13, 2006 Abstract. The response of living cells to change in cell 6. Differential inhibition of PDE1 isozymes and its environment depends on the action of second messenger therapeutic applications molecules. The two second messenger molecules cAMP and 7. Role of proteolysis in regulating PDE1A2 Ca2+ regulate a large number of eukaryotic cellular events. 8. Role of PDE1A1 in ischemic-reperfused heart Calmodulin-stimulated cyclic nucleotide phosphodiesterase 9. Conclusion (PDE1) is one of the key enzymes involved in the complex interaction between cAMP and Ca2+ second messenger systems. Some PDE1 isozymes have similar kinetic and 1. Introduction immunological properties but are differentially regulated by Ca2+ and calmodulin. Accumulating evidence suggests that the A variety of cellular activities are regulated through mech- activity of PDE1 is selectively regulated by cross-talk between anisms controlling the level of cyclic nucleotides. These Ca2+ and cAMP signalling pathways. These isozymes are mechanisms include synthesis, degradation, efflux and seque- also further distinguished by various pharmacological agents. stration of cyclic adenosine 3':5'-monophosphate (cAMP) and We have demonstrated a potentially novel regulation of PDE1 cyclic guanosine 3':5'- monophosphate (cGMP) within the by calpain.
    [Show full text]
  • Tannin Degradation by Phytopathogen's Tannase: a Plant's
    Biocatalysis and Agricultural Biotechnology 21 (2019) 101342 Contents lists available at ScienceDirect Biocatalysis and Agricultural Biotechnology journal homepage: http://www.elsevier.com/locate/bab Tannin degradation by phytopathogen’s tannase: A Plant’s defense perspective Kanti Prakash Sharma Department of Biosciences, Mody University of Science and Technology, Lakshmangarh, Sikar, Rajasthan, 332311, India ARTICLE INFO ABSTRACT Keywords: Tannins are plant secondary metabolites and characterized as plant defensive molecules. They impose a barrier Tannin against phytopathogens invasion in plants and thus oppose diseases occurrence in them. Tannase is an enzyme Tannase known for its ability to degrade plant tannins. Important plant pathogens also possess tannase coding sequence in Plant defense their genome. Researches on tannase are till date focused on its applications in animal nutrition, in bioreme­ Pathogen diation and in food industries etc. The information about tannase role with respect to pathogen’s virulence is Virulence very scanty or almost nil in scientific literature. The presence of tannase in pathogen’s genome is an adaptive feature which may be a part of its strategy to overcome the negative effects of plants tannins. The present review summarizes important aspects of tannase and its possible role in disease causing ability of pathogens in plants. 1. Introduction hydrolyzable tannins (Zhang et al., 2001). In complex tannins, a cate­ chin or epicatechin unit is bound glycosidically to a gallotannin or an Tannins are universally present in plants and represent the fourth ellagitannin unit to yield catechin or epicatechin and gallic acid or most abundant group of secondary metabolites after cellulose, hemi­ ellagic acid upon hydrolysis.
    [Show full text]
  • Maleylacetate Reductase from Trichosporon Cutaneum
    Biochem. J. (1980) 185, 783-786 783 Printed in Great Britain Maleylacetate Reductase from Trichosporon cutaneum Andras B. GAAL and Halina Y. NEUJAHR Department ofBiochemistry and Biochemical Technology, The Royal Institute of Technology, S 100 44 Stockholm, Sweden (Received 12 November 1979) The enzyme catalysing the reduction of maleylacetate to 3-oxoadipate was purified 150-fold from Trichosporon cutaneum, induced for aromatic metabolism by growth with resorcinol as a major carbon source. The enzyme separated upon electrofocusing into three species with pI values 4.6, 5.1 and 5.6. They had similar catalytic properties and the same molecular weight. Our group has previously reported that the yeast fer, pH 7.6, 0.2pmol of maleylacetate, 0.2,mol of Trichosporon cutaneum can be induced to metabol- NADPH and 50-200#ug of enzyme protein. Under ize phenol and resorcinol, both phenols being these conditions 1 enzyme unit corresponds to an attacked by the same hydroxylating enzyme and the absorbance decrease of 6.1 A340 units/min. same ring-cleavage enzyme (Neujahr & Varga, Determination of molecular weight. Molecular 1970; Varga & Neujahr, 1970). We have since weight was determined by gel filtration (Andrews, demonstrated that both phenol and resorcinol are 1965) on a Sephadex G-150 column metabolized to 3-oxoadipate (Gaal & Neujahr, (2.5cm x 85cm) equilibrated with 50mM-Tris/ 1979). The metabolism of resorcinol goes through H2SO4 buffer, pH 7.6. Alcohol dehydrogenase 1,2,4-trihydroxybenzene and maleylacetate. The (mol.wt. 150000), lactate dehydrogenase (mol.wt. enzyme catalysing the reduction of maleylacetate to 136000), hexokinase (mol.wt. 105000) and avidin 3-oxoadipate was enriched from crude extracts (mol.wt.
    [Show full text]