DOCSLIB.ORG

Genetic and Molecular Analysis of Two New Loci Controlling Flowering in Garden Pea

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Genetic and Molecular Analysis of Two New Loci Controlling Flowering in Garden Pea Genetic and molecular analysis of two new loci controlling flowering in garden pea By A S M Mainul Hasan School of Natural Sciences Submitted in fulfilment of the requirements for the degree of Doctor of Philosophy University of Tasmania, July 2018 Declaration of originality This thesis contains no material which has been accepted for a degree or diploma by the University or any other institution, except by way of background information and duly acknowledge in the thesis, and to the best of my knowledge and belief no material previously published or written by another person except where due acknowledgement is made in the text of the thesis, nor does the thesis contain any material that infringes copyright. Authority of access This thesis may be made available for loan. Copying and communication of any part of this thesis is prohibited for two years from the date this statement was signed; after that time limited copying and communication is permitted in accordance with the Copyright Act 1968. Date: 6-07-2018 A S M Mainul Hasan i Abstract Flowering is one of the key developmental process associated with the life cycle of plant and it is regulated by different environmental factors and endogenous cues. In the model species Arabidopsis thaliana a mobile protein, FLOWERING LOCUS T (FT) plays central role to mediate flowering time and expression of FT is regulated by photoperiod. While flowering mechanisms are well-understood in A. thaliana, knowledge about this process is limited in legume (family Fabaceae) which are the second major group of crops after cereals in satisfying the global demand for food and fodder. Due to its short generation time, ability to reproduce via self or cross-pollination and availability of diverse lines, garden pea (Pisum sativum) serves as a model legume species for flowering time studies. Isolation and characterization of mutants have been a key research strategy in order to identify genes responsible for flowering in pea. The current study involved investigation of two novel EMS mutants namely late3 and late4 in the background of a cultivated pea line NGB5839 which are extremely late flowering indicating that LATE3 and LATE4 are essential for normal promotion of flowering in pea. Detailed phenotypic characterization carried out in the present study showed that both the loci positively regulate various vegetative, reproductive and yield related traits across different growth stages strongly suggesting potential global regulatory role for the underlying genes. Prior to the present study, synteny between pea and a closely related species, M. truncatula was exploited in order to roughly map LATE3 and LATE4 at the middle of pea LGIII and bottom of LGV respectively. These positions were significantly refined in the present study as LATE3 and LATE4 were mapped within a narrow genetic intervals in the syntenic regions of M. truncatula consisted of 62 (chromosome 3) and 54 (chromosome 7) genes respectively. Usage of the high-throughput RNA sequencing technology along with phylogenetic, co- segregation analysis and direct sequencing assisted in determining LATE3 and LATE4 genes as the pea homologue of Cyclin Dependent Kinase 8 (PsCDK8) and Cyclin C (PsCYCC1). CDK8 and CYCC1 are components of highly conserved CDK8 module (along with MED12 and MED13) of eukaryotic mediator complex that negatively regulate transcription of various genes involved in different biological processes. Analysis of the entire mediator complex revealed that this ii complex is highly conserved in A. thaliana, M. truncatula and pea. Phenotypic characterization of loss-of-function mutant of novel flowering gene CYCC1 in A. thaliana exhibited delayed flowering similar to already known similar mutants of AtCDK8, AtMED12 and AtMED13 which was consistent with the notion that these four genes act together to carry out the same regulatory process. Genetic interaction and yeast two hybrid assay unveiled complementarity and strong physical interaction between LATE3 and LATE4 which strongly suggested that these two genes act in the same regulatory process in a likely inter-dependent manner. Further genetic and regulatory interaction studies involving already known key pea flowering loci showed that LATE3 and LATE4 mediate flowering by regulating expression of known genes such as FTa1, FTc, PIM (PsAP1), VEG1(PsFULc), UNI (PsLFY)and VEG2 (PsFD) and LF (PsTF1c). The present study also undertook a systems biology approach for generating relevant hypothesis about the function and regulation of LATE3 and LATE4 genes. To this end, STRING v10.5 predicted the potential interactome network of AtCDK8 and AtCYCC1 consisted of members from cell cycle and mediator complex indicating a conserved role for them. In addition, predicted functions of MtCDK8 and MtCYCC1 genes obtained from AraNET v2.0 database was similar to that of PsCDK8, PsCYCC1, AtCYCC1 genes, thus giving hints of potential conservation of the function of both the genes in plant system. Moreover, PlantTFDB v4.0 database was used to forecast the transcription factors that may regulate the function of CDK8 and CYCC1 genes in M. truncatula and pea. As various mediator complex genes in A. thaliana are known to be involved in the regulatory processes driving response to different environmental factors, therefore relevant experimentation have shown that both LATE3 and LATE4 genes are important for controlling response to general light/darkness, ambient temperature, UVB, heat, mechanical wound and salt stress in pea. Overall, the present study provided significant understanding about the role of LATE3/PsCDK8 and LATE4/PsCYCC1 in mediating diverse range of reproductive, developmental and adaptive characteristics in pea where flowering time was the most important trait. iii Acknowledgements During my journey as a PhD student at the School of Natural Sciences, University of Tasmania I have received assistance from many individuals and I would like to humbly convey my gratitude to all of them. First of all, I would like to thank my primary supervisor and mentor Dr. Jim Weller who always managed time for me whenever I sought guidance for any aspects of the project be it laboratory/glasshouse work, writing the thesis or attending conferences. I indeed believe that I have become a better scientist over the past three and half years where his leadership played a significant role. Likewise, I am thankful to my second supervisor Dr. Valerie Hecht whose technical expertise and in-depth knowledge about various aspects of flowering time regulation have contributed immensely towards my development as a PhD student. Special thanks goes to my colleague Jackie Vander Schoor who has played significant role in the development of this project at different stages. Another person who has offered guidance and inspiration regarding my academic responsibilities and ownership of my PhD project is my graduate research coordinator Dr. Erik Wapstra and therefore I am beholden to him. Next, I would like to acknowledge helps that I have received from my colleague Raul Ortega for useful discussion about various issues related to my PhD project. I am also conveying similar humility to Dr. Lu Wang specifically for the A. thaliana part of the project. In addition, I am grateful for various suggestions and scientific brainstorming by my former and current group mates Dr. Frances Sussmilch, Dr. Steven Ridge, Dr. Vinodan Rajendran, Owen Williams, Beatriz Contreras, Andy Rubenach and Kelsey Picard. Colleagues in the glass house Michelle Lang and Tracy Winterbottom were fantastic and cooperative and their help from time to time is highly appreciated. The same humbleness goes to recognize the assistance of colleagues from CSL molecular biology laboratory Adam Smolenski and Sharee McCammon. I would also like to thank the bigger family of the School of Natural Sciences specially those with whom I worked as part of the school’s student organization in organizing various social events in the first year of the PhD. In addition, I would like to thank University of Tasmania and Australian Research council for providing financial iv support for this project. Moreover, I am thankful to Australian Society of Plant Scientists (ASPS) for providing grant in order to be able to attend the Combio 2017 conference in Adelaide. I would like to specifically mention the contributions being made by my previous professional mentors Prof. Dr. Dr. Wolfgang Friedt, late Dr. Patrick Schweizer and Dr. Thorsten Schnurbusch towards my development which enabled me to undertake intensive plant molecular genetics based research in the form of a PhD. I am highly indebted to my lovely wife who constantly provided support and took care of various aspects of my life during this period. At this specific junction of my life, I would also like to convey utmost respect and gratitude to my mother, late father and elder brothers without whom I would not have been where I am today. Besides, I would like to thank my fellow compatriots living in Hobart for their consistent assistance and care about different matters during my stay as a PhD student in this city. v Conference proceedings from this project Invited talk: A.S.M Mainul Hasan, Valerie Hecht, Jacqueline K. Vander Schoor, Jim Weller, October 30-November 1, 2017. Genetic and molecular analysis of two new loci controlling flowering in garden pea, Pisum sativum. In: Australasian Genomics Technologies Association Conference, Hobart, Australia. Poster presentation: A.S.M Mainul Hasan, Valerie Hecht, Jacqueline K. Vander Schoor, Jim Weller, October 4-6, 2017. Genetic and molecular analysis of two new loci controlling flowering in garden pea, Pisum sativum. In: Combio 2017, Adelaide Convention Centre, Adelaide, Australia. vi Abbreviation 3AT 3-amino-1,2,4-triazole ABA Abscisic acid AFR SAP30 FUNCTION-RELATED AGL18 AGAMOUS LIKE 18 ANOVA Analysis of variance AP1 APETALA1 bp Base pair bZIP Basic leucine zipper CAPS Cleaved amplified polymorphic sequence CDF CYCLING DOF FACTOR CDK8 Cyclin Dependent Kinase 8 cDNA Complemetary Deoxyribonucleic Acid cM Centi Morgan CO CONSTANS Col-0 Columbia 0 CRY2 CRYPTOCHROME 2 CSM Cryptic splice motif CSS Cryptic splice site cv.
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]
  • 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]
  • Peroxidase Activity As an Indicator of the Iron Deficiency in Banana
    IndianJ Plant Physiol., Vol. 5, No.4, (N.S.) pp. 389-391 (Oct.-Dec., 2000) SHORT COMMUNICATION PEROXIDASE ACTIVITY AS AN INDICATOR OF THE IRON DEFICIENCY IN BANANA K. BALAKRISHNAN Department ofCrop Physiology, Horticultural College and Research Institute, Periyakulam - 625 604 Received on 30 Sept., 1998, Revised on 30 Nov., 2000 Effect oflime induced iron chlorosis on enzyme activities was studied in Banana cv. Rasthali. Iron content decreased progressively as the intensity of chlorosis increased. Iron content had positive correlation with catalase, peroxidase, acid phosphatase, polyphenol oxidase and nitrate reductase. Among the enzymes, the activityofperoxidasehad highest positivesignificant(r=997**) associationwith Fecontent. Hence, peroxidase activity could serve as a diagnostic tool to indentify the Fe deficiency/Fe status in Banana. Key words: Banana, chlorosis, iron, peroxidase Among the micrountrients, Fe deficiency is the most ofgreenness in sixmonths old crop. This leafwas used for widespread in ourcountry(Takkar, 1996). Iron deficiency all the physiological analysis viz chlorophyll (Yoshida et is very common in calcareous soils and hence termed as al., 1976) chlorophyllase (Almela et al., 1990), catalase, lime induced iron chlorosis. In a normal green plant 60% peroxidase and polyphenol oxidase (Kar and Mishra, ofall leafiron is present in the chlorophyIl and hence any 1976), acid phosphatase (Parida and Mishra, 1980) and reduction in Fe contentcauses chlorosis (Chen and Barak, nitrate reductase (Klepperetal., 1973). The Fe content of 1982). Iron deficiency in plant not only causes chlorosis the plant sample was estimated using atomic absorption because of its involvement in chlorophyll synthesis, but spectrophotometry. Data were subjected to simple also reduces the activity ofcertain enzymes viz., catalase correlation co-efficient.
    [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]
  • Phospholipases, Nucleic Acids Encoding Them and Methods for Making and Using Them
    (19) TZZ¥_Z_ _T (11) EP 3 190 182 A1 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 12.07.2017 Bulletin 2017/28 C12N 9/20 (2006.01) C12N 1/20 (2006.01) C12N 15/00 (2006.01) C07H 21/04 (2006.01) (21) Application number: 16184319.8 (22) Date of filing: 08.03.2005 (84) Designated Contracting States: • FIELDING, Roderick AT BE BG CH CY CZ DE DK EE ES FI FR GB GR San Diego, CA 92109 (US) HU IE IS IT LI LT LU MC NL PL PT RO SE SI SK TR • BROWN, Robert C. San Diego, CA 92130 (US) (30) Priority: 08.03.2004 US 796907 • VASAVADA, Amit Poway, CA 92064 (US) (62) Document number(s) of the earlier application(s) in • TAN, Xuqiu accordance with Art. 76 EPC: San Diego, CA 92130 (US) 05727242.9 / 1 748 954 • BADILLO, Adrian Poway, CA 92064 (US) (27) Previously filed application: • VAN HOEK, Wilhelmus P. 08.03.2005 PCT/US2005/007908 San Diego, CA 92126 (US) • JANSSEN, Giselle (71) Applicant: DSM IP Assets B.V. San Diego, CA 92121 (US) 6411 TE Heerlen (NL) • ISAAC, Charles Carlsbad, CA 92008 (US) (72) Inventors: • BURK, Mark J. • GRAMATIKOVA, Svetlana San Diego, CA 92130 (US) San Diego, CA 92122 (US) • HAZLEWOOD, Geoff (74) Representative: Cazemier, Anne Engeline et al San Diego, CA 92130 (US) DSM Intellectual Property •LAM,David P.O. Box 4 Encinitas, CA 92024 (US) 6100 AA Echt (NL) • BARTON, Nelson R. San Diego, CA 92131 (US) Remarks: • STURGIS, Blake G. •A request for correction of the description has been Solana Beach, CA 92075 (US) filed pursuant to Rule 139 EPC.
    [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]
  • Legionella Genus Genome Provide Multiple, Independent Combinations for Replication in Human Cells
    Supplemental Material More than 18,000 effectors in the Legionella genus genome provide multiple, independent combinations for replication in human cells Laura Gomez-Valero1,2, Christophe Rusniok1,2, Danielle Carson3, Sonia Mondino1,2, Ana Elena Pérez-Cobas1,2, Monica Rolando1,2, Shivani Pasricha4, Sandra Reuter5+, Jasmin Demirtas1,2, Johannes Crumbach1,2, Stephane Descorps-Declere6, Elizabeth L. Hartland4,7,8, Sophie Jarraud9, Gordon Dougan5, Gunnar N. Schroeder3,10, Gad Frankel3, and Carmen Buchrieser1,2,* Table S1: Legionella strains analyzed in the present study Table S2: Type IV secretion systems predicted in the genomes analyzed Table S3: Eukaryotic like domains identified in the Legionella proteins analyzed Table S4: Small GTPases domains detected in the genus Legionella as defined in the CDD ncbi domain database Table S5: Eukaryotic like proteins detected in the Legionella genomes analyzed in this study Table S6: Aminoacid identity of the Dot/Icm components in Legionella species with respect to orthologous proteins in L. pneumophila Paris Table S7: Distribution of seventeen highly conserved Dot/Icm secreted substrates Table S8: Comparison of the effector reperotoire among strains of the same Legionella species Table S9. Number of Dot/Icm secreted proteins predicted in each strain analyzed Table S10: Replication capacity of the different Legionella species analyzed in this study and collection of literature data on Legionella replication Table S11: Orthologous table for all genes of the 80 analyzed strains based on PanOCT. The orthologoss where defined with the program PanOCT using the parameters previously indicated in material and methods.) Figure S1: Distribution of the genes predicted to encode for the biosynthesis of flagella among all Legionella species.
    [Show full text]
  • Open Matthew R Moreau Ph.D. Dissertation Finalfinal.Pdf
    The Pennsylvania State University The Graduate School Department of Veterinary and Biomedical Sciences Pathobiology Program PATHOGENOMICS AND SOURCE DYNAMICS OF SALMONELLA ENTERICA SEROVAR ENTERITIDIS A Dissertation in Pathobiology by Matthew Raymond Moreau 2015 Matthew R. Moreau Submitted in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy May 2015 The Dissertation of Matthew R. Moreau was reviewed and approved* by the following: Subhashinie Kariyawasam Associate Professor, Veterinary and Biomedical Sciences Dissertation Adviser Co-Chair of Committee Bhushan M. Jayarao Professor, Veterinary and Biomedical Sciences Dissertation Adviser Co-Chair of Committee Mary J. Kennett Professor, Veterinary and Biomedical Sciences Vijay Kumar Assistant Professor, Department of Nutritional Sciences Anthony Schmitt Associate Professor, Veterinary and Biomedical Sciences Head of the Pathobiology Graduate Program *Signatures are on file in the Graduate School iii ABSTRACT Salmonella enterica serovar Enteritidis (SE) is one of the most frequent common causes of morbidity and mortality in humans due to consumption of contaminated eggs and egg products. The association between egg contamination and foodborne outbreaks of SE suggests egg derived SE might be more adept to cause human illness than SE from other sources. Therefore, there is a need to understand the molecular mechanisms underlying the ability of egg- derived SE to colonize the chicken intestinal and reproductive tracts and cause disease in the human host. To this end, the present study was carried out in three objectives. The first objective was to sequence two egg-derived SE isolates belonging to the PFGE type JEGX01.0004 to identify the genes that might be involved in SE colonization and/or pathogenesis.
    [Show full text]
  • Short De-Etiolation Increases the Rooting of VC801 Avocado Rootstock
    plants Article Short De-Etiolation Increases the Rooting of VC801 Avocado Rootstock Zvi Duman 1,2, Gal Hadas-Brandwein 1,2, Avi Eliyahu 1,2, Eduard Belausov 1, Mohamad Abu-Abied 1, Yelena Yeselson 1, Adi Faigenboim 1, Amnon Lichter 3, Vered Irihimovitch 1 and Einat Sadot 1,* 1 The Institute of Plant Sciences, The Volcani Center, ARO, 68 HaMaccabim Road, Rishon LeZion 7528809, Israel; [email protected] (Z.D.); [email protected] (G.H.-B.); [email protected] (A.E.); [email protected] (E.B.); [email protected] (M.A.-A.); [email protected] (Y.Y.); [email protected] (A.F.); [email protected] (V.I.) 2 The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, The Robert H. Smith Faculty of Agriculture, Food and Environment, The Hebrew University of Jerusalem, Rehovot 7610001, Israel 3 The Institute of Post Harvest and Food Sciences, The Volcani Center, ARO, 68 HaMaccabim Road, Rishon LeZion 7528809, Israel; [email protected] * Correspondence: [email protected] Received: 5 August 2020; Accepted: 2 November 2020; Published: 3 November 2020 Abstract: Dark-grown (etiolated) branches of many recalcitrant plant species root better than their green counterparts. Here it was hypothesized that changes in cell-wall properties and hormones occurring during etiolation contribute to rooting efficiency. Measurements of chlorophyll, carbohydrate and auxin contents, as well as tissue compression, histological analysis and gene-expression profiles were determined in etiolated and de-etiolated branches of the avocado rootstock VC801. Differences in chlorophyll content and tissue rigidity, and changes in xyloglucan and pectin in cambium and parenchyma cells were found.
    [Show full text]
  • The Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and Disease Jonathan Z
    REVIEW pubs.acs.org/CR The Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and Disease Jonathan Z. Long* and Benjamin F. Cravatt* The Skaggs Institute for Chemical Biology and Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United States CONTENTS 2.4. Other Phospholipases 6034 1. Introduction 6023 2.4.1. LIPG (Endothelial Lipase) 6034 2. Small-Molecule Hydrolases 6023 2.4.2. PLA1A (Phosphatidylserine-Specific 2.1. Intracellular Neutral Lipases 6023 PLA1) 6035 2.1.1. LIPE (Hormone-Sensitive Lipase) 6024 2.4.3. LIPH and LIPI (Phosphatidic Acid-Specific 2.1.2. PNPLA2 (Adipose Triglyceride Lipase) 6024 PLA1R and β) 6035 2.1.3. MGLL (Monoacylglycerol Lipase) 6025 2.4.4. PLB1 (Phospholipase B) 6035 2.1.4. DAGLA and DAGLB (Diacylglycerol Lipase 2.4.5. DDHD1 and DDHD2 (DDHD Domain R and β) 6026 Containing 1 and 2) 6035 2.1.5. CES3 (Carboxylesterase 3) 6026 2.4.6. ABHD4 (Alpha/Beta Hydrolase Domain 2.1.6. AADACL1 (Arylacetamide Deacetylase-like 1) 6026 Containing 4) 6036 2.1.7. ABHD6 (Alpha/Beta Hydrolase Domain 2.5. Small-Molecule Amidases 6036 Containing 6) 6027 2.5.1. FAAH and FAAH2 (Fatty Acid Amide 2.1.8. ABHD12 (Alpha/Beta Hydrolase Domain Hydrolase and FAAH2) 6036 Containing 12) 6027 2.5.2. AFMID (Arylformamidase) 6037 2.2. Extracellular Neutral Lipases 6027 2.6. Acyl-CoA Hydrolases 6037 2.2.1. PNLIP (Pancreatic Lipase) 6028 2.6.1. FASN (Fatty Acid Synthase) 6037 2.2.2. PNLIPRP1 and PNLIPR2 (Pancreatic 2.6.2.
    [Show full text]