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Effects of Altered Expression of the Sumo Conjugating Enzyme, UBC9 on Mitosis, Meiosis and Conjugation in Tetrahymena Thermophila Qianyi Yang Purdue University
Purdue University Purdue e-Pubs Open Access Dissertations Theses and Dissertations Fall 2014 Effects of altered expression of the sumo conjugating enzyme, UBC9 on mitosis, meiosis and conjugation in Tetrahymena thermophila Qianyi Yang Purdue University Follow this and additional works at: https://docs.lib.purdue.edu/open_access_dissertations Part of the Biochemistry Commons, and the Molecular Biology Commons Recommended Citation Yang, Qianyi, "Effects of altered expression of the sumo conjugating enzyme, UBC9 on mitosis, meiosis and conjugation in Tetrahymena thermophila" (2014). Open Access Dissertations. 395. https://docs.lib.purdue.edu/open_access_dissertations/395 This document has been made available through Purdue e-Pubs, a service of the Purdue University Libraries. Please contact [email protected] for additional information. Graduate School Form 30 (Revised 08/14) PURDUE UNIVERSITY GRADUATE SCHOOL Thesis/Dissertation Acceptance This is to certify that the thesis/dissertation prepared By Qianyi Yang Entitled EFFECTS OF ALTERED EXPRESSION OF THE SUMO CONJUGATING ENZYME, UBC9 ON MITOSIS, MEIOSIS AND CONJUGATION IN TETRAHYMENA THERMOPHILA Doctor of Philosophy For the degree of Is approved by the final examining committee: James D. Forney Scott D. Briggs Mark C. Hall Clifford F. Weil To the best of my knowledge and as understood by the student in the Thesis/Dissertation Agreement, Publication Delay, and Certification/Disclaimer (Graduate School Form 32), this thesis/dissertation adheres to the provisions of Purdue University’s “Policy -
S1 SUPPORTING INFORMATION Comparative Proteomic Analysis
SUPPORTING INFORMATION Comparative proteomic analysis unveils critical pathways underlying the role of nitrogen fertilizer treatment in American elderberry Bo Yang1, Andrew L. Thomas2, and C. Michael Greenlief 1, † 1Department of Chemistry, University of Missouri, Columbia, Missouri 65211, USA 2Division of Plant Sciences, Southwest Research Center, University of Missouri, Mt. Vernon, Missouri 65712, USA †Corresponding author: C. Michael Greenlief Phone: 573-882-3288; Fax: 573-882-2754; E-mail: [email protected] TABLE OF CONTENTS Figure S1. Scatter graph of relative spots volumes detected on 2-DE gels Figure S2. Representative 2-DE maps of differentially expressed proteins Figure S3. PCA analysis of differentially expressed proteins Figure S4. Mercator protein functional categorization of each genotype Table S1. Statistical analysis of differentially expressed proteins Table S2. Protein report for MALDI-TOF/TOF Table S3. Protein report for LC-MS/MS Table S4. Identification of altered proteins after 56 kg N/ha treatment Table S5. Identification of altered proteins after 112 kg N/ha treatment Table S6. Identification of altered proteins after 169 kg N/ha treatment S1 Figure S1. Scatter graph based on the ratios of relative spots volumes detected in the master gel (y-axis) and the respective replicates (x-axis). (A-D): 0, 56, 112 and 169 kg N/ha treated Adams II. (E-H): 0, 56, 112 and 169 kg N/ha treated Bob Gordon. (I-L): 0, 56, 112 and 169 kg N/ha treated Wyldewood. A B C S2 D E F G S3 H I J K S4 L S5 Figure S2. Representative 2-DE maps of proteins extracted from American elderberry leaves. -
Identification of QTL for Resistance Against Two Fungal Pathogens, Pyrenophora Teres F
Fluturë Novakazi Institut für Resistenzforschung und Stresstoleranz Identification of QTL for resistance against two fungal pathogens, Pyrenophora teres f. teres and Bipolaris sorokiniana, in a barley (Hordeum vulgare L.) diversity set Dissertationen aus dem Julius Kühn-Institut Julius Kühn-Institut Bundesforschungsinstitut für Kulturpflanzen Kontakt | Contact: Fluturë Novakazi Beethovenstraße 24 18069 Rostock Die Schriftenreihe ,,Dissertationen aus dem Julius Kühn-lnstitut“ veröffentlicht Doktorarbeiten, die in enger Zusammenarbeit mit Universitäten an lnstituten des Julius Kühn-lnstituts entstan- den sind. The publication series „Dissertationen aus dem Julius Kühn-lnstitut“ publishes doctoral disser- tations originating from research doctorates and completed at the Julius Kühn-Institut (JKI) either in close collaboration with universities or as an outstanding independent work in the JKI research fields. Der Vertrieb dieser Monographien erfolgt über den Buchhandel (Nachweis im Verzeichnis liefer- barer Bücher - VLB) und OPEN ACCESS unter: https://www.openagrar.de/receive/openagrar_mods_00005667 The monographs are distributed through the book trade (listed in German Books in Print - VLB) and OPEN ACCESS here: https://www.openagrar.de/receive/openagrar_mods_00005667 Wir unterstützen den offenen Zugang zu wissenschaftlichem Wissen. Die Dissertationen aus dem Julius Kühn-lnstitut erscheinen daher OPEN ACCESS. Alle Ausgaben stehen kostenfrei im lnternet zur Verfügung: http://www.julius-kuehn.de Bereich Veröffentlichungen. We advocate open access to scientific knowledge. Dissertations from the Julius Kühn-lnstitut are therefore published open access. All issues are available free of charge under http://www.julius-kuehn.de (see Publications). Bibliografische Information der Deutschen Nationalbibliothek Die Deutsche Nationalbibliothek verzeichnet diese Publikation In der Deutschen Nationalbibliografie: detaillierte bibliografische Daten sind im lnternet über http://dnb.d-nb.de abrufbar. -
Transcriptomic Signature of Drought Response in Pearl Millet
www.nature.com/scientificreports OPEN Transcriptomic signature of drought response in pearl millet (Pennisetum glaucum (L.) and Received: 4 September 2017 Accepted: 4 February 2018 development of web-genomic Published: xx xx xxxx resources Sarika Jaiswal1, Tushar J. Antala2, M. K. Mandavia2, Meenu Chopra1, Rahul Singh Jasrotia1, Rukam S. Tomar2, Jashminkumar Kheni2, U. B. Angadi1, M. A. Iquebal1, B. A. Golakia2, Anil Rai1 & Dinesh Kumar1 Pearl millet, (Pennisetum glaucum L.), an efcient (C4) crop of arid/semi-arid regions is known for hardiness. Crop is valuable for bio-fortifcation combating malnutrition and diabetes, higher caloric value and wider climatic resilience. Limited studies are done in pot-based experiments for drought response at gene-expression level, but feld-based experiment mimicking drought by withdrawal of irrigation is still warranted. We report de novo assembly-based transcriptomic signature of drought response induced by irrigation withdrawal in pearl millet. We found 19983 diferentially expressed genes, 7595 transcription factors, gene regulatory network having 45 hub genes controlling drought response. We report 34652 putative markers (4192 simple sequence repeats, 12111 SNPs and 6249 InDels). Study reveals role of purine and tryptophan metabolism in ABA accumulation mediating abiotic response in which MAPK acts as major intracellular signal sensing drought. Results were validated by qPCR of 13 randomly selected genes. We report the frst web-based genomic resource (http://webtom. cabgrid.res.in/pmdtdb/) which can be used for candidate genes-based SNP discovery programs and trait-based association studies. Looking at climatic change, nutritional and pharmaceutical importance of this crop, present investigation has immense value in understanding drought response in feld condition. -
Citrate Synthase Polyclonal Antibody Catalog Number:16131-1-AP Featured Product 45 Publications
For Research Use Only Citrate synthase Polyclonal antibody www.ptglab.com Catalog Number:16131-1-AP Featured Product 45 Publications Catalog Number: GenBank Accession Number: Purification Method: Basic Information 16131-1-AP BC010106 Antigen affinity purification Size: GeneID (NCBI): Recommended Dilutions: 150ul , Concentration: 350 μg/ml by 1431 WB 1:1000-1:8000 Nanodrop and 313 μg/ml by Bradford Full Name: IP 0.5-4.0 ug for IP and 1:500-1:2000 method using BSA as the standard; citrate synthase for WB Source: IHC 1:100-1:400 Calculated MW: IF 1:50-1:500 Rabbit 466 aa, 52 kDa Isotype: Observed MW: IgG 45-50 kDa Immunogen Catalog Number: AG9117 Applications Tested Applications: Positive Controls: IF, IHC, IP, WB,ELISA WB : mouse heart tissue, HeLa cells Cited Applications: IP : mouse heart tissue, IF, IHC, WB IHC : human liver cancer tissue, Species Specificity: human, mouse, rat IF : HepG2 cells, Cited Species: hamster, human, mouse, rat Note-IHC: suggested antigen retrieval with TE buffer pH 9.0; (*) Alternatively, antigen retrieval may be performed with citrate buffer pH 6.0 Citrate synthase (CS), the first and rate-limiting enzyme of the tricarboxylic acid cycle, plays a key role in Background Information regulating energy generation of mitochondrial respiration(PMID:19479947).It belongs to the citrate synthase family. The deduced 466-amino acid protein contains an N-terminal mitochondrial targeting sequence and a motif highly conserved in citrate synthases(PMID:12549038). It can exsit as a dimer(PMID:8749851). Northern blot analysis detected no CS expression in thymus and small intestine(PMID:12549038). -
In Silico Characterization of the Citrate Synthase Family in Mycobacterium Tuberculosis
Turkish Journal of Biochemistry – Türk Biyokimya Dergisi 2016; 41(2): 118–126 Bioinformatics Research Article – 66743 Sezer Okay In silico characterization of the citrate synthase family in Mycobacterium tuberculosis Mycobacterium tuberculosis’te sitrat sentaz ailesinin in silico karakterizasyonu DOI 10.1515/tjb-2016-0019 Conclusion: This comprehensive bioinformatics analysis Received November 13, 2015; accepted January 4, 2016 of CS family in MTB has a contribution to the knowledge of the genetics and physiology of this pathogen. Abstract: Objective: Mycobacterium tuberculosis (MTB) is an obligate aerobe bacterial pathogen. Here, the citrate Keywords: Aerobic respiration, citrate synthase, Myco- synthase (CS) family, an important component of aerobic bacterium tuberculosis, pathogenicity respiration, was investigated in MTB. Methods: MTB genome was analyzed in silico to reveal Özet: Amaç: Mycobacterium tuberculosis (MTB) zorunlu the members of CS family. The nucleotide and amino acid aerop olan bakteriyel bir patojendir. Burada, oksijenli sequences were retrieved from the NCBI database, and solunumun önemli bir bileşeni olan sitrat sentaz (SS) searched for the similarity using the NCBI BLAST tool. ailesi MTB’de incelenmiştir. Sequence alignment and phylogenetic analysis were per- formed using MEGA6. The physicochemical parameters, Metod: SS ailesinin üyelerini belirlemek için MTB genomu cellular localization, HMM profiles, motif structure, 3D in silico analiz edildi. Nükleotit ve aminoasit dizileri NCBI modeling, and the interactions of the proteins were ana- veri tabanından alındı ve benzerlikleri NCBI BLAST ara- lyzed using GPMAW, PSORTb, Pfam and SMART, MEME, cıyla tarandı. Dizi hizalama ve filogenetik analiz MEGA6 Phyre2, and STRING databases, respectively. kullanılarak gerçekleştirildi. Fizikokimyasal parametre- ler, hücresel lokalizasyon, HMM profilleri, motif yapısı, üç Results: The members of CS family in MTB were identified boyutlu modelleme ve diğer proteinlerle etkileşimler sıra- as CitA, GltA2, and PrpC. -
An Integrated Approach of Proteomics and Computational Genetic Modification Effectiveness Analysis to Uncover the Mechanism of Flood Tolerance in Soybeans
International Journal of Molecular Sciences Article An Integrated Approach of Proteomics and Computational Genetic Modification Effectiveness Analysis to Uncover the Mechanism of Flood Tolerance in Soybeans Xin Wang 1,2, Katsumi Sakata 3,* and Setsuko Komatsu 1,2,* 1 Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba 305-8572, Japan; [email protected] 2 National Institute of Crop Science, National Agriculture and Food Research Organization, Tsukuba 305-8518, Japan 3 Department of Life Science and Informatics, Maebashi Institute of Technology, Maebashi 371-0816, Japan * Correspondence: [email protected] (K.S.); [email protected] (S.K.) Received: 9 March 2018; Accepted: 22 April 2018; Published: 26 April 2018 Abstract: Flooding negatively affects the growth of soybeans. Recently, omic approaches have been used to study abiotic stress responses in plants. To explore flood-tolerant genes in soybeans, an integrated approach of proteomics and computational genetic modification effectiveness analysis was applied to the soybean (Glycine max L. (Merrill)). Flood-tolerant mutant and abscisic acid (ABA)-treated soybean plants were used as the flood-tolerant materials. Among the primary metabolism, glycolysis, fermentation, and tricarboxylic acid cycle were markedly affected under flooding. Fifteen proteins, which were related to the affected processes, displayed similar protein profiles in the mutant and ABA-treated soybean plants. Protein levels of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), aconitase 1, and 2-oxoglutarate dehydrogenase were higher in flood-tolerant materials than in wild-type soybean plants under flood conditions. These three proteins were positioned in each of the three enzyme groups revealed by our computational genetic modification effectiveness analysis, and the three proteins configured a candidate set of genes to promote flood tolerance. -
The Apricot (Prunus Armeniaca L.) Genome Elucidates Rosaceae
Jiang et al. Horticulture Research (2019) 6:128 Horticulture Research https://doi.org/10.1038/s41438-019-0215-6 www.nature.com/hortres ARTICLE Open Access The apricot (Prunus armeniaca L.) genome elucidates Rosaceae evolution and beta-carotenoid synthesis Fengchao Jiang1,2,JunhuanZhang1,2,SenWang3,LiYang1,2, Yingfeng Luo3, Shenghan Gao3, Meiling Zhang1,2, Shuangyang Wu3, Songnian Hu3, Haoyuan Sun1,2 and Yuzhu Wang1,2 Abstract Apricots, scientifically known as Prunus armeniaca L, are drupes that resemble and are closely related to peaches or plums. As one of the top consumed fruits, apricots are widely grown worldwide except in Antarctica. A high-quality reference genome for apricot is still unavailable, which has become a handicap that has dramatically limited the elucidation of the associations of phenotypes with the genetic background, evolutionary diversity, and population diversity in apricot. DNA from P. armeniaca was used to generate a standard, size-selected library with an average DNA fragment size of ~20 kb. The library was run on Sequel SMRT Cells, generating a total of 16.54 Gb of PacBio subreads (N50 = 13.55 kb). The high-quality P. armeniaca reference genome presented here was assembled using long-read single-molecule sequencing at approximately 70× coverage and 171× Illumina reads (40.46 Gb), combined with a genetic map for chromosome scaffolding. The assembled genome size was 221.9 Mb, with a contig NG50 size of 1.02 Mb. Scaffolds covering 92.88% of the assembled genome were anchored on eight chromosomes. Benchmarking Universal Single-Copy Orthologs analysis showed 98.0% complete genes. We predicted 30,436 protein-coding genes, 1234567890():,; 1234567890():,; 1234567890():,; 1234567890():,; and 38.28% of the genome was predicted to be repetitive. -
1A59 Lichtarge Lab 2006
Pages 1–8 1a59 Evolutionary trace report by report maker August 8, 2010 4.3.3 DSSP 7 4.3.4 HSSP 7 4.3.5 LaTex 7 4.3.6 Muscle 7 4.3.7 Pymol 8 4.4 Note about ET Viewer 8 4.5 Citing this work 8 4.6 About report maker 8 4.7 Attachments 8 1 INTRODUCTION From the original Protein Data Bank entry (PDB id 1a59): Title: Cold-active citrate synthase Compound: Mol id: 1; molecule: citrate synthase; chain: a; engineered: yes Organism, scientific name: Antarctic Bacterium Ds2-3r; 1a59 contains a single unique chain 1a59A (377 residues long). 2 CHAIN 1A59A 2.1 O34002 overview From SwissProt, id O34002, 100% identical to 1a59A: CONTENTS Description: Citrate synthase (EC 2.3.3.1). 1 Introduction 1 Organism, scientific name: Antarctic bacterium DS2-3R. Taxonomy: Bacteria. 2 Chain 1a59A 1 Catalytic activity: Acetyl-CoA + H(2)O + oxaloacetate = citrate + 2.1 O34002 overview 1 CoA. 2.2 Multiple sequence alignment for 1a59A 1 Biophysicochemical properties: 2.3 Residue ranking in 1a59A 1 Temperature dependence: Optimum temperature is 31 degrees Cel- 2.4 Top ranking residues in 1a59A and their position on sius. Cold-active. Is rapidly inactivated at 45 degrees Celsius, and the structure 2 shows significant activity at 10 degrees Celsius and below; 2.4.1 Clustering of residues at 25% coverage. 2 Pathway: Tricarboxylic acid cycle. 2.4.2 Overlap with known functional surfaces at Subunit: Homodimer. 25% coverage. 2 Miscellaneous: Citrate synthase is found in nearly all cells capable of oxidative metabolism. -
1471-2164-6-174-S4.PDF (299.1Kb)
Sup_Table_2. Comparison of the whole genomes in Fig. 3A. Segment 1- Conserved in Bm, Bp, and Bt to Bp to Bt Gene Description % length % identity % length % identity BMA0001 chromosomal replication initiator protein DnaA 100 99 100 96 BMA0002 DNA polymerase III, beta subunit 100 100 100 99 BMA0003 DNA gyrase, B subunit 100 100 100 99 BMA0006 carboxymuconolactone decarboxylase family protein 100 98 100 99 BMA0010 hypothetical protein 100 99 100 92 BMA0011 hypothetical protein 100 100 100 91 BMA0014.1 hypothetical protein 100 99 96 94 BMA0018 hypothetical protein 100 99 100 95 BMA0019 FHA domain protein 100 100 100 94 BMA0020 protein kinase domain protein 100 99 100 90 BMA0023 conserved hypothetical protein 100 99 100 90 BMA0024 aldolase, class II 100 98 100 91 BMA0027 polysaccharide biosynthesis family protein 100 100 100 96 BMA0028 glycosyl transferase, group 1 family protein 100 99 100 94 BMA0029 mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase 100 99 100 92 BMA0030 ElaA family protein 100 99 100 90 BMA0032 glycosyl transferase, group 1 family protein 100 99 100 93 BMA0037 sigma-54 dependent transcriptional regulator 100 99 100 97 BMA0039 beta-mannosidase-related protein 100 99 100 91 BMA0040 conserved hypothetical protein 100 100 100 94 BMA0041 conserved hypothetical protein 100 99 100 95 BMA0042 acyl-CoA dehydrogenase domain protein 100 99 100 96 BMA0043 acyl carrier protein, putative 100 100 100 95 BMA0044 conserved hypothetical protein 100 99 100 96 BMA0045 conserved hypothetical protein 100 100 100 98 BMA0046 -
IDENTIFICAÇÃO DE Micrornas ENVOLVIDOS NO DESENVOLVIMENTO DE SEMENTES DE GLYCINE MAX (L.)
IDENTIFICAÇÃO DE microRNAs ENVOLVIDOS NO DESENVOLVIMENTO DE SEMENTES DE GLYCINE MAX (L.) MERRILL PAULA MACHADO DE ARAÚJO UNIVERSIDADE ESTADUAL DO NORTE FLUMINENSE DARCY RIBEIRO Campos dos Goytacazes, RJ Fevereiro de 2020 IDENTIFICAÇÃO DE microRNAs ENVOLVIDOS NO DESENVOLVIMENTO DE SEMENTES DE GLYCINE MAX (L.) MERRILL PAULA MACHADO DE ARAÚJO Dissertação apresentada ao Centro de Biociências e Biotecnologia da Universidade Estadual do Norte Fluminense Darcy Ribeiro, como parte das exigências para obtenção do título de Mestre em Biociências e Biotecnologia. Orientadora: Profa. Dra. Clícia Grativol Gaspar de Matos UNIVERSIDADE ESTADUAL DO NORTE FLUMINENSE DARCY RIBEIRO Campos dos Goytacazes, RJ Fevereiro de 2020 ii IDENTIFICAÇÃO DE microRNAsENVOLVIDOS NO DESENVOLVIMENTO DE SEMENTES DE GLYCINE MAX (L.) MERRILL PAULA MACHADO DE ARAÚJO Dissertação apresentada ao Centro de Biociências e Biotecnologia da Universidade Estadual do Norte Fluminense Darcy Ribeiro, como parte das exigências para obtenção do título de Mestre em Biociências e Biotecnologia. Aprovada em de fevereiro de 2020. Comissão Examinadora: Douglas Silva omtngles (DSc., Biotecnologia)— UNESP Claudete ta-Catarina DSc., Biotecnologia)— UENF Kátia Valevski Sales Femandes (PhD, Bioquímica e Biologia Molecularde Plantas)- UENF Clícia GrativolGaspar de atos (DSc., Química Biológica)- UENF (Orientadora) iii FICHA CATALOGRÁFICA UENF - Bibliotecas Elaborada com os dados fornecidos pela autora. A663 Araújo, Paula Machado de. Identificação de microRNAs envolvidos no desenvolvimento de sementes de Glycine max (L.) Merrill. / Paula Machado de Araújo. - Campos dos Goytacazes, RJ, 2020. 72 f. : il. Inclui bibliografia. Dissertação (Mestrado em Biociências e Biotecnologia) - Universidade Estadual do Norte Fluminense Darcy Ribeiro, Centro de Biociências e Biotecnologia, 2020. Orientadora: Clicia Grativol Gaspar. 1. microRNAs. 2. embriogênese de sementes. -
1Cts Lichtarge Lab 2006
Pages 1–7 1cts Evolutionary trace report by report maker July 3, 2009 4.3.3 DSSP 6 4.3.4 HSSP 6 4.3.5 LaTex 6 4.3.6 Muscle 6 4.3.7 Pymol 6 4.4 Note about ET Viewer 7 4.5 Citing this work 7 4.6 About report maker 7 4.7 Attachments 7 1 INTRODUCTION From the original Protein Data Bank entry (PDB id 1cts): Title: Crystallographic refinement and atomic models of two diffe- rent forms of citrate synthase at 2.7 and 1.7 angstroms resolution Compound: Mol id: 1; molecule: citrate synthase; chain: a; ec: 4.1.3.7; engineered: yes Organism, scientific name: Sus Scrofa 1cts contains a single unique chain 1ctsA (437 residues long). 2 CHAIN 1CTSA 2.1 P00889 overview CONTENTS From SwissProt, id P00889, 100% identical to 1ctsA: 1 Introduction 1 Description: Citrate synthase, mitochondrial precursor (EC 2.3.3.1). Organism, scientific name: Sus scrofa (Pig). 2 Chain 1ctsA 1 Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 2.1 P00889 overview 1 Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; 2.2 Multiple sequence alignment for 1ctsA 1 Suina; Suidae; Sus. 2.3 Residue ranking in 1ctsA 1 Catalytic activity: Acetyl-CoA + H(2)O + oxaloacetate = citrate + 2.4 Top ranking residues in 1ctsA and their position on CoA. the structure 1 Pathway: Tricarboxylic acid cycle. 2.4.1 Clustering of residues at 25% coverage. 1 Subunit: Homodimer. 2.4.2 Overlap with known functional surfaces at Subcellular location: Mitochondrial matrix. 25% coverage. 2 Miscellaneous: Citrate synthase is found in nearly all cells capable of oxidative metabolism.