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A Novel 65-Bp Indel in the GOLGB1 Gene Is Associated with Chicken Growth and Carcass Traits
animals Article A Novel 65-bp Indel in the GOLGB1 Gene Is Associated with Chicken Growth and Carcass Traits Rong Fu 1,2, Tuanhui Ren 1,2, Wangyu Li 1,2, Jiaying Liang 1,2, Guodong Mo 1,2, Wen Luo 1,2, Danlin He 1,2, Shaodong Liang 1,2 and Xiquan Zhang 1,2,* 1 Department of Animal Genetics, Breeding and Reproduction, College of Animal Science, South China Agricultural University, Guangzhou 510642, China; [email protected] (R.F.); [email protected] (T.R.); [email protected] (W.L.); [email protected] (J.L.); [email protected] (G.M.); [email protected] (W.L.); [email protected] (D.H.); [email protected] (S.L.) 2 Guangdong Provincial Key Lab of Agro-Animal Genomics and Molecular Breeding, and Key Laboratory of Chicken Genetics, Breeding and Reproduction, Ministry of Agriculture, Guangzhou 510642, China * Correspondence: [email protected] Received: 20 February 2020; Accepted: 4 March 2020; Published: 12 March 2020 Simple Summary: Many Chinese-local chickens show slow-growing and low-producing performance, which is not conductive to the development of the poultry industry. The identification of thousands of indels in the last twenty years has helped us to make progress in animal genetics and breeding. Golgin subfamily B member 1 (GOLGB1) is located on chromosome 1 in chickens. Previous study showed that a large number of QTLs on the chicken chromosome 1 were related to the important economic traits. However, the biological function of GOLGB1 gene in chickens is still unclear. In this study, we detected a novel 65-bp indel in the fifth intron of the chicken GOLGB1 gene. -
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Barlow et al. BMC Biology (2018) 16:27 https://doi.org/10.1186/s12915-018-0492-9 RESEARCHARTICLE Open Access A sophisticated, differentiated Golgi in the ancestor of eukaryotes Lael D. Barlow1, Eva Nývltová2,3, Maria Aguilar1, Jan Tachezy2 and Joel B. Dacks1,4* Abstract Background: The Golgi apparatus is a central meeting point for the endocytic and exocytic systems in eukaryotic cells, and the organelle’s dysfunction results in human disease. Its characteristic morphology of multiple differentiated compartments organized into stacked flattened cisternae is one of the most recognizable features of modern eukaryotic cells, and yet how this is maintained is not well understood. The Golgi is also an ancient aspect of eukaryotes, but the extent and nature of its complexity in the ancestor of eukaryotes is unclear. Various proteins have roles in organizing the Golgi, chief among them being the golgins. Results: We address Golgi evolution by analyzing genome sequences from organisms which have lost stacked cisternae as a feature of their Golgi and those that have not. Using genomics and immunomicroscopy, we first identify Golgi in the anaerobic amoeba Mastigamoeba balamuthi. We then searched 87 genomes spanning eukaryotic diversity for presence of the most prominent proteins implicated in Golgi structure, focusing on golgins. We show some candidates as animal specific and others as ancestral to eukaryotes. Conclusions: None of the proteins examined show a phyletic distribution that correlates with the morphology of stacked cisternae, suggesting the possibility of stacking as an emergent property. Strikingly, however, the combination of golgins conserved among diverse eukaryotes allows for the most detailed reconstruction of the organelle to date, showing a sophisticated Golgi with differentiated compartments and trafficking pathways in the common eukaryotic ancestor. -
Human OMG Blocking Peptide (CDBP2120) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Human OMG blocking peptide (CDBP2120) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Product Overview Blocking/Immunizing peptide for anti-OMG antibody Antigen Description OMG (oligodendrocyte myelin glycoprotein) is a protein-coding gene. Diseases associated with OMG include patulous eustachian tube, and internuclear ophthalmoplegia, and among its related super-pathways are p75NTR regulates axonogenesis and Development MAG-dependent inhibition of neurite outgrowth. GO annotations related to this gene include identical protein binding. Nature Synthetic Expression System N/A Species Human Species Reactivity Human Conjugate Unconjugated Applications Apuri, BL, ELISA Procedure None Format Lyophilized powder Size 100 μg Preservative None Storage Shipped at ambient temperature, store at -20°C. ANTIGEN GENE INFORMATION Gene Name OMG oligodendrocyte myelin glycoprotein [ Homo sapiens ] Official Symbol OMG Synonyms OMG; oligodendrocyte myelin glycoprotein; oligodendrocyte-myelin glycoprotein; OMGP; Entrez Gene ID 4974 mRNA Refseq NM_002544 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Protein Refseq NP_002535 UniProt ID P23515 Chromosome Location 17q11-q12 Pathway Axonal growth inhibition (RHOA activation), organism-specific biosystem; Signal Transduction, organism-specific biosystem; Signalling by NGF, organism-specific biosystem; p75 NTR receptor-mediated signalling, organism-specific biosystem; p75(NTR)-mediated signaling, organism-specific biosystem; p75NTR regulates axonogenesis, organism-specific biosystem; Function identical protein binding; 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 2 © Creative Diagnostics All Rights Reserved. -
Knock-Out of ACBD3 Leads to Dispersed Golgi Structure, but Unaffected Mitochondrial Functions in HEK293 and Hela Cells
International Journal of Molecular Sciences Article Knock-Out of ACBD3 Leads to Dispersed Golgi Structure, but Unaffected Mitochondrial Functions in HEK293 and HeLa Cells Tereza Da ˇnhelovská 1 , Lucie Zdražilová 1 , Hana Štufková 1, Marie Vanišová 1, Nikol Volfová 1, Jana Kˇrížová 1 , OndˇrejKuda 2 , Jana Sládková 1 and Markéta Tesaˇrová 1,* 1 Department of Paediatrics and Inherited Metabolic Disorders, Charles University, First Faculty of Medicine and General University Hospital in Prague, 128 01 Prague, Czech Republic; [email protected] (T.D.); [email protected] (L.Z.); [email protected] (H.Š.); [email protected] (M.V.); [email protected] (N.V.); [email protected] (J.K.); [email protected] (J.S.) 2 Institute of Physiology, Academy of Sciences of the Czech Republic, 142 00 Prague, Czech Republic; [email protected] * Correspondence: [email protected] Abstract: The Acyl-CoA-binding domain-containing protein (ACBD3) plays multiple roles across the cell. Although generally associated with the Golgi apparatus, it operates also in mitochondria. In steroidogenic cells, ACBD3 is an important part of a multiprotein complex transporting cholesterol into mitochondria. Balance in mitochondrial cholesterol is essential for proper mitochondrial protein biosynthesis, among others. We generated ACBD3 knock-out (ACBD3-KO) HEK293 and HeLa cells and characterized the impact of protein absence on mitochondria, Golgi, and lipid profile. In ACBD3- Citation: Daˇnhelovská,T.; KO cells, cholesterol level and mitochondrial structure and functions are not altered, demonstrating Zdražilová, L.; Štufková, H.; that an alternative pathway of cholesterol transport into mitochondria exists. However, ACBD3- Vanišová, M.; Volfová, N.; Kˇrížová,J.; Kuda, O.; Sládková, J.; Tesaˇrová,M. -
Signal Peptide Peptidase‐Like 2C Impairs Vesicular Transport And
Article Signal peptide peptidase-like 2c impairs vesicular transport and cleaves SNARE proteins Alkmini A Papadopoulou1, Stephan A Müller2, Torben Mentrup3, Merav D Shmueli2,4,5, Johannes Niemeyer3, Martina Haug-Kröper1, Julia von Blume6, Artur Mayerhofer7, Regina Feederle2,8,9 , Bernd Schröder3,10 , Stefan F Lichtenthaler2,5,9 & Regina Fluhrer1,2,* Abstract Introduction Members of the GxGD-type intramembrane aspartyl proteases The high degree of compartmentalization in eukaryotic cells creates have emerged as key players not only in fundamental cellular a need for specific and precise protein trafficking. To meet this need, processes such as B-cell development or protein glycosylation, but cells have developed a complex system of vesicle transport that also in development of pathologies, such as Alzheimer’s disease or ensures safe sorting of cargo proteins, in particular between the dif- hepatitis virus infections. However, one member of this protease ferent compartments of the secretory pathway [1–3]. Vesicles origi- family, signal peptide peptidase-like 2c (SPPL2c), remains orphan nate from a donor membrane, translocate in a targeted manner, and and its capability of proteolysis as well as its physiological function get specifically tethered to the target membrane, before fusing with is still enigmatic. Here, we demonstrate that SPPL2c is catalytically it. Soluble N-ethylmaleimide-sensitive factor attachment protein active and identify a variety of SPPL2c candidate substrates using receptor (SNARE) proteins are known since three decades to medi- proteomics. The majority of the SPPL2c candidate substrates clus- ate specific membrane fusion [4,5]. So far, 38 SNARE proteins have ter to the biological process of vesicular trafficking. -
CALIFORNIA STATE UNIVERSITY, NORTHRIDGE Bioinformatic
CALIFORNIA STATE UNIVERSITY, NORTHRIDGE Bioinformatic Comparison of the EVI2A Promoter and Coding Regions A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science in Biology By Max Weinstein May 2020 The thesis of Max Weinstein is approved: Professor Rheem D. Medh Date Professor Virginia Oberholzer Vandergon Date Professor Cindy Malone, Chair Date California State University Northridge ii Table of Contents Signature Page ii List of Figures v Abstract vi Introduction 1 Ecotropic Viral Integration Site 2A, a Gene within a Gene 7 Materials and Methods 11 PCR and Cloning of Recombinant Plasmid 11 Transformation and Cell Culture 13 Generation of Deletion Constructs 15 Transfection and Luciferase Assay 16 Identification of Transcription Factor Binding Sites 17 Determination of Region for Analysis 17 Multiple Sequence Alignment (MSA) 17 Model Testing 18 Tree Construction 18 Promoter and CDS Conserved Motif Search 19 Results and Discussion 20 Choice of Species for Analysis 20 Mapping of Potential Transcription Factor Binding Sites 20 Confirmation of Plasmid Generation through Gel Electrophoresis 21 Analysis of Deletion Constructs by Transient Transfection 22 EVI2A Coding DNA Sequence Phylogenetics 23 EVI2A Promoter Phylogenetics 23 EVI2A Conserved Leucine Zipper 25 iii EVI2A Conserved Casein kinase II phosphorylation site 26 EVI2A Conserved Sox-5 Binding Site 26 EVI2A Conserved HLF Binding Site 27 EVI2A Conserved cREL Binding Site 28 EVI2A Conserved CREB Binding Site 28 Summary 29 Appendix: Figures 30 Literature Cited 44 iv List of Figures Figure 1. EVI2A is nested within the gene NF1 30 Figure 2 Putative Transcriptions Start Site 31 Figure 3. Gel Electrophoresis of pGC Blue cloned, Restriction Digested Plasmid 32 Figure 4. -
The Murine Orthologue of the Golgi-Localized TPTE Protein Provides Clues to the Evolutionary History of the Human TPTE Gene Family
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by RERO DOC Digital Library Hum Genet (2001) 109:569–575 DOI 10.1007/s004390100607 ORIGINAL INVESTIGATION Michel Guipponi · Caroline Tapparel · Olivier Jousson · Nathalie Scamuffa · Christophe Mas · Colette Rossier · Pierre Hutter · Paolo Meda · Robert Lyle · Alexandre Reymond · Stylianos E. Antonarakis The murine orthologue of the Golgi-localized TPTE protein provides clues to the evolutionary history of the human TPTE gene family Received: 5 June 2001 / Accepted: 17 August 2001 / Published online: 27 October 2001 © Springer-Verlag 2001 Abstract The human TPTE gene encodes a testis-spe- events. The Y chromosome copy of TPTE is a pseudo- cific protein that contains four potential transmembrane gene and is not therefore involved in the testis expression domains and a protein tyrosine phosphatase motif, and of this gene family. shows homology to the tumor suppressor PTEN/MMAC1. Chromosomal mapping revealed multiple copies of the TPTE gene present on the acrocentric chromosomes 13, Introduction 15, 21 and 22, and the Y chromosome. Zooblot analysis suggests that mice may possess only one copy of TPTE. We have recently identified a testis-specific cDNA, TPTE In the present study, we report the isolation and initial (Transmembrane Phosphatase with TEnsin homology), characterization of the full-length cDNA of the mouse ho- that encodes a predicted protein of 551 amino acids con- mologue Tpte. At least three different mRNA transcripts taining four potential transmembrane domains and a tyro- (Tpte.a, b, c) are produced via alternative splicing, encod- sine phosphatase motif (Chen H et al. -
Behavioral and Other Phenotypes in a Cytoplasmic Dynein Light Intermediate Chain 1 Mutant Mouse
The Journal of Neuroscience, April 6, 2011 • 31(14):5483–5494 • 5483 Cellular/Molecular Behavioral and Other Phenotypes in a Cytoplasmic Dynein Light Intermediate Chain 1 Mutant Mouse Gareth T. Banks,1* Matilda A. Haas,5* Samantha Line,6 Hazel L. Shepherd,6 Mona AlQatari,7 Sammy Stewart,7 Ida Rishal,8 Amelia Philpott,9 Bernadett Kalmar,2 Anna Kuta,1 Michael Groves,3 Nicholas Parkinson,1 Abraham Acevedo-Arozena,10 Sebastian Brandner,3,4 David Bannerman,6 Linda Greensmith,2,4 Majid Hafezparast,9 Martin Koltzenburg,2,4,7 Robert Deacon,6 Mike Fainzilber,8 and Elizabeth M. C. Fisher1,4 1Department of Neurodegenerative Disease, 2Sobell Department of Motor Science and Movement Disorders, 3Division of Neuropathology, and 4Medical Research Council (MRC) Centre for Neuromuscular Diseases, University College London (UCL) Institute of Neurology, London WC1N 3BG, United Kingdom, 5MRC National Institute for Medical Research, London NW7 1AA, United Kingdom, 6Department of Experimental Psychology, University of Oxford, Oxford OX1 3UD, United Kingdom, 7UCL Institute of Child Health, London WC1N 1EH, United Kingdom, 8Department of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel, 9School of Life Sciences, University of Sussex, Brighton BN1 9QG, United Kingdom, and 10MRC Mammalian Genetics Unit, Harwell OX11 ORD, United Kingdom The cytoplasmic dynein complex is fundamentally important to all eukaryotic cells for transporting a variety of essential cargoes along microtubules within the cell. This complex also plays more specialized roles in neurons. The complex consists of 11 types of protein that interact with each other and with external adaptors, regulators and cargoes. Despite the importance of the cytoplasmic dynein complex, weknowcomparativelylittleoftherolesofeachcomponentprotein,andinmammalsfewmutantsexistthatallowustoexploretheeffects of defects in dynein-controlled processes in the context of the whole organism. -
Multifaceted Polo-Like Kinases: Drug Targets and Antitargets for Cancer Therapy
REVIEWS Multifaceted polo-like kinases: drug targets and antitargets for cancer therapy Klaus Strebhardt Abstract | The polo-like kinase 1 (PLK1) acts in concert with cyclin-dependent kinase 1–cyclin B1 and Aurora kinases to orchestrate a wide range of critical cell cycle events. Because PLK1 has been preclinically validated as a cancer target, small-molecule inhibitors of PLK1 have become attractive candidates for anticancer drug development. Although the roles of the closely related PLK2, PLK3 and PLK4 in cancer are less well understood, there is evidence showing that PLK2 and PLK3 act as tumour suppressors through their functions in the p53 signalling network, which guards the cell against various stress signals. In this article, recent insights into the biology of PLKs will be reviewed, with an emphasis on their role in malignant transformation, and progress in the development of small-molecule PLK1 inhibitors will be examined. More than two decades ago polo, the founding member Early observations on the overexpression of PLK1 of the family of polo-like kinases (PLKs), was identified in human tumours12 and on the inhibition of cellu- as having an essential role in the ordered execution of lar proliferation by microinjecting antibodies against mitotic events in Drosophila melanogaster 1,2. Since the PLK1 into HeLa cells13 initiated a series of follow-on discovery of polo, a wealth of functional information on studies using a broad spectrum of inhibitors (for exam- PLKs has been collected in a wide phylogenetic space. ple, dominant-negative forms of PLK1, antisense oli- Five mammalian PLK family members have been iden- gonucleotides and small interfering RNAs) aiming to tified so far, PLK1 (also known as STPK13), PLK2 (also evaluate PLK1 as a potential target for the treatment known as SNK), PLK3 (also known as CNK, FNK and of cancer14–17. -
Discoveryspace: an Interactive Data Analysis Application
Open Access Software2007RobertsonetVolume al. 8, Issue 1, Article R6 DiscoverySpace: an interactive data analysis application comment Neil Robertson, Mehrdad Oveisi-Fordorei, Scott D Zuyderduyn, Richard J Varhol, Christopher Fjell, Marco Marra, Steven Jones and Asim Siddiqui Address: Canada's Michael Smith Genome Sciences Centre, British Columbia Cancer Research Centre (BCCRC), British Columbia Cancer Agency (BCCA), Vancouver, BC, Canada. reviews Correspondence: Neil Robertson. Email: [email protected]. Mehrdad Oveisi-Fordorei. Email: [email protected]. Asim Siddiqui. Email: [email protected] Published: 08 January 2007 Received: 24 March 2006 Revised: 4 July 2006 Genome Biology 2007, 8:R6 (doi:10.1186/gb-2007-8-1-r6) Accepted: 8 January 2007 The electronic version of this article is the complete one and can be found online at http://genomebiology.com/2007/8/1/R6 reports © 2007 Robertson et al.; licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Interactive<p>DiscoverySpace, data analysis a graphical application for bioinformatics data analysis, in particular analysis of SAGE data, is described</p> deposited research Abstract DiscoverySpace is a graphical application for bioinformatics data analysis. Users can seamlessly traverse references between biological databases and draw together annotations in an intuitive tabular interface. Datasets can be compared using a suite of novel tools to aid in the identification of significant patterns. DiscoverySpace is of broad utility and its particular strength is in the analysis of serial analysis of gene expression (SAGE) data. -
Datasheet: MCA3923Z Product Details
Datasheet: MCA3923Z Description: MOUSE ANTI HUMAN ACBD3:Preservative Free Specificity: ACBD3 Format: Preservative Free Product Type: Monoclonal Antibody Clone: 2G2 Isotype: IgG1 Quantity: 0.1 mg Product Details Applications This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit www.bio-rad-antibodies.com/protocols. Yes No Not Determined Suggested Dilution Immunohistology - Paraffin (1) 0.1 - 10 ug/ml Western Blotting Immunofluorescence 0.1 - 10 ug/ml Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls. (1)This product requires antigen retrieval using heat treatment prior to staining of paraffin sections.Sodium citrate buffer pH 6.0 is recommended for this purpose. Target Species Human Species Cross Reacts with: Rat, Mouse Reactivity N.B. Antibody reactivity and working conditions may vary between species. Product Form Purified IgG - liquid Preparation Purified IgG prepared by affinity chromatography on Protein A Buffer Solution Phosphate buffered saline Preservative None present Stabilisers Approx. Protein Ig concentration 0.5 mg/ml Concentrations Immunogen Recombinant protein corresponding to aa 73-172 of human ACBD3 Page 1 of 3 External Database Links UniProt: Q9H3P7 Related reagents Entrez Gene: 64746 ACBD3 Related reagents Synonyms GCP60, GOCAP1, GOLPH1 Fusion Partners Spleen cells from immunised Balb/c mice were fused with cells from the Sp2/0 myeloma cell line. -
In This Table Protein Name, Uniprot Code, Gene Name P-Value
Supplementary Table S1: In this table protein name, uniprot code, gene name p-value and Fold change (FC) for each comparison are shown, for 299 of the 301 significantly regulated proteins found in both comparisons (p-value<0.01, fold change (FC) >+/-0.37) ALS versus control and FTLD-U versus control. Two uncharacterized proteins have been excluded from this list Protein name Uniprot Gene name p value FC FTLD-U p value FC ALS FTLD-U ALS Cytochrome b-c1 complex P14927 UQCRB 1.534E-03 -1.591E+00 6.005E-04 -1.639E+00 subunit 7 NADH dehydrogenase O95182 NDUFA7 4.127E-04 -9.471E-01 3.467E-05 -1.643E+00 [ubiquinone] 1 alpha subcomplex subunit 7 NADH dehydrogenase O43678 NDUFA2 3.230E-04 -9.145E-01 2.113E-04 -1.450E+00 [ubiquinone] 1 alpha subcomplex subunit 2 NADH dehydrogenase O43920 NDUFS5 1.769E-04 -8.829E-01 3.235E-05 -1.007E+00 [ubiquinone] iron-sulfur protein 5 ARF GTPase-activating A0A0C4DGN6 GIT1 1.306E-03 -8.810E-01 1.115E-03 -7.228E-01 protein GIT1 Methylglutaconyl-CoA Q13825 AUH 6.097E-04 -7.666E-01 5.619E-06 -1.178E+00 hydratase, mitochondrial ADP/ATP translocase 1 P12235 SLC25A4 6.068E-03 -6.095E-01 3.595E-04 -1.011E+00 MIC J3QTA6 CHCHD6 1.090E-04 -5.913E-01 2.124E-03 -5.948E-01 MIC J3QTA6 CHCHD6 1.090E-04 -5.913E-01 2.124E-03 -5.948E-01 Protein kinase C and casein Q9BY11 PACSIN1 3.837E-03 -5.863E-01 3.680E-06 -1.824E+00 kinase substrate in neurons protein 1 Tubulin polymerization- O94811 TPPP 6.466E-03 -5.755E-01 6.943E-06 -1.169E+00 promoting protein MIC C9JRZ6 CHCHD3 2.912E-02 -6.187E-01 2.195E-03 -9.781E-01 Mitochondrial 2-