• Login
    View Item 
    •   Home
    • University Colleges
    • SUNY Brockport
    • Theses
    • Biology Master’s Theses
    • View Item
    •   Home
    • University Colleges
    • SUNY Brockport
    • Theses
    • Biology Master’s Theses
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of SUNY Open Access RepositoryCommunitiesPublication DateAuthorsTitlesSubjectsDepartmentThis CollectionPublication DateAuthorsTitlesSubjectsDepartmentAuthor ProfilesView

    My Account

    LoginRegister

    Campus Communities in SOAR

    Alfred State CollegeBrockportBroomeCantonDownstateEmpireFashion Institute of TechnologyFredoniaMaritimeNew PaltzOneontaOptometryOswegoPlattsburghSUNY Polytechnic InstituteSUNY PressUpstate Medical

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Arginine Methylation and Enzymatic Activity of TbLpn, a Lipin Homologue from T. Brucei

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    bio_theses/23/fulltext (1).pdf
    Size:
    1.568Mb
    Format:
    PDF
    Download
    Average rating
     
       votes
    Cast your vote
    You can rate an item by clicking the amount of stars they wish to award to this item. When enough users have cast their vote on this item, the average rating will also be shown.
    Star rating
     
    Your vote was cast
    Thank you for your feedback
    Author
    Bumstead, Andrew R.
    Keyword
    Trypanosoma Brucei
    Protein Arginine Methylation
    TbLpn
    Lipins
    Date Published
    2016-07-21
    
    Metadata
    Show full item record
    URI
    http://hdl.handle.net/20.500.12648/4490
    Abstract
    Trypanosoma brucei is a flagellated protozoan parasite responsible for African Trypanosomiasis. T. brucei is a deadly immune-evasive parasite which circulates the bloodstream of mammalian hosts and requires the Tsetse fly as a transmission vector. The parasite is capable of antigenic variation which allows it to change its glycoprotein coat in order to escape immune detection. Of great concern is the parasite’s growing resistance to various chemotherapeutic treatments which may allow for reemergence. Protein-arginine methyltransferases (PRMTs) are a group of proteins responsible for transferring methyl groups to arginine residues within proteins. Protein methylation causes epigenetic modification of histones or changes in protein-protein interactions which, in turn, leads to the regulation of a variety of biological functions including, but not limited to: transcriptional/translational activation or repression, signal transduction, protein localization, and cell differentiation. Several PRMTs have been discovered in T. brucei including TbPRMT1, TbPRMT3, TbPRMT5, TbPRMT6 and TbPRMT7. TbLpn, a lipin family protein, was discovered based on its protein interactions with PRMTs. Lipins act as Mg2+-dependent phosphatidate phosphatases (PAPs) which catalyze the dephosphorylation of phosphatidic acid (PA) to diacylglycerol (DAG). DAG is a powerful cell signaling molecule which can then be channeled into the synthesis of triacylglycerol (TAG) as well as the phospholipids phosphatidylcholine (PC) and phosphotidlyethanolamine (PE) via the Kennedy pathway. PE and PC are both core constituents of the protozoan cell membrane, and PE in particular is necessary for synthesis of the glycosylphosphatidylinositol (GPI) anchor. Importantly, T. brucei synthesizes its phospholipids de novo, ensuring that these phospholipids are produced by the Kennedy pathway and not by host scavenging. To observe any methylation interaction between TbPRMTs and TbLpn, a methylation assay was conducted using Adomet as a methyl source. The results show that TbPRMT1, TbPRMT5, and TbPRMT7 all successfully methylated TbLpn independently in vitro. TbPRMT3 and TbPRMT6 were incapable of methylating TbLpn in vitro. Furthermore a phosphatidic acid phosphatase assay was conducted to observe how effective TbLpn functions as an enzyme when methylated by TbPRMTs. This assay determined the enzymatic activity of TbLpn based on the release of organic phosphate (Pi) released during the dephosphorylation of PA to DAG. Results from the phosphatidic phosphatase assay show that the enzymatic activity of TbLpn increases greatly following methylation by TbPRMT5 or TbPRMT7, but not TbPRMT1, over control TbLpn.
    Collections
    Biology Master’s Theses

    entitlement

     

    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Quick Guide | Contact Us
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.