rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: Functional and structural characterization of cation/H⁺ antiporters
  name:
    name part: Manohar, Murli.
    role:
      role term: creator
  name:
    name part: Hirschi, Kendal
    role:
      role term: thesis advisor.
  name:
    name part: Patil, Bhimanagouda S.
    role:
      role term: thesis advisor.
  type of resource: text
  genre: bibliography
  origin info:
    place:
      place term: txu
    date issued: 2012
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: remote
    extent: 1 online resource
  abstract: Inorganic cations play decisive roles in many cellular and physiological processes and are essential components of plant nutrition. Therefore, the uptake of cations and their redistribution must be precisely controlled. Vacuolar antiporters are important elements in mediating the intracellular sequestration of these cations. CAXs (for CAtion eXchanger) are members of a multigene family and appear to predominately reside on vacuoles. Defining CAX regulation and substrate specificity have been aided by utilizing yeast as an experimental tool. Studies in plants suggest CAXs regulate apoplastic Ca²⁺ levels in order to optimize cell wall expansion, photosynthesis, transpiration and plant productivity. CAX studies provide the basis for making designer transporters that have been used to develop nutrient enhanced crops and plants for remediating toxic soils. In my second study, I have characterized and defined autoinhibitory domain of Arabidopsis CAX3. Several CAX transporters, including CAX1, appear to contain an approximately 40 amino acid N-terminal regulatory regions (NRR) that modulates transport through N-terminal autoinhibition. Deletion of the NRR from several CAXs (sCAX) enhances function in plant and yeast expression assays; however, to date, there are no functional assays for CAX3. In this report, we create a series of truncations in the CAX3 NRR and demonstrate activation of CAX3 in both yeast and plants by truncating a large portion of the NRR. Experiments on endomembrane-enriched vesicles isolated from yeast expressing activated CAX3 demonstrate that the gene encodes Ca²⁺/H⁺ exchange with properties distinct from CAX1. These studies demonstrate shared and unique aspects of CAX1 and CAX3 transport and regulation. My third study is to express and purify CAX proteins for X-ray crystallographic analysis. In this study, I initiated crystallization of vacuolar membrane localized CAX protein from eukaryotes. Membrane proteins continue to be challenging targets for s…
  note: by Murli Manohar.
  note: "Major Subject: Molecular and Environmental Plant Sciences"
  note: Electronic resource.
  note: Doctor of Philosophy Texas A&M University 2012 http://hdl.handle.net/1969.1/ETD-TAMU-2012-05-10915
  note: Includes bibliographical references.
  note: Text (Dissertation)
  subject:
    topic: Major Molecular and Environmental Plant Sciences
  subject:
    topic: Autoinhibition
  subject:
    topic: Nutrition
  subject:
    topic: Biofortification
  subject:
    topic: Cation exchanger
  subject:
    topic: Membrane protein structure
  identifier: http://hdl.handle.net/1969.1/ETD-TAMU-2012-05-10915
  record info:
    record content source: TXA
    record creation date: 121011
    record change date: 20150922123533.0
    record identifier: in00002765000