Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Dimerization of recombinant tobacco mosaic virus movement protein

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Brill, L. M.
  • Dechongkit, S.
  • DeLaBarre, B.
  • Stroebel, J.
  • Beachy, R. N.
  • Yeager, Mark

publication date

  • April 2004

journal

  • Journal of Virology  Journal

abstract

  • The p30 movement protein (MP) is essential for cell-to-cell spread of tobacco mosaic virus in planta. We used anion-exchange chromatography and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to obtain highly purified 30-kDa MP, which migrated as a single band in native PAGE. Analytical ultracentrifugation suggested that the protein was monodisperse and dimeric in the nonionic detergent n-octyl-beta-D-glucopyranoside. Circular dichroism (CD) spectroscopy showed that the detergent-solubilized protein contained significant alpha-helical secondary structure. Proteolysis of the C-tail generated a trypsin-resistant core that was a mixture of primarily monomers and some dimers. We propose that MP dimers are stabilized by electrostatic interactions in the C terminus as well as hydrophobic interactions between putative transmembrane alpha-helical coiled coils.

subject areas

  • Amino Acid Sequence
  • Circular Dichroism
  • Dimerization
  • Models, Molecular
  • Molecular Sequence Data
  • Plant Viral Movement Proteins
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Solubility
  • Tobacco Mosaic Virus
  • Trypsin
  • Ultracentrifugation
  • Viral Proteins
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.78.7.3372-3377.2004

PubMed ID

  • 15016859
scroll to property group menus

Additional Document Info

start page

  • 3372

end page

  • 3377

volume

  • 78

issue

  • 7

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support