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Recombinant tobacco mosaic virus movement protein is an rna-binding, alpha-helical membrane protein

Academic Article
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Overview

authors

  • Brill, L. M.
  • Nunn, R. S.
  • Kahn, T. W.
  • Yeager, Mark
  • Beachy, R. N.

publication date

  • June 2000

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • The 30-kDa movement protein (MP) is essential for cell-cell spread of tobacco mosaic virus in planta. To explore the structural properties of MP, the full-length recombinant MP gene was expressed in Escherichia coli, and one-step purification from solubilized inclusion bodies was accomplished by using anion exchange chromatography. Soluble MP was maintained at >4 mg/ml without aggregation and displayed approximately 70% alpha-helical conformation in the presence of urea and SDS. A trypsin-resistant core domain of the MP had tightly folded tertiary structure, whereas 18 aa at the C terminus of the monomer were rapidly removed by trypsin. Two hydrophobic regions within the core were highly resistant to proteolysis. Based on results of CD spectroscopy, trypsin treatment, and MS, we propose a topological model in which MP has two putative alpha-helical transmembrane domains and a protease-sensitive carboxyl terminus.

subject areas

  • Amino Acid Sequence
  • Membrane Proteins
  • Molecular Sequence Data
  • Plant Viral Movement Proteins
  • Protein Folding
  • RNA-Binding Proteins
  • Recombinant Proteins
  • Tobacco Mosaic Virus
  • Viral Proteins
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Identity

PubMed Central ID

  • PMC16508

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.130187897

PubMed ID

  • 10840061
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Additional Document Info

start page

  • 7112

end page

  • 7117

volume

  • 97

issue

  • 13

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