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Title page for ETD etd-0430102-142639


Document Typethesis
Author NameZhan, Ye
URNetd-0430102-142639
TitleMolecular Analysis of Turnip Crinkle Virus Coat Protein Mutations
DegreeMS
DepartmentChemistry & Biochemistry
Advisors
  • Dr. Kristin K. Wobbe, Advisor
  • Dr. Craig D. Fairchild, Committee Member
  • Dr. William D. Hobey, Committee Member
  • Keywords
  • protein interaction
  • coat protein
  • resistance
  • arabidopsis
  • turnip crinkle virus
  • Date of Presentation/Defense2002-04-29
    Availability unrestricted

    Abstract

    TCV (Turnip crinkle virus) coat protein is required for the resistance response in Arabidopsis thaliana Di-17 plants. An aspartate to asparagine mutation at amino acid four of the coat protein is sufficient to result in resistance-breaking. To determine the essential chemical properties responsible for the induction of resistance, a series of site-directed mutants were produced. Serine as well as asparagine at amino acid four induces systemic disease on both Di-3 and Di-17 plants; however, replacement of aspartate with glutamate retains the ability to induce the HR (hypersensitive response) and resist TCV infection with rapid and strong induction of PR-1 gene. These data suggest that the negative charge at the fourth amino acid of the coat protein is critical for the induction of resistance. Taken together with other mutagenesis research, the N-terminus of the coat protein appears to be the sole viral recognition element.

    The A. thaliana TIP protein is suggested to be involved in resistance, mainly through its C-terminus. Interestingly, one of the resistance-breaking mutants (D4N) produces a HR on Di-3 plants that are normally susceptible. The Di-3 TIP protein has several differences from the Di-17 TIP. To detect whether the delayed HR is related to interaction between Di-3 TIP and D4N mutation, a yeast two-hybrid assay was attempted. Interactions have not yet been detected. There are a number of possible explanations.

    Files
  • zhan.pdf

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