Title page for ETD etd-0430102-142639

Document Type thesis

Author Name Zhan, Ye

URN etd-0430102-142639

Title Molecular Analysis of Turnip Crinkle Virus Coat Protein Mutations

Degree MS

Department Chemistry & 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/Defense 2002-04-29

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

Browse by Author | Browse by Department | Search all available ETDs

Questions? Email etd-questions@wpi.edu
Maintained by webmaster@wpi.edu

Document Type	thesis
Author Name	Zhan, Ye
URN	etd-0430102-142639
Title	Molecular Analysis of Turnip Crinkle Virus Coat Protein Mutations
Degree	MS
Department	Chemistry & 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/Defense	2002-04-29
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