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.

Creator

• Zhan, Ye

Colaboradores

• Fairchild, Craig D.
• Wobbe, Kristin K.
• Hobey, William D.

Degree

• MS

Unit

• Chemistry & Biochemistry

Publisher

• Worcester Polytechnic Institute

Language

• English

Identifier

• etd-0430102-142639

Palabra Clave

• Turnip crinkle virus
• arabidopsis
• resistance
• protein interaction
• coat protein

Advisor

• Wobbe, Kristin K.

Committee

• Fairchild, Craig D.
• Hobey, William D.

Defense date

• 2002-04-29

Year

• 2002

Date created

• 2002-04-30

Resource type

• Thesis

Rights statement

• In Copyright