The Eight Amino-Acid Differences Within Three Leucine-Rich Repeats Between Pi2 and Piz-t Resistance Proteins Determine the Resistance Specificity to Magnaporthe grisea
| Autor: | Hajime Sakai, Guo-Liang Wang, Maria Bellizzi, Bo Zhou, Shaohong Qu, Guifu Liu, Guodong Lu, Maureen Dolan |
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| Rok vydání: | 2006 |
| Předmět: |
Repetitive Sequences
Amino Acid Physiology Amino Acid Motifs Molecular Sequence Data Mutant Gene Expression Leucine-rich repeat Genes Plant Evolution Molecular Gene mapping Leucine Gene cluster Magnaporthe grisea Amino Acid Sequence Cloning Molecular Peptide sequence Gene Alleles Plant Diseases Plant Proteins Genetics biology Genetic Complementation Test Oryza Exons General Medicine Plants Genetically Modified biology.organism_classification Introns Complementation Magnaporthe Mutation Agronomy and Crop Science |
| Zdroj: | Molecular Plant-Microbe Interactions®. 19:1216-1228 |
| ISSN: | 1943-7706 0894-0282 |
| Popis: | The rice blast resistance (R) genes Pi2 and Piz-t confer broad-spectrum resistance against different sets of Magnaporthe grisea isolates. We first identified the Pi2 gene using a map-based cloning strategy. The Pi2 gene is a member of a gene cluster comprising nine gene members (named Nbs1-Pi2 to Nbs9-Pi2) and encodes a protein with a nucleotide-binding site and leucine-rich repeat (LRR) domain. Fine genetic mapping, molecular characterization of the Pi2 susceptible mutants, and complementation tests indicated that Nbs4-Pi2 is the Pi2 gene. The Piz-t gene, a Pi2 allele in the rice cultivar Toride 1, was isolated based on the Pi2 sequence information. Complementation tests confirmed that the family member Nbs4-Piz-t is Piz-t. Sequence comparison revealed that only eight amino-acid changes, which are confined within three consecutive LRR, differentiate Piz-t from Pi2. Of the eight variants, only one locates within the xxLxLxx motif. A reciprocal exchange of the single amino acid between Pi2 and Piz-t did not convert the resistance specificity to each other but, rather, abolished the function of both resistance proteins. These results indicate that the single amino acid in the xxLxLxx motif may be critical for maintaining the recognition surface of Pi2 and Piz-t to their respective avirulence proteins. |
| Databáze: | OpenAIRE |
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