Amino acid substitutions in a polygalacturonase inhibiting protein (OsPGIP2) increases sheath blight resistance in rice.

ABSTRACT:

Background

An economic strategy to control plant disease is to improve plant defense to pathogens by deploying resistance genes. Plant polygalacturonase inhibiting proteins (PGIPs) have a vital role in plant defense against phytopathogenic fungi by inhibiting fungal polygalacturonase (PG) activity. We previously reported that rice PGIP1 (OsPGIP1) inhibits PG activity in Rhizoctonia solani, the causal agent of rice sheath blight (SB), and is involved in regulating resistance to SB.

Result

Here, we report that OsPGIP2, the protein ortholog of OsPGIP1, does not possess PGIP activity; however, a few amino acid substitutions in a derivative of OsPGIP2, of which we provide support for L233F being the causative mutation, appear to impart OsPGIP2 with PG inhibition capability. Furth

SUBMITTER: Chen X 

PROVIDER: S-EPMC6663954 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature