A Comprehensive Structure–Function Analysis ofArabidopsisSNI1 Defines Essential Regions and Transcriptional Repressor Activity | Zendy

Rebecca A. Mosher | Zendy; Wendy E. Durrant | Zendy; Dong Wang | Zendy; Junqi Song | Zendy; Xinnian Dong | Zendy

Open Access

A Comprehensive Structure–Function Analysis ofArabidopsisSNI1 Defines Essential Regions and Transcriptional Repressor Activity

Author(s) -

Rebecca A. Mosher,

Wendy E. Durrant,

Dong Wang,

Junqi Song,

Xinnian Dong

Publication year - 2006

Publication title -

the plant cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.324

H-Index - 341

eISSN - 1532-298X

pISSN - 1040-4651

DOI - 10.1105/tpc.105.039677

Subject(s) - biology , repressor , arabidopsis , chromatin immunoprecipitation , gene , genetics , systemic acquired resistance , transcription (linguistics) , general transcription factor , transcription factor , psychological repression , mutant , transcriptional regulation , microbiology and biotechnology , promoter , gene expression , linguistics , philosophy

The expression of systemic acquired resistance (SAR) in plants involves the upregulation of many Pathogenesis-Related (PR) genes, which work in concert to confer resistance to a broad spectrum of pathogens. Because SAR is a costly process, SAR-associated transcription must be tightly regulated. Arabidopsis thaliana SNI1 (for Suppressor of NPR1, Inducible) is a negative regulator of SAR required to dampen the basal expression of PR genes. Whole genome transcriptional profiling showed that in the sni1 mutant, Nonexpresser of PR genes (NPR1)-dependent benzothiadiazole S-methylester-responsive genes were specifically derepressed. Interestingly, SNI1 also repressed transcription when expressed in yeast, suggesting that it functions as an active transcriptional repressor through a highly conserved mechanism. Chromatin immunoprecipitation indicated that histone modification may be involved in SNI1-mediated repression. Sequence comparison with orthologs in other plant species and a saturating NAAIRS-scanning mutagenesis of SNI1 identified regions in SNI1 that are required for its activity. The structural similarity of SNI1 to Armadillo repeat proteins implies that SNI1 may form a scaffold for interaction with proteins that modulate transcription.

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