+検索条件
-Structure paper
タイトル | A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. |
---|---|
ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 972, Year 2019 |
掲載日 | 2019年2月27日 |
著者 | Ariel Talavera / Hedvig Tamman / Andres Ainelo / Albert Konijnenberg / San Hadži / Frank Sobott / Abel Garcia-Pino / Rita Hõrak / Remy Loris / |
PubMed 要旨 | Bacterial toxin-antitoxin (TA) modules are tightly regulated to maintain growth in favorable conditions or growth arrest during stress. A typical regulatory strategy involves the antitoxin binding ...Bacterial toxin-antitoxin (TA) modules are tightly regulated to maintain growth in favorable conditions or growth arrest during stress. A typical regulatory strategy involves the antitoxin binding and repressing its own promoter while the toxin often acts as a co-repressor. Here we show that Pseudomonas putida graTA-encoded antitoxin GraA and toxin GraT differ from other TA proteins in the sense that not the antitoxin but the toxin possesses a flexible region. GraA auto-represses the graTA promoter: two GraA dimers bind cooperatively at opposite sides of the operator sequence. Contrary to other TA modules, GraT is a de-repressor of the graTA promoter as its N-terminal disordered segment prevents the binding of the GraTA complex to the operator. Removal of this region restores operator binding and abrogates Gr aT toxicity. GraTA represents a TA module where a flexible region in the toxin rather than in the antitoxin controls operon expression and toxin activity. |
リンク | Nat Commun / PubMed:30814507 / PubMed Central |
手法 | SAS (X-ray synchrotron) / X線回折 |
解像度 | 2.002 - 3.8 Å |
構造データ | SASDE48: Toxin GraT (Putative killer protein, Toxin GraT., GraT) PDB-6f8h: PDB-6f8s: PDB-6fix: |
化合物 | ChemComp-HOH: ChemComp-SO4: ChemComp-PEG: |
由来 |
|
キーワード | ANTITOXIN / GraA / HigA / TOXIN / GraT / HigB / GraTA / HigBA / operator / DNA |