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Keyword
- activation mechanism1
- aerolysin-like protein (ALP)1
- antibiotic resistance1
- autoinhibition1
- bacterial toxin1
- BmALP31
- crystal structure1
- dimerization1
- disulfide1
- DNA-binding protein1
- drug resistance1
- endolysosomes1
- multidrug resistance (MDR)1
- pore-forming protein1
- redox regulation1
- structure biology1
- TipA1
- transcription promoter1
- transcription regulation1
- transcriptional regulator1
- vesicles1
- βγ-CAT1
Gene Regulation
2 Results
- Protein Structure and FoldingOpen Access
Antibiotic binding releases autoinhibition of the TipA multidrug-resistance transcriptional regulator
Journal of Biological ChemistryVol. 295Issue 51p17865–17876Published online: December 18, 2020- Xuguang Jiang
- Linjuan Zhang
- Maikun Teng
- Xu Li
Cited in Scopus: 1Investigations of bacterial resistance strategies can aid in the development of new antimicrobial drugs as a countermeasure to the increasing worldwide prevalence of bacterial antibiotic resistance. One such strategy involves the TipA class of transcription factors, which constitute minimal autoregulated multidrug resistance (MDR) systems against diverse antibiotics. However, we have insufficient information regarding how antibiotic binding induces transcriptional activation to design molecules that could interfere with this process. - Gene RegulationOpen Access
A cellular endolysosome-modulating pore-forming protein from a toad is negatively regulated by its paralog under oxidizing conditions
Journal of Biological ChemistryVol. 295Issue 30p10293–10306Published online: June 4, 2020- Qiquan Wang
- Xianling Bian
- Lin Zeng
- Fei Pan
- Lingzhen Liu
- Jinyang Liang
- and others
Cited in Scopus: 9Endolysosomes are key players in cell physiology, including molecular exchange, immunity, and environmental adaptation. They are the molecular targets of some pore-forming aerolysin-like proteins (ALPs) that are widely distributed in animals and plants and are functionally related to bacterial toxin aerolysins. βγ-CAT is a complex of an ALP (BmALP1) and a trefoil factor (BmTFF3) in the firebelly toad (Bombina maxima). It is the first example of a secreted endogenous pore-forming protein that modulates the biochemical properties of endolysosomes by inducing pore formation in these intracellular vesicles.