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《Molecular Microbiology》对我组和复旦大学生命科学学院甘建华教授研究组在该刊发表的肺炎克雷伯菌中乙酰基转移酶类毒素-抗毒素系统的以下合作论文配发了专评 
H. Qian, Q. Yao, C. Tai, Z. Deng, J. Gan*, H.Y. Ou* (2018) Identification and characterization of acetyltransferase-type toxin-antitoxin loci in Klebsiella pneumoniae. Molecular Microbiology, DOI:10.1111/mmi.13934.

专评如下:

Molecular Microbiology, 2018, DOI:10.1111/mmi.13958.

GNAT Toxins of Bacterial Toxin‐Antitoxin Systems: Acetylation of Charged tRNAs to Inhibit Translation

Chew Chieng Yeo

 Link to Molecular Microbiology
 
GCN5‐related N‐acetyltransferase (GNAT) is a huge superfamily of proteins spanning the prokaryotic and eukaryotic domains of life. GNAT proteins usually transfer an acetyl group from acetyl‐CoA to a wide variety of substrates ranging from aminoglycoside antibiotics to large macromolecules. Type II toxin‐antitoxin (TA) modules are typically bicistronic and widespread in bacterial and archael genomes with diverse cellular functions. Recently, a novel family of type II TA toxins was described which presents a GNAT‐fold and functions by acetylating charged tRNA thereby precluding translation. These GNAT toxins are usually associated with a corresponding ribbon‐helix‐helix‐fold (RHH) antitoxin. In this issue of Molecular Microbiology, Qian et al. describes a unique GNAT‐RHH TA system, designated KacAT, from a multidrug resistant strain of the pathogen, Klebsiella pneumoniae. Like most type II TA loci, kacAT is transcriptionally autoregulated with the KacAT complex binding to the operator site via the N‐terminus region of KacA to repress kacAT transcription. The crystal structure of the KacT toxin is also presented giving a structural basis for KacT toxicity. These findings expand our knowledge on this newly discovered family of TA toxins and the potential role that they may play in antibiotic tolerance and persistence of bacterial pathogens. This article is protected by copyright. All rights reserved.
 
 


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