arsRBOCT arsenic resistance system encoded by linear plasmid pHZ227 in Streptomyces sp. strain FR-008

Article Abstract:

The analysis of an arsenic resistance (ars) gene cluster from a large linear plasmid, pHZ227, in Streptomyces sp. strain FR-008 is reported and the determinant is compared with the putative ars gene clusters from Streptomyces coelicolor A3(2) (1) and Streptomyces sp. strain F2. The pHZ227 ArsB protein has showed homology to the yeast arsenite transporter Acr3p and the pHZ227 ArsC is a bacterial thioredoxin-dpendent ArsC-type arsenate reductase with four conserved cysteine thioreduction-requiring motifs.

author: Xiufen Zhou, Zixin Deng, Xiang Xiao, Lianrong Wang, Shi Chen, Xi Huang, Delin You
All Other Basic Inorganic Chemical Manufacturing, Industrial inorganic chemicals, not elsewhere classified, Arsenic & Compounds, Genetic aspects, Drug resistance in microorganisms, Microbial drug resistance, Plasmids, Arsenic compounds, Streptomyces, Chemical properties

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Chitinase genes in lake sediments of Ardley Island, Antarctica

Article Abstract:

A sediment core spanning approximately 1,600 years was collected from a lake on Ardley Island, Antarctica, and molecular methods are used to study the chitinolytic bacterial community along this sediment core. The phylogeny of the chitinase genes obtained from the isolates did not correspond well to that of the isolates, which indicates acquisition via horizontal gene transfer.

author: Peng Wang, Fengping Wang, Xiang Xiao, Xuebin Yin, Jian Lin, Liguang Sun, Ziyong You
Antarctica, Nitrogenous Fertilizer Manufacturing, Nitrogenous fertilizers, Guano, Microbiological research, Penguins, Lake sediments

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Putative exposed aromatic and hydroxyl residues on the surface of the N-terminal domains of Chi1 from Aeromonas caviae CB101 are essential for chitin binding and hydrolysis

Article Abstract:

Chitinase Chi1 of Aeromonas caviae CB101 possesses chitin binding sites at both its N and C termini. Four putative exposed residues aligned in a line on the surface of the N-terminal domains of Chi1 are found to contribute to the enzyme-chitin binding and hydrolysis through site-directed mutagenesis.

author: Qiang Li, Fengping Wang, Xiang Xiao, Ying Zhou
Chitin, Hydrolysis, Mutagenesis

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subjects list: Research
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