Interactions between Pteris vittata L. genotypes and a polycyclic aromatic hydrocarbon (PAH)-degrading bacterium ( Alcaligenes sp.) in arsenic uptake and PAH-dissipation

2017 ◽  
Vol 230 ◽  
pp. 862-870 ◽  
Author(s):  
Lu Sun ◽  
Ganghui Zhu ◽  
Xiaoyong Liao ◽  
Xiulan Yan
2012 ◽  
Vol 194 (23) ◽  
pp. 6677-6677 ◽  
Author(s):  
Qiliang Lai ◽  
Weiwei Li ◽  
Baojiang Wang ◽  
Zhiwei Yu ◽  
Zongze Shao

ABSTRACTCycloclasticussp. strain P1 was isolated from deep-sea sediments of the Pacific Ocean and characterized as a unique bacterium in the degradation of pyrene, a four-ring polycyclic aromatic hydrocarbon (PAH). Here we report the complete genome of P1 and genes associated with PAH degradation.


2004 ◽  
Vol 54 (6) ◽  
pp. 2313-2317 ◽  
Author(s):  
Kerstin Derz ◽  
Ulrich Klinner ◽  
Ingolf Schuphan ◽  
Erko Stackebrandt ◽  
Reiner M. Kroppenstedt

The taxonomic position of a polycyclic-aromatic-hydrocarbon-degrading bacterium, strain 17A3T, isolated from contaminated soil was determined using a combination of phenotypic and genotypic properties. The isolate showed phenotypic properties that were diagnostic for species of the genus Mycobacterium. Comparative 16S rRNA gene sequence analysis assigned 17A3T to the 16S rRNA gene subgroup that contains Mycobacterium aurum, Mycobacterium austroafricanum, Mycobacterium vaccae and Mycobacterium vanbaalenii, but it could clearly be distinguished from these species using a combination of physiological, chemotaxonomic markers and internal rRNA gene spacer analyses. The data showed that strain 17A3T (=DSM 44605T=NRRL B-24244T) merits recognition as the type strain of a novel species of the genus Mycobacterium. The name Mycobacterium pyrenivorans sp. nov. is proposed for the species because of its ability to use pyrene as a sole source of carbon and energy.


2000 ◽  
Vol 66 (10) ◽  
pp. 4300-4304 ◽  
Author(s):  
Rong-Fu Wang ◽  
David Wennerstrom ◽  
Wei-Wen Cao ◽  
Ashraf A. Khan ◽  
Carl E. Cerniglia

ABSTRACT A 81-kDa protein from Mycobacterium sp. strain PYR-1 was expressed in response to exposure of the strain to the polycyclic aromatic hydrocarbon pyrene and recovered by two-dimensional gel electrophoresis. The N-terminal sequence of the protein indicated that it was similar to catalase-peroxidase. An oligonucleotide probe designed from this sequence was used to screen a genomic library ofMycobacterium sp. strain PYR-1, and a positive clone, containing a part of the gene encoding the 81-kDa protein, was isolated. A gene-walking technique was used to sequence the entire gene, which was identified as katG for catalase-peroxidase. The deduced KatG protein sequence showed significant homology to KatGII of Mycobacterium fortuitum and clustered with catalase-peroxidase proteins from other Mycobacteriumspecies in a phylogenetic tree. The katG gene was expressed in Escherichia coli to produce a protein with catalase-peroxidase activity. Since the induction of this catalase-peroxidase occurred in pyrene-induced cultures and the exposure of these cultures to hydrogen peroxide reduced pyrene metabolism, our data suggest that this enzyme plays a role in polycyclic aromatic hydrocarbon metabolism by strain PYR-1.


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