A microorganism capable of degrading 4-chloro-2-methylphenoxyacetic acid (MCPA) was isolated from soil and identified as Flavobacterium peregrinum. All of the chlorine of MCPA was released as chloride, and the carboxyl-carbon was converted to volatile products by growing cultures of the bacterium, but a phenol accumulated in the medium. The phenol was identified as 4-chloro-2-methylphenol on th...

An Arthrobacter species FB24 gene (locus tag Arth_1007) was previously annotated as a putative intein-containing DnaB helicase of phage origin (Arsp-FB24 DnaB intein). However, it is not a helicase gene because the sequence similarity is limited to inteins. In fact, the flanking exteins total only 66 amino acids. Therefore, the intein should be referred to as the Arsp-FB24 Arth_1007 intein. The...

We report the first genome sequence for Arthrobacter siccitolerans 4J27, a newly described desiccation-tolerant species. The complete genome of A. siccitolerans 4J27 has been sequenced and is estimated to be around 5.3 Mb in size, with an average GC content of 65.13%. We predict 4,480 protein-coding sequences (CDSs).

Microbial antagonism in an Arctic soil habitat was demonstrated by assessing the inhibitory interactions between bacterial isolates from the same location. Of 139 isolates obtained from five soil samples, 20 antagonists belonging to the genera, Arthrobacter, Pseudomonas and Flavobacterium were identified. Inter-genus, inter-species and inter-strain antagonism was observed between the interactin...

During the course of growth of Arthrobacter oxidans, induction of the enantiozymes 6-hydroxy-D-nicotine oxidase and 6-hydroxy-L-nicotine oxidase occurred in the presence of DL-nicotine. Cryoultramicrotomed sections obtained from cells grown to stationary phase were gold immunolabeled. The results obtained demonstrate that both enzymes are localized in the cytoplasm.

Two extracellular, heat-labile alkaline phosphatases were purified from a psychrophilic Arthrobacter isolate, D10. The enzymes were active over different pH ranges, used distinct substrates, and had different kinetic properties. Each enzyme reacted specifically to its own antibody during immunoblot analysis. One had both monophosphatase and diesterase activities.