Studies of Dimethylglycine Oxidase Isoenzymes in Arthrobacter globiformis Cells

• Published in: Current microbiology Vol. 62; no. 4; pp. 1267 - 1273
• Main Authors: Casait, Vida, Povilonien, Simona, Meskien, Rita, Rutkien, Rasa, Meskys, Rolandas
• Format: Journal Article
• Language: English
• Published: New York New York : Springer-Verlag 01.04.2011; Springer-Verlag; Springer Nature B.V
• Subjects: Arthrobacter - chemistry; Arthrobacter - enzymology; Arthrobacter - genetics; Arthrobacter globiformis; Bacteria; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; betaine; Betaine - metabolism; Biomedical and Life Sciences; Biotechnology; carbon; Carbon sources; DNA; Enzymes; genes; Isoenzymes - genetics; Isoenzymes - metabolism; isozymes; Life Sciences; metabolism; Microbiology; Molecular Sequence Data; osmotolerance; Oxidoreductases Acting on CH-NH Group Donors - genetics; Oxidoreductases Acting on CH-NH Group Donors - metabolism; reverse transcriptase polymerase chain reaction; Salinity; salt concentration; Sole Carbon Source; Glycine Betaine; Compatible Solute; Arthrobacter
• ISSN: 0343-8651; 1432-0991
• DOI: 10.1007/s00284-010-9852-6

Glycine betaine (GB) could be used by Arthrobacter globiformis cells as a sole carbon source. The cells took up this molecule in the low as well as in the high salinity medium. Addition of GB to the mineral medium with high salt concentration revealed that GB was also used as an osmoprotectant. Dimethylglycine oxidase (DMGO) was involved in the catabolism of GB. Two genes for DMGO were detected in a cloned 26267 bp fragment of A. globiformis DNA. The genes involved in the tetrahydrofolate-dependent assimilation of methyl groups were located nearby the two of DMGO genes. Both cloned A. globiformis DMGO were active. The activity of DMGO was detected in A. globiformis cells and it depended on the addition of GB and the salinity of the medium. Reverse transcription-PCR demonstrated that the addition of GB influenced the transcription of dmg genes.