数字农科院2.0

Role Of N,N-Dimethylglycine And Its Catabolism To Sarcosine In Chromohalobacter Salexigens Dsm 3043

文献类型： 外文期刊

作者： Yang, T; Shao, YH; Guo, LZ; Meng, XL; Yu, H; Lu, WD

作者机构：

关键词： Chromohalobacter Salexigens; Metabolism; N,N Dimethylglycine; Dimethylglycine Dehydrogenase; Flavoprotein; Compatible Solute

期刊名称： APPLIED AND ENVIRONMENTAL MICROBIOLOGY

ISSN： 0099-2240

年卷期： 2020 年 86 卷 17 期

页码：

收录情况： JCR（2021版） ; EI（2021版）

摘要： Chromohalobacter salexigens DSM 3043 can grow on N,N-dimethylglycine (DMG) as the sole C, N, and energy source and utilize sarcosine as the sole N source under aerobic conditions. However, little is known about the genes and enzymes involved in the conversion of DMG to sarcosine in this strain. In the present study, gene disruption and complementation assays indicated that the csal_0990, csal_0991, csal_0992, and csal_0993 genes are responsible for DMG degradation to sarcosine. The csal_0990 gene heterologously expressed in Escherichia coli was proven to encode an unusual DMG dehydrogenase (DMGDH). The enzyme, existing as a monomer of 79 kDa with a noncovalently bound flavin adenine dinucleotide, utilized both DMG and sarcosine as substrates and exhibited dual coenzyme specificity, preferring NAD(+) to NADP(+). The optimum pH and temperature of enzyme activity were determined to be 7.0 and 60 degrees C, respectively. Kinetic parameters of the enzyme toward its substrates were determined accordingly. Under high-salinity conditions, the presence of DMG inhibited growth of the wild type and induced the production and accumulation of trehalose and glucosylglycerate intracellularly. Moreover, exogenous addition of DMG significantly improved the growth rates of the four DMG - mutants (Delta csal_0990, Delta csal_0991, Delta csal_0992, and Delta csal_0993) incubated at 37 degrees C in S-M63 synthetic medium with sarcosine as the sole N source. C-13 nuclear magnetic resonance (C-13-NMR) experiments revealed that not only ectoine, glutamate, and N-acetyl-2,4-diaminobutyrate but also glycine betaine (GB), DMG, sarcosine, trehalose, and glucosylglycerate are accumulated intracellularly in the four mutants. IMPORTANCE Although N,N-dimethylglycine (DMG) dehydrogenase (DMGDH) activity was detected in cell extracts of microorganisms, the genes encoding microbial DMGDHs have not been determined until now. In addition, to our knowledge, the physiological role of DMG in moderate halophiles has never been investigated. In this study, we identified the genes involved in DMG degradation to sarcosine, characterized an unusual DMGDH, and investigated the role of DMG in Chromohalobacter salexigens DSM 3043 and its mutants. Our results suggested that the conversion of DMG to sarcosine is accompanied by intramolecular delivery of electrons in DMGDH and intermolecular electron transfer between DMGDH and other electron acceptors. Moreover, an unidentified methyltransferase catalyzing the production of glycine betaine (GB) from DMG but sharing no homology with the reported sarcosine DMG methyltransferases was predicted to be present in the cells. The results of this study expand our understanding of the physiological role of DMG and its catabolism to sarcosine in C. salexigens.

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