Cotinine Hydroxylase CotA Initiates Biodegradation of Wastewater Micropollutant Cotinine in Nocardioides sp. Strain JQ2195

Cotinine Hydroxylase CotA Initiates Biodegradation of Wastewater Micropollutant Cotinine in Nocardioides sp. Strain JQ2195
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可替宁羟化酶 CotA 启动诺卡氏菌中废水微污染物可替宁的生物降解。

DOI:
10.1128/aem.00923-21
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发表时间:
2021-07
影响因子:
4.4
通讯作者:
He Jian
He Jian
中科院分区:
生物学2区
文献类型:
--
作者:
Zhao Lingling;Zhao Zhenyang;Zhang Kaiyun;Zhang Xuan;Xu Siqiong;Liu Junwei;Liu Bin;Hong Qing;Qiu Jiguo;He Jian

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在人体内,可替宁是尼古丁的主要代谢产物,产生的可替宁的10 - 15%通过尿液排泄。可替宁是尼古丁的结构类似物,比尼古丁稳定得多。摘要可替宁是一种稳定的有毒污染物,是吸烟的副产品。由于其在水生环境中的全球分布,它正在引起人们的关注。微生物具有降解可替宁的潜力;然而,该过程的遗传机制尚不清楚。Nocardioides sp.菌株JQ 2195是一种纯培养菌株,已报道在微污染物浓度下降解可替宁。该菌株利用可替宁作为其唯一的碳源和氮源。在这项研究中,一个50 kb的基因簇(指定的cot),参与可替宁降解,预测基于基因组和转录组学分析。一个新的三组分可替宁羟化酶基因(命名为cotA 1A 2A 3),启动可替宁catalysts,被确定和表征。异源表达并纯化来自Shinella sp.菌株HZN 7的科塔,并显示将可替宁转化为6-羟基可替宁。H218 O标记和电喷雾电离质谱(ESI-MS)分析证实,6-羟基可替宁中的羟基来自水。这项研究为杂环化学污染物的微生物代谢提供了新的分子见解。在人体内,可替宁是尼古丁的主要代谢物,产生的可替宁的10 - 15%通过尿液排泄。可替宁是尼古丁的结构类似物,比尼古丁稳定得多。烟草消费的增加导致可替宁的高环境浓度,这可能对水生生态系统和人类健康产生有害影响。Nocardioides sp.菌株JQ 2195是一种独特的可替宁降解菌。然而,可替宁降解的潜在遗传和生化基础仍然未知。在这项研究中,一个50 kb的基因簇(指定的cot)被确定为参与可替宁的降解的基因组和转录组学分析。一个新的三组分可替宁羟化酶基因(命名为cotA 1A 2A 3)催化可替宁生成6-羟基可替宁。该研究为可替宁的微生物降解和酶促转化提供了新的分子视角。
In the human body, cotinine is the major metabolite of nicotine, and 10 to 15% of generated cotinine is excreted in urine. Cotinine is a structural analogue of nicotine and is much more stable than nicotine. ABSTRACT Cotinine is a stable toxic contaminant, produced as a by-product of smoking. It is of emerging concern due to its global distribution in aquatic environments. Microorganisms have the potential to degrade cotinine; however, the genetic mechanisms of this process are unknown. Nocardioides sp. strain JQ2195 is a pure-culture strain that has been reported to degrade cotinine at micropollutant concentrations. This strain utilizes cotinine as its sole carbon and nitrogen source. In this study, a 50-kb gene cluster (designated cot), involved in cotinine degradation, was predicted based on genomic and transcriptomic analyses. A novel three-component cotinine hydroxylase gene (designated cotA1A2A3), which initiated cotinine catabolism, was identified and characterized. CotA from Shinella sp. strain HZN7 was heterologously expressed and purified and was shown to convert cotinine into 6-hydroxycotinine. H218O-labeling and electrospray ionization-mass spectrometry (ESI-MS) analysis confirmed that the hydroxyl group incorporated into 6-hydroxycotinine was derived from water. This study provides new molecular insights into the microbial metabolism of heterocyclic chemical pollutants. IMPORTANCE In the human body, cotinine is the major metabolite of nicotine, and 10 to 15% of generated cotinine is excreted in urine. Cotinine is a structural analogue of nicotine and is much more stable than nicotine. Increased tobacco consumption has led to high environmental concentrations of cotinine, which may have detrimental effects on aquatic ecosystems and human health. Nocardioides sp. strain JQ2195 is a unique cotinine-degrading bacterium. However, the underlying genetic and biochemical foundations of cotinine degradation are still unknown. In this study, a 50-kb gene cluster (designated cot) was identified by genomic and transcriptomic analyses as being involved in the degradation of cotinine. A novel three-component cotinine hydroxylase gene (designated cotA1A2A3) catalyzed cotinine to 6-hydroxy-cotinine. This study provides new molecular insights into the microbial degradation and enzymatic transformation of cotinine.
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