The Ruegeria pomeroyi acuI gene has a role in DMSP catabolism and resembles yhdH of E. coli and other bacteria in conferring resistance to acrylate.

The Ruegeria pomeroyi acuI gene has a role in DMSP catabolism and resembles yhdH of E. coli and other bacteria in conferring resistance to acrylate.
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DOI:
10.1371/journal.pone.0035947
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发表时间:
2012
期刊:
影响因子:
3.7
通讯作者:
Johnston AW
Johnston AW
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Todd JD;Curson AR;Sullivan MJ;Kirkwood M;Johnston AW

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大肠杆菌YhdH多肽属于MDR 012中链还原酶/脱氢酶亚组,但其生物学功能尚不清楚,也没有描述过YhdH−突变体的表型。我们发现一个E. yhdH插入突变的大肠杆菌菌株对丙烯酸酯的抑制作用高度敏感,对3-羟基丙酸酯的抑制作用也高度敏感。YhdH的同源物存在于许多细菌分类群和至少两种动物中。YhdH−突变体的丙烯酸酯敏感性通过从几种细菌中克隆的相应同源物进行校正。其中一种同系物是acuI,它在海洋细菌降解丙烯酸酯中起作用,海洋细菌分解代谢二甲基磺基丙酸酯(DMSP),这是一种由海洋浮游植物产生的丰富的抗应激化合物。这种细菌的acuI基因通常与ddd基因相关联,ddd基因编码将DMSP切割成丙烯酸酯加二甲基硫醚(DMS)的酶,即使这些酶在不相关的细菌中属于不同的多肽家族。此外,玫瑰杆菌属的大多数菌株(丰富的海洋细菌的进化枝)将DMSP裂解成丙烯酸酯加DMS,并且还可以使用DMSP脱甲基酶将其脱甲基。在大多数玫瑰杆菌中,相应的基因dmdA位于acuI的直接上游,在模型玫瑰杆菌菌株Ruegeria pomeroyi DSS-3中,dmdA-acuI响应于共诱导物丙烯酸酯而被共调节。这些观察结果,连同其他AcuI具有丙烯酰辅酶A还原酶活性的发现,使我们认为YdhH/AcuI酶保护细胞免受内源性形成的细胞内丙烯酰辅酶A和/或通过分解代谢外源性丙烯酸酯的损伤作用。为了为从DMSP形成丙烯酸酯的细菌提供“额外的保护”,acuI被招募到参与这种转化的基因簇中,并且在玫瑰杆菌中acuI和dmdA的情况下,它们的共表达可能支持DMSP催化剂的两种途径之间的相互作用,由此DMSP裂解酶的丙烯酸酯产物是去甲基化途径的共诱导物。
The Escherichia coli YhdH polypeptide is in the MDR012 sub-group of medium chain reductase/dehydrogenases, but its biological function was unknown and no phenotypes of YhdH− mutants had been described. We found that an E. coli strain with an insertional mutation in yhdH was hyper-sensitive to inhibitory effects of acrylate, and, to a lesser extent, to those of 3-hydroxypropionate. Close homologues of YhdH occur in many Bacterial taxa and at least two animals. The acrylate sensitivity of YhdH− mutants was corrected by the corresponding, cloned homologues from several bacteria. One such homologue is acuI, which has a role in acrylate degradation in marine bacteria that catabolise dimethylsulfoniopropionate (DMSP) an abundant anti-stress compound made by marine phytoplankton. The acuI genes of such bacteria are often linked to ddd genes that encode enzymes that cleave DMSP into acrylate plus dimethyl sulfide (DMS), even though these are in different polypeptide families, in unrelated bacteria. Furthermore, most strains of Roseobacters, a clade of abundant marine bacteria, cleave DMSP into acrylate plus DMS, and can also demethylate it, using DMSP demethylase. In most Roseobacters, the corresponding gene, dmdA, lies immediately upstream of acuI and in the model Roseobacter strain Ruegeria pomeroyi DSS-3, dmdA-acuI were co-regulated in response to the co-inducer, acrylate. These observations, together with findings by others that AcuI has acryloyl-CoA reductase activity, lead us to suggest that YdhH/AcuI enzymes protect cells against damaging effects of intracellular acryloyl-CoA, formed endogenously, and/or via catabolising exogenous acrylate. To provide “added protection” for bacteria that form acrylate from DMSP, acuI was recruited into clusters of genes involved in this conversion and, in the case of acuI and dmdA in the Roseobacters, their co-expression may underpin an interaction between the two routes of DMSP catabolism, whereby the acrylate product of DMSP lyases is a co-inducer for the demethylation pathway.
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期刊: COMPUTER APPLICATIONS IN THE BIOSCIENCES
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