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首页> 外文期刊>Journal of bacteriology >Identification of the Amidotransferase AsnB1 as Being Responsible for meso-Diaminopimelic Acid Amidation in Lactobacillus plantarum Peptidoglycan
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Identification of the Amidotransferase AsnB1 as Being Responsible for meso-Diaminopimelic Acid Amidation in Lactobacillus plantarum Peptidoglycan

机译：酰胺转移酶AsnB1的鉴定是负责植物乳杆菌肽聚糖中-二氨基庚二酸酰胺化。

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摘要

The peptidoglycan (PG) of Lactobacillus plantarum contains amidated meso-diaminopimelic acid (mDAP). The functional role of this PG modification has never been characterized in any bacterial species, except for its impact on PG recognition by receptors of the innate immune system. In silico analysis of loci carrying PG biosynthesis genes in the L. plantarum genome revealed the colocalization of the murE gene, which encodes the ligase catalyzing the addition of mDAP to UDP-N-muramoyl-d-glutamate PG precursors, with asnB1, which encodes a putative asparagine synthase with an N-terminal amidotransferase domain. By gene disruption and complementation experiments, we showed that asnB1 is the amidotransferase involved in mDAP amidation. PG structural analysis revealed that mDAP amidation plays a key role in the control of the l,d-carboxypeptidase DacB activity. In addition, a mutant strain with a defect in mDAP amidation is strongly affected in growth and cell morphology, with filamentation and cell chaining, while a DacB-negative strain displays a phenotype very similar to that of a wild-type strain. These results suggest that mDAP amidation may play a critical role in the control of the septation process.
机译：植物乳杆菌的肽聚糖（PG）含有酰胺化的 meso -二氨基庚二酸（mDAP）。除了对先天免疫系统受体对PG识别的影响之外，这种PG修饰的功能作用从未在任何细菌中得到鉴定。在植物乳杆菌基因组中携带PG生物合成基因的基因座的 Insilico 分析表明， murE 基因在共定位中，该基因编码连接酶，将mDAP添加到UDP- < em> N -muramoyl-d-谷氨酸PG前体，带有 asnB1 ，其编码带有N末端酰胺基转移酶结构域的假定的天冬酰胺合酶。通过基因破坏和互补实验，我们发现 asnB1 是参与mDAP酰胺化的酰胺转移酶。 PG结构分析表明，mDAP酰胺化在控制1，d-羧肽酶DacB活性中起关键作用。此外，具有mDAP酰胺化缺陷的突变株在生长和细胞形态上受到丝状化和细胞链的强烈影响，而DacB阴性株表现出与野生株非常相似的表型。这些结果表明，mDAP酰胺化可能在分隔过程的控制中起关键作用。

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