The bacterial septal ring protein RlpA is a lytic transglycosylase that contributes to rod shape and daughter cell separation in Pseudomonas aeruginosa.

The bacterial septal ring protein RlpA is a lytic transglycosylase that contributes to rod shape and daughter cell separation in Pseudomonas aeruginosa.
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细菌隔环蛋白RLPA是一种裂解的乳糖基化酶,在铜绿假单胞菌中有助于杆状形状和子细胞分离。

DOI:
10.1111/mmi.12643
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发表时间:
2014-07
影响因子:
3.6
通讯作者:
Weiss DS
Weiss DS
中科院分区:
生物学2区
文献类型:
--
作者:
Jorgenson MA;Chen Y;Yahashiri A;Popham DL;Weiss DS

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稀有脂蛋白A(RlpA)是一种功能未知的广泛保守的外膜蛋白,以前只在大肠杆菌中研究过,它定位于隔环和沿着侧壁的散在病灶,但突变体没有表型变化。在这里,我们显示铜绿假单胞菌的rlpA突变体形成短链,脂肪细胞生长在低渗透强度介质。这些形态学缺陷表明RlpA是有效分离子细胞和维持杆状所必需的。来自rlpA缺失突变体的肽聚糖囊的分析揭示了缺乏茎肽的四糖和六糖(下文称为“裸聚糖”)增加。将这些球囊与纯化的RlpA孵育导致释放含有1,6-脱水N-乙酰胞壁酸末端的裸聚糖。RlpA不降解来自野生型细胞的球囊,除非球囊用酰胺酶进行有限消化以除去一些茎肽。因此,RlpA是对裸聚糖链具有强烈偏好的裂解性转糖基酶。我们建议,RlpA活性调节在体内的底物的可用性,和酰胺酶和RlpA串联工作,以降解肽聚糖的分裂隔膜和侧壁。
Rare lipoprotein A (RlpA) is a widely-conserved outer membrane protein of unknown function that has previously only been studied in Escherichia coli, where it localizes to the septal ring and scattered foci along the lateral wall, but mutants have no phenotypic change. Here we show rlpA mutants of Pseudomonas aeruginosa form chains of short, fat cells when grown in low osmotic strength media. These morphological defects indicate RlpA is needed for efficient separation of daughter cells and maintenance of rod shape. Analysis of peptidoglycan sacculi from an rlpA deletion mutant revealed increased tetra and hexasaccharides that lack stem peptides (hereafter called “naked glycans”). Incubation of these sacculi with purified RlpA resulted in release of naked glycans containing 1,6-anhydro N-acetylmuramic acid ends. RlpA did not degrade sacculi from wild-type cells unless the sacculi were subjected to a limited digestion with an amidase to remove some of the stem peptides. Thus, RlpA is a lytic transglycosylase with a strong preference for naked glycan strands. We propose that RlpA activity is regulated in vivo by substrate availability, and that amidases and RlpA work in tandem to degrade peptidoglycan in the division septum and lateral wall.
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