An amino-terminal secretion signal is required for YplA export by the Ysa, Ysc, and flagellar type III secretion systems of Yersinia enterocolitica biovar 1B.
An amino-terminal secretion signal is required for YplA export by the Ysa, Ysc, and flagellar type III secretion systems of Yersinia enterocolitica biovar 1B.
复制标题
小肠结肠炎耶尔森菌生物变种 1B 的 Ysa、Ysc 和鞭毛 III 型分泌系统输出 YplA 需要氨基末端分泌信号。
DOI：
10.1128/jb.187.17.6075-6083.2005
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发表时间：
2005
影响因子：
3.2
通讯作者：
Young,GlennM
中科院分区：
文献类型：
--
作者：
Warren,SashaM;Young,GlennM
小肠结肠炎耶尔森氏菌 1B 维持三个不同的 III 型分泌 (TTS) 系统，这些系统独立运作，将蛋白质靶向细胞外位点。 Ysa 和 Ysc 系统是典型的接触依赖性 TTS 系统，在感染过程中将毒性效应物转移到目标真核宿主细胞的胞质溶胶中。鞭毛 TTS 系统在鞭毛组装过程中被利用，并且是毒力相关磷脂酶 YplA 分泌到细菌环境所必需的。当异位产生时，YplA 也是 Ysa 和 Ysc TTS 系统的分泌底物。在本研究中，我们定义了允许 Ysa、Ysc 和鞭毛 TTS 系统识别和输出 YplA 的元素。 YplA的各个氨基末端区域与缺乏其天然分泌信号的大肠杆菌碱性磷酸酶(PhoA)的融合证明YplA的前20个氨基酸或相应的mRNA密码子足以通过每个TTS系统输出YplA-PhoA嵌合体。还发现三个 TTS 系统中的每一个系统输出的天然 YplA 都取决于其氨基末端的完整性。编码氨基末端20个残基的ypl序列的移码突变或缺失的引入对YplA分泌产生负面影响。 otherypA区域的缺失是可以容忍的，包括导致多肽的氨基酸残基30至40的去除和mRNA的5'非翻译区域的去除。这项工作支持一个模型，其中 Y 的独立且远程相关的 TTS 系统。小肠结肠炎通过类似的机制识别蛋白质底物。
Yersinia enterocoliticabiovar 1B maintains three distinct type III secretion (TTS) systems, which independently operate to target proteins to extracellular sites. The Ysa and Ysc systems are prototypical contact-dependent TTS systems that translocate toxic effectors to the cytosols of targeted eukaryotic host cells during infection. The flagellar TTS system is utilized during the assembly of the flagellum and is required for secretion of the virulence-associated phospholipase YplA to the bacterial milieu. When ectopically produced, YplA is also a secretion substrate for the Ysa and Ysc TTS systems. In this study, we define elements that allow YplA recognition and export by the Ysa, Ysc, and flagellar TTS systems. Fusion of various amino-terminal regions of YplA toEscherichia colialkaline phosphatase (PhoA) lacking its native secretion signal demonstrated that the first 20 amino acids or corresponding mRNA codons of YplA were sufficient for export of YplA-PhoA chimeras by each TTS system. Export of native YplA by each of the three TTS systems was also found to depend on the integrity of its amino terminus. Introduction of a frameshift mutation or deletion ofyplAsequences encoding the amino-terminal 20 residues negatively impacted YplA secretion. Deletion of otheryplAregions was tolerated, including that resulting in the removal of amino acid residues 30 through 40 of the polypeptide and removal of the 5′ untranslated region of the mRNA. This work supports a model in which independent and distantly related TTS systems ofY. enterocoliticarecognize protein substrates by a similar mechanism.