The PASTA domain of penicillin-binding protein SpoVD is dispensable for endospore cortex peptidoglycan assembly in Bacillus subtilis
The PASTA domain of penicillin-binding protein SpoVD is dispensable for endospore cortex peptidoglycan assembly in Bacillus subtilis
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DOI：
10.1099/mic.0.000011
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发表时间：
2015-02-01
期刊：
影响因子：
2.8
通讯作者：
Hederstedt, Lars
中科院分区：
文献类型：
--
作者：
Bukowska-Faniband, Ewa;Hederstedt, Lars
肽聚糖是细菌细胞壁的主要结构成分。青霉素结合蛋白（PBP）位于细胞质膜外部，在肽聚糖合成和重塑中发挥重要作用。在多种细菌中的一些 PBP 和类真核蛋白丝氨酸/苏氨酸激酶的 C 末端发现了约 65 个残基的 PASTA 结构域（青霉素结合蛋白和丝氨酸/苏氨酸激酶相关结构域）。 PASTA 结构域的功能尚不清楚，但其中一些被认为可以结合非交联的肽聚糖。枯草芽孢杆菌有 16 种不同的 PBP，但其中只有 2 个（Pbp2b 和 SpoVD）包含 PASTA 结构域。 SpoVD 对孢子形成具有特异性，并且对于内生孢子皮层肽聚糖的合成至关重要。我们通过删除 PASTA 结构域并分析其对内生孢子形成和 SpoVD 亚细胞定位的影响，研究了 PASTA 结构域在 SpoVD 中的作用。我们的结果表明，SpoVD 中的 PASTA 结构域对于皮层合成不是必需的，对于在孢子形成过程中将 SpoVD 靶向前孢子外膜也不重要。
Peptidoglycan is the major structural component of the bacterial cell wall. Penicillin-binding proteins (PBPs), located at the exterior of the cytoplasmic membrane, play a major role in peptidoglycan synthesis and remodelling. A PASTA domain (penicillin-binding protein and serine/threonine kinase associated domain) of about 65 residues is found at the C-terminal end of some PBPs and eukaryotic-like protein serine/threonine kinases in a variety of bacteria. The function of PASTA domains is not understood, but some of them are thought to bind uncross linked peptidoglycan. Bacillus subtilis has 16 different PBPs, but only 2 of them, Pbp2b and SpoVD, contain a PASTA domain. SpoVD is specific for sporulation and essential for endospore cortex peptidoglycan synthesis. We have studied the role of the PASTA domain in SpoVD by deleting this domain and analysing the effects on endospore formation and subcellular localization of SpoVD. Our results demonstrate that the PASTA domain in SpoVD is not essential for cortex synthesis and not important for targeting SpoVD to the forespore outer membrane during sporulation.