Monnet V
Unité de Biochimie et Structure des Protéines, Institut National de la Recherche Agronomique, 78352 Jouy en Josas, France.
Cell Mol Life Sci. 2003 Oct;60(10):2100-14. doi: 10.1007/s00018-003-3054-3.
This review focuses on bacterial oligopeptide-binding proteins, which form part of the oligopeptide transport system belonging to the ATP-binding cassette family of transporters. Depending on the bacterial species, these binding proteins (OppA) capture peptides ranging in size from 2 to 18 amino acids from the environment and pass them on to the other components of the oligopeptide transport system for internalisation. Bacteria have developed several strategies to produce these binding proteins, which are periplasmic in Gram- bacteria and membrane-anchored in Gram+, with a higher stoichiometry (probably necessary for efficient transport) than the other components in the transport system. The expression of OppA-encoding genes is clearly modulated by external factors, especially nitrogen compounds, but the mechanisms of regulation are not always clear. The best-understood roles played by OppAs are internalisation of peptides for nutrition and recycling of muropeptides. It has, however, recently become clear that OppAs are also involved in sensing the external medium via specific or non-specific peptides.
本综述聚焦于细菌寡肽结合蛋白，它们是属于ATP结合盒转运蛋白家族的寡肽转运系统的一部分。根据细菌种类的不同，这些结合蛋白（OppA）从环境中捕获大小为2至18个氨基酸的肽，并将它们传递给寡肽转运系统的其他组分以便内化。细菌已开发出多种策略来产生这些结合蛋白，它们在革兰氏阴性菌中位于周质，在革兰氏阳性菌中锚定在膜上，其化学计量比高于转运系统中的其他组分（这可能是高效转运所必需的）。OppA编码基因的表达明显受到外部因素的调节，尤其是氮化合物，但调节机制并不总是清楚的。OppA所发挥的最广为人知的作用是肽的营养内化和胞壁肽的循环利用。然而，最近已明确OppA也通过特异性或非特异性肽参与感知外部介质。
