Protein-protein interactions and the spatiotemporal dynamics of bacterial outer membrane proteins.
Protein-protein interactions and the spatiotemporal dynamics of bacterial outer membrane proteins.
复制标题
DOI：
10.1016/j.sbi.2015.10.007
复制
发表时间：
2015-12
影响因子：
6.8
通讯作者：
Baumann CG
中科院分区：
文献类型：
--
作者：
Kleanthous C;Rassam P;Baumann CG
我们讨论细菌外膜的时空模式。外膜蛋白之间混杂的相互作用控制着它们的行为。外膜蛋白的周转和生物发生与簇的形成有关。讨论了时空模式对细菌生理学的影响。直到最近，人们还不清楚革兰氏阴性细菌的外膜蛋白（OMP）是否是随机组织或分布的。现在的研究表明，大肠杆菌中β-桶OMP之间混杂的蛋白质-蛋白质相互作用（PPIs）控制着它们的局部和整体动态，使外膜的时空模式形成微域，并且是β-桶蛋白质周转的基础。我们将这些最新进展置于背景下，推测可能受到 OMP 组织成超分子组装体影响的细菌细胞生物学领域，并强调这种修正的细菌外膜观点提出的新问题和争议。
We discuss spatiotemporal patterning in the bacterial outer membrane. Promiscuous interactions between outer membrane proteins govern their behaviour. Turnover and biogenesis of outer membrane proteins linked to formation of clusters. Implications of spatiotemporal patterning for bacterial physiology discussed. It has until recently been unclear whether outer membrane proteins (OMPs) of Gram-negative bacteria are organized or distributed randomly. Studies now suggest promiscuous protein–protein interactions (PPIs) between β-barrel OMPs in Escherichia coli govern their local and global dynamics, engender spatiotemporal patterning of the outer membrane into micro-domains and are the basis of β-barrel protein turnover. We contextualize these latest advances, speculate on areas of bacterial cell biology that might be influenced by the organization of OMPs into supramolecular assemblies, and highlight the new questions and controversies this revised view of the bacterial outer membrane raises.