System-wide analyses reveal essential roles of N-terminal protein modification in bacterial membrane integrity
Chien‐I Yang, Zikun Zhu, Jeffrey J. Jones, Brett Lomenick, Tsui‐Fen Chou, Shu‐ou Shan
Abstract
translatome and proteome to investigate the consequences of PDF inhibition. Loss of PDF activity rapidly induces cellular stress responses, especially those associated with protein misfolding and membrane defects, followed by a global down-regulation of metabolic pathways. Rapid membrane hyperpolarization and impaired membrane integrity were observed shortly after PDF inhibition, suggesting that the plasma membrane disruption is the most immediate and primary consequence of formyl group retention on nascent proteins. This work resolves the physiological function of a ubiquitous protein modification and uncovers its crucial role in maintaining the structure and function of the bacterial membrane.