The maintenance of protein homeostasis is ensured by a proteostasis network consisting of molecular chaperones, trafficking factors and proteases. This network ensures the functionality of proteins and prevents the accumulation of misfolded protein species. It becomes particularly important under stress conditions that affect the structural integrity of proteins. Bacteria constantly and most directly face severe changes in environmental growth conditions. Adapting to such stress situations by repairing or removing damaged proteins not only ensures survival of bacteria, but also enables them to stay competitive when fighting with other microorganisms for limited resources. Stress management is also crucial for pathogenic bacteria during host colonization and when fighting host defense mechanisms. Targeting bacterial protein homeostasis is therefore considered as a novel anti-bacterial strategy.
The aim of the Research topic is to broadly cover novel insights in the bacterial proteostasis research field, ranging from the mechanisms of chaperone and protease activities to their roles as potential drug targets in treatment of infectious diseases. The topic will cover the basic physiological processes assisted by protein quality control factors and how the diverse proteostasis pathways are interlinked. It will highlight recent advances describing structures and dynamics of protein quality factors made possible by cryo-EM and NMR spectroscopy. It will also describe how bacteria can sense diverse stress conditions, enabling them to trigger specific stress responses, but also to integrate this information to additionally control basic cellular processes. Finally, the topic will illustrate how recent advances in understanding bacterial proteostasis opens new avenues in biotechnology and medicine. Together these topics aim at providing a comprehensive description of bacterial proteostasis strategies and networks that can serve as prime example for understanding cellular adaptations to stress conditions.
Areas to be covered by original work or review articles may include, but are not limited to:
• general proteostasis strategies of bacteria, including folding and trafficking of newly synthesized proteins, degradation of misfolded proteins and formation and removal of protein aggregates
• mechanisms of bacterial stress resistance(s)
• coupling stress conditions to the control of house keeping processes by quality control factors
• regulation of bacterial stress responses
• structures and mechanisms of bacterial chaperones and proteases
• role of protein quality control factors in bacterial virulence
• targeting proteostasis as novel anti-bacterial strategy
• applications of bacterial protein quality control factors in biotechnology and bacterial production factories
A full list of accepted article types including descriptions can be found at this
linkThe cover image for this Research Topic is used with permission of the authors and publishers of the following article: Winkler J, Seybert A, König L, Pruggnaller S, Haselmann U, Sourjik V, Weiss M, Frangakis AS, Mogk A, Bukau B.EMBO J. 2010 Mar 3;29(5):910-23. doi: 10.1038/emboj.2009.412. Epub 2010 Jan 21The maintenance of protein homeostasis is ensured by a proteostasis network consisting of molecular chaperones, trafficking factors and proteases. This network ensures the functionality of proteins and prevents the accumulation of misfolded protein species. It becomes particularly important under stress conditions that affect the structural integrity of proteins. Bacteria constantly and most directly face severe changes in environmental growth conditions. Adapting to such stress situations by repairing or removing damaged proteins not only ensures survival of bacteria, but also enables them to stay competitive when fighting with other microorganisms for limited resources. Stress management is also crucial for pathogenic bacteria during host colonization and when fighting host defense mechanisms. Targeting bacterial protein homeostasis is therefore considered as a novel anti-bacterial strategy.
The aim of the Research topic is to broadly cover novel insights in the bacterial proteostasis research field, ranging from the mechanisms of chaperone and protease activities to their roles as potential drug targets in treatment of infectious diseases. The topic will cover the basic physiological processes assisted by protein quality control factors and how the diverse proteostasis pathways are interlinked. It will highlight recent advances describing structures and dynamics of protein quality factors made possible by cryo-EM and NMR spectroscopy. It will also describe how bacteria can sense diverse stress conditions, enabling them to trigger specific stress responses, but also to integrate this information to additionally control basic cellular processes. Finally, the topic will illustrate how recent advances in understanding bacterial proteostasis opens new avenues in biotechnology and medicine. Together these topics aim at providing a comprehensive description of bacterial proteostasis strategies and networks that can serve as prime example for understanding cellular adaptations to stress conditions.
Areas to be covered by original work or review articles may include, but are not limited to:
• general proteostasis strategies of bacteria, including folding and trafficking of newly synthesized proteins, degradation of misfolded proteins and formation and removal of protein aggregates
• mechanisms of bacterial stress resistance(s)
• coupling stress conditions to the control of house keeping processes by quality control factors
• regulation of bacterial stress responses
• structures and mechanisms of bacterial chaperones and proteases
• role of protein quality control factors in bacterial virulence
• targeting proteostasis as novel anti-bacterial strategy
• applications of bacterial protein quality control factors in biotechnology and bacterial production factories
A full list of accepted article types including descriptions can be found at this
linkThe cover image for this Research Topic is used with permission of the authors and publishers of the following article: Winkler J, Seybert A, König L, Pruggnaller S, Haselmann U, Sourjik V, Weiss M, Frangakis AS, Mogk A, Bukau B.EMBO J. 2010 Mar 3;29(5):910-23. doi: 10.1038/emboj.2009.412. Epub 2010 Jan 21