Modification of the side chains of critical amino acids in proteins may have important consequences, such as regulation of activity or stability, and influencing protein-protein interactions, protein conformation, or subcellular localization. Within the past 20 years, it has been appreciated that post-translational modifications (PTMs) are widespread among bacteria, contrary to the original thought that it was a rare phenomenon. Currently, there are thousands of identified PTMs, including acetylation, phosphorylation, and succinylation, distributed among hundreds of proteins. However, the biological significance of the majority of such modifications remains unknown. Moreover, the mechanisms of control of these processes are not completely understood.
With the current availability of catalogs of modified proteins in bacteria generated from large-scale mass spectrometry-based proteomics studies, we must now turn our attention to understanding the underlying function and purpose of these modifications. In order to completely understand these processes, we must identify and characterize all of the important regulatory elements. Bacterial PTMs can be challenging to study, due to their relatively low stoichiometry, and inherently unstable nature. Thus, new methodologies and tools to study these modifications are required. Finally, we are only beginning to discover the breadth of bacterial PTMs, and the possibility remains that novel modifications are waiting to be discovered.
This research topic focuses on studies (including original research, methods, perspectives, review, and commentaries) that explore and discuss:
· The physiological significance of bacterial PTMs (such as phosphorylation, acylation, methylation, etc.)
· The identification or characterization of novel bacterial PTMs
· The identification or characterization of novel enzymes involved in controlling PTMs
· Exploration of non-enzymatic mechanisms of lysine acylations, or other PTMs
· Development of new methodology or tools to study bacterial PTMs
Modification of the side chains of critical amino acids in proteins may have important consequences, such as regulation of activity or stability, and influencing protein-protein interactions, protein conformation, or subcellular localization. Within the past 20 years, it has been appreciated that post-translational modifications (PTMs) are widespread among bacteria, contrary to the original thought that it was a rare phenomenon. Currently, there are thousands of identified PTMs, including acetylation, phosphorylation, and succinylation, distributed among hundreds of proteins. However, the biological significance of the majority of such modifications remains unknown. Moreover, the mechanisms of control of these processes are not completely understood.
With the current availability of catalogs of modified proteins in bacteria generated from large-scale mass spectrometry-based proteomics studies, we must now turn our attention to understanding the underlying function and purpose of these modifications. In order to completely understand these processes, we must identify and characterize all of the important regulatory elements. Bacterial PTMs can be challenging to study, due to their relatively low stoichiometry, and inherently unstable nature. Thus, new methodologies and tools to study these modifications are required. Finally, we are only beginning to discover the breadth of bacterial PTMs, and the possibility remains that novel modifications are waiting to be discovered.
This research topic focuses on studies (including original research, methods, perspectives, review, and commentaries) that explore and discuss:
· The physiological significance of bacterial PTMs (such as phosphorylation, acylation, methylation, etc.)
· The identification or characterization of novel bacterial PTMs
· The identification or characterization of novel enzymes involved in controlling PTMs
· Exploration of non-enzymatic mechanisms of lysine acylations, or other PTMs
· Development of new methodology or tools to study bacterial PTMs
