Research Topic

Bacterial Post-Translational Modifications

About this Research Topic

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


Keywords: Acetylation, Phosphorylation, Acylation, Succinylation, PTM


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

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


Keywords: Acetylation, Phosphorylation, Acylation, Succinylation, PTM


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

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Submission Deadlines

31 July 2021 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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Topic Editors

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Submission Deadlines

31 July 2021 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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