Overview of protein phosphorylation in bacteria with a main focus on unusual protein kinases in Bacillus subtilis

Zhang, Ao; Pompeo, Frédérique; Galinier, Anne

doi:10.1016/j.resmic.2021.103871

Cited by 6 publications

(3 citation statements)

References 79 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“… 2021 , Zhang et al . 2021 ). As we shall discuss here, the Arg-phosphoproteome provides a major clue to elucidate molecular pathways succeeding the activation of the Ger-receptors.…”

Section: Introduction: Entering and Exiting Dormancymentioning

confidence: 99%

Reviving the view: evidence that macromolecule synthesis fuels bacterial spore germination

et al. 2022

View full text Add to dashboard Cite

The Gram positive bacterium Bacillus subtilis and its relatives are capable of forming a durable dormant long-lasting spore. Although spores can remain dormant for years, they possess the remarkable capacity to rapidly resume life and convert into actively growing cells. This cellular transition initiates with a most enigmatic irreversible event, termed germination, lasting only for a few minutes. Germination is typified by a morphological conversion that culminates in loss of spore resilient properties. Yet, the molecular events occurring during this brief critical phase are largely unknown. The current widely accepted view considers germination to occur without the need for any macromolecule synthesis; however, accumulating data from our laboratory and others, highlighted here, provide evidence that both transcription and translation occur during germination and are required for its execution. We further underline numerous overlooked studies, conducted mainly during the 1960s-70s, reinforcing this notion. We propose to revisit the fascinating process of spore germination and redefine it as a pathway involving macromolecule synthesis. We expect our perspective to shed new light on the awakening process of a variety of spore-forming environmental, commensal and pathogenic bacteria and possibly be applicable to additional organisms displaying a quiescent life form.

show abstract

“… 2021 , Zhang et al . 2021 ). As we shall discuss here, the Arg-phosphoproteome provides a major clue to elucidate molecular pathways succeeding the activation of the Ger-receptors.…”

Section: Introduction: Entering and Exiting Dormancymentioning

confidence: 99%

Reviving the view: evidence that macromolecule synthesis fuels bacterial spore germination

et al. 2022

View full text Add to dashboard Cite

show abstract

“… 33 Protein phosphorylation affects the protein activity by adding phosphate moieties on relevant amino acids. 34 In bacterial species, protein kinases and phosphatases play an important role in host–pathogen interactions through phosphorylation of key molecules. 35 In this regard, phosphorylation can indicate functionally active proteins, which is vital to understanding the metabolic state of the organism at the time of the experiment.…”

Section: Discussionmentioning

confidence: 99%

“…Phosphorylations of serine, threonine, and tyrosine are well-known bacterial transcriptional regulators that regulate gene expression and signal transduction signaling networks . Protein phosphorylation affects the protein activity by adding phosphate moieties on relevant amino acids . In bacterial species, protein kinases and phosphatases play an important role in host–pathogen interactions through phosphorylation of key molecules .…”

Section: Discussionmentioning

confidence: 99%

Unique Posttranslational Modification Sites of Acetylation, Citrullination, Glutarylation, and Phosphorylation Are Found to Be Specific to the Proteins Partitioned in the Triton X-114 Fractions of Leptospira

et al. 2022

View full text Add to dashboard Cite

Posttranslational modifications (PTMs) are decisive factors in the structure, function, and localization of proteins in prokaryotic and eukaryotic organisms. However, prokaryotic organisms lack subcellular organelles, and protein localization based on subcellular locations like cytoplasm, inner membrane, periplasm, and outer membrane can be accounted for functional characterization. We have identified 131 acetylated, 1182 citrullinated, 72 glutarylated, 5 palmitoylated, and 139 phosphorylated proteins from Triton X-114 fractionated proteins of Leptospira , the pathogen of re-emerging zoonotic disease leptospirosis. In total, 74.7% of proteins were found exclusively in different Triton X-114 fractions. Additionally, 21.9% of proteins in multiple fractions had one or more PTM specific to different Triton X-114 fractions. Altogether, 96.6% of proteins showed exclusiveness to different Triton X-114 fractions either due to the presence of the entire protein or with a specific PTM type or position. Further, the PTM distribution within Triton X-114 fractions showed higher acetylation in aqueous, glutarylation in detergent, phosphorylation in pellet, and citrullination in wash fractions representing cytoplasmic, outer membrane, inner membrane, and extracellular locations, respectively. Identification of PTMs in proteins with respect to the subcellular localization will help to characterize candidate proteins before developing novel drugs and vaccines rationally to combat leptospirosis.

show abstract

Post-translational modifications in bacteria – The dynamics of bacterial physiology

Chapot‐Chartier

Buddelmeijer

2021

Research in Microbiology

View full text Add to dashboard Cite

Overview of protein phosphorylation in bacteria with a main focus on unusual protein kinases in Bacillus subtilis

Cited by 6 publications

References 79 publications

Reviving the view: evidence that macromolecule synthesis fuels bacterial spore germination

Reviving the view: evidence that macromolecule synthesis fuels bacterial spore germination

Unique Posttranslational Modification Sites of Acetylation, Citrullination, Glutarylation, and Phosphorylation Are Found to Be Specific to the Proteins Partitioned in the Triton X-114 Fractions of Leptospira

Post-translational modifications in bacteria – The dynamics of bacterial physiology

Contact Info

Product

Resources

About