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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
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Reciprocal Regulation of PASTA Kinase Signaling by Differential Modification.

Benjamin D Labbe1, Cherisse L Hall1, Stephanie L Kellogg1

  • 1Department of Microbiology and Immunology, Center for Infectious Disease Research, Medical College of Wisconsin-Milwaukee, Milwaukee, Wisconsin, USA.

Journal of Bacteriology
|March 13, 2019
PubMed
Summary

Phosphorylation of the bacterial PASTA kinase IreK at distinct sites reciprocally regulates its activity, impacting antimicrobial resistance in Enterococcus faecalis. This study reveals novel mechanisms for bacterial adaptation to cell wall stress.

Keywords:
PASTA kinaseantimicrobial resistancecell wall stressregulatory phosphorylation

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Area of Science:

  • Bacterial physiology and molecular biology
  • Enzyme regulation and signal transduction
  • Antibiotic resistance mechanisms

Background:

  • Transmembrane Ser/Thr kinases with PASTA domains are crucial in bacteria, regulating processes like antibiotic resistance and cell division.
  • PASTA kinases are known to autophosphorylate, but the functional roles of phosphorylation at different sites and deactivation mechanisms remain unclear.
  • The PASTA kinase IreK in Enterococcus faecalis is essential for intrinsic resistance to antimicrobials.

Purpose of the Study:

  • To identify and functionally characterize multiple phosphorylation sites on the Enterococcus faecalis PASTA kinase, IreK.
  • To elucidate the role of distinct phosphorylation sites in regulating IreK activity and antimicrobial resistance.
  • To understand the mechanisms of IreK deactivation in response to environmental stimuli.

Main Methods:

  • Identification of phosphorylation sites on IreK using in vivo and in vitro approaches.
  • Functional analysis of identified phosphorylation sites through mutation studies in Enterococcus faecalis.
  • Assessment of IreK activity and antimicrobial resistance levels under various conditions.

Main Results:

  • Phosphorylation of the IreK activation loop is essential for kinase activity.
  • Phosphorylation at a site distinct from the activation loop reciprocally modulates IreK activity, reducing kinase function and antimicrobial resistance.
  • This distinct phosphorylation site is critical for IreK deactivation upon removal of the activating stimulus.

Conclusions:

  • Distinct phosphorylation sites on IreK reciprocally regulate its activity, providing a mechanism for adaptation to cell wall stresses.
  • Phosphorylation plays a dual role in IreK regulation: activation via the activation loop and deactivation via a separate site.
  • These findings offer new insights into the complex regulation of PASTA kinases, relevant to antibiotic resistance and bacterial physiology.