The Chemical Biology of Protein Phosphorylation

Tarrant, Mary Katherine; Cole, Philip A.

doi:10.1146/annurev.biochem.78.070907.103047

Cited by 206 publications

(193 citation statements)

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“…In a typical phosphorylation event, a protein kinase transfers the γ-phosphate from ATP to specific amino acids of a protein to initiate signal transduction; in eukaryotes, these phosphorylated amino acids are usually Ser, Thr, and Tyr residues (3,4). In contrast, His/Asp-based phospho-relay of two-component systems has been well recognized as a classic mode of signal transduction in the bacterial world (5).…”

mentioning

confidence: 99%

Protein cysteine phosphorylation of SarA/MgrA family transcriptional regulators mediates bacterial virulence and antibiotic resistance

Sun

Ding

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

161

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Protein posttranslational modifications (PTMs), particularly phosphorylation, dramatically expand the complexity of cellular regulatory networks. Although cysteine (Cys) in various proteins can be subject to multiple PTMs, its phosphorylation was previously considered a rare PTM with almost no regulatory role assigned. We report here that phosphorylation occurs to a reactive cysteine residue conserved in the staphylococcal accessary regulator A (SarA)/MarR family global transcriptional regulator A (MgrA) family of proteins, and is mediated by the eukaryotic-like kinase-phosphatase pair Stk1-Stp1 in Staphylococcus aureus. Cys-phosphorylation is crucial in regulating virulence determinant production and bacterial resistance to vancomycin. Cell wall-targeting antibiotics, such as vancomycin and ceftriaxone, inhibit the kinase activity of Stk1 and lead to decreased Cys-phosphorylation of SarA and MgrA. An in vivo mouse model of infection established that the absence of stp1, which results in elevated protein Cys-phosphorylation, significantly reduces staphylococcal virulence. Our data indicate that Cys-phosphorylation is a unique PTM that can play crucial roles in bacterial signaling and regulation.

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mentioning

confidence: 99%

Protein cysteine phosphorylation of SarA/MgrA family transcriptional regulators mediates bacterial virulence and antibiotic resistance

Sun

Ding

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

161

170

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“…The performance of NiZnFe 2 O 4 has also been compared with other approaches including TiO 2 27-30 , Fe 3 þ -IMAC 31 and HAP (hydroxyapatite) 32,33 (Supplementary Note 2; Supplementary Table S2). These materials can bind with both mono-and multi-phosphorylated peptides without selectivity ( Supplementary Fig.…”

Section: Resultsmentioning

confidence: 99%

“…R eversible protein phosphorylation is an important regulatory mechanism for prokaryotic and eukaryotic cells 1,2 . Cycles of phosphorylation and dephosphorylation cause conformational changes in structures of many enzymes and receptors and also function as electrostatic switches to modulate the on and off states of many signalling pathways [3][4][5] .…”

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confidence: 99%

Mass spectrometric analysis of mono- and multi-phosphopeptides by selective binding with NiZnFe2O4 magnetic nanoparticles

et al. 2013

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Selective isolation of mono-and multi-phosphorylated peptides is important for understanding how a graded protein kinase or phosphatase signal can precisely modulate the on and off states of signal transduction pathways. Here we report that metal ions at exposed octahedral sites of nano-ferrites, including Fe 3 O 4 , NiFe 2 O 4 , ZnFe 2 O 4 and NiZnFe 2 O 4 , have distinctly selective coordination abilities with mono-and multi-phosphopeptides. Due to their intrinsic magnetic properties and high surface area to volume ratios, these nanoparticles enable the rapid isolation of mono-and multi-phosphopeptides by an external magnetic field. Model phosphoprotein a-casein and two synthesized mono-and di-phosphopeptides have been chosen for proof-of-principle demonstrations, and these nanoparticles have also been applied to phosphoproteome profiling of zebrafish eggs. It is shown that NiZnFe 2 O 4 is highly selective for multi-phosphopeptides. In contrast, Fe 3 O 4 , NiFe 2 O 4 and ZnFe 2 O 4 can bind with both mono-and multi-phosphopeptides with relatively stronger affinity towards monophosphopeptides.

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“…[80][81][82] If one embraces Julian's idea of antibiotics as mediators of cell-cell communication, it is interesting also to consider aminoglycoside phosphotransferases potentially serving as modulators of such signaling pathways-much as kinases that act on key regulatory proteins can profoundly alter cellular and developmental signaling networks. [83][84][85][86] Julian's challenge to us, to rethink just what roles antibiotics may play in Nature, illustrates yet once again his creativity, his clarity of thought, his biochemical and evolutionary insights, and why it was such an immense pleasure and privilege to work with him in Geneva and Madison some four decades ago.…”

Section: Aminoglycosides Sequence Relationships Of Their Phosphotranmentioning

confidence: 99%

Julian Davies and the discovery of kanamycin resistance transposon Tn5

Berg

2016

J Antibiot

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This paper recounts some of my fond memories of a collaboration between Julian Davies and myself that started in 1974 in Geneva and that led to our serendipitous discovery of the bacterial kanamycin resistance transposon Tn5, and aspects of the lasting positive impact of our interaction and discovery on me and the community. Tn5 was one of the first antibiotic resistance transposons to be found. Its analysis over the ensuing decades provided valuable insights into mechanisms and control of transposition, and led to its use as a much-valued tool in diverse areas of molecular genetics, as also will be discussed here. The Journal of Antibiotics (2017) 70, 339-346; doi:10.1038/ja.2016.120; published online 12 October 2016 BACKGROUND It was wonderfully educational, productive and exciting for me to work with Julian Davies for a few years in the mid 1970s, doing experiments that led to the serendipitous discovery and initial characterizations of kanamycin resistance transposon Tn5 1 -one of the first and most useful of the many bacterial antibiotic resistance (AR) transposons that have been found. 2 I was inspired by Julian's knowledge of mechanisms of antibiotic action and resistance mechanisms, his creativity and clarity of thought and expression, as illustrated in his numerous papers, 3-6 and by his high energy, kindness and inventive good humor-traits that have enriched the lives and careers of many people over the years. Described here, in tribute to Julian and his special character, are my memories of a collaboration that led to Tn5's unexpected discovery, Tn5's properties, and some lasting impacts of our collaboration on the field and on me personally.We began interacting in 1974, soon after Julian arrived in Geneva to begin his sabbatical with Pierre Francois Spahr (Department of Molecular Biology of the University). 7 I was then in my fourth (final) year as Chargé de Recherche (senior postdoc) in Lucien Caro's group in the same department, studying λdv plasmids, often in collaboration with Grete Kellenberger-Gujer, also in Lucien's group 8-13 -and during these years, also hugely enjoying features in and out of the lab that have drawn researchers to Geneva for decades: a superb scientific atmosphere, year-round easy access to the exquisite Alps and Jura mountains, and the language, cuisine and culture of Geneva and vicinity. I had become intrigued the year before by Julian's ideas about origins and evolution of resistance genes, as described in his paper with Raoul Benveniste. 14 They advanced the then-novel theory that the types of bacteria that had provided life saving antibiotics were also the ancestral sources of AR genes that were becoming increasingly common in human and veterinary pathogens. Their inferences were

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The Chemical Biology of Protein Phosphorylation

Cited by 206 publications

References 163 publications

Protein cysteine phosphorylation of SarA/MgrA family transcriptional regulators mediates bacterial virulence and antibiotic resistance

Protein cysteine phosphorylation of SarA/MgrA family transcriptional regulators mediates bacterial virulence and antibiotic resistance

Mass spectrometric analysis of mono- and multi-phosphopeptides by selective binding with NiZnFe2O4 magnetic nanoparticles

Julian Davies and the discovery of kanamycin resistance transposon Tn5

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