Changes in Ribosome Function Induced by Protein Kinase Associated with Ribosomes of Streptomyces collinus Producing Kirromycin

Mikulı́k, Karel; Suchan, Petr; Bobek, Jan

doi:10.1006/bbrc.2001.6017

Cited by 14 publications

(17 citation statements)

References 38 publications

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“…Importantly, EF-Tu phosphorylation inhibited binding to amino-acylated tRNA and to kirromycin, an antibiotic that inhibits the elongation step of translation by preventing the release of EF-Tu-GDP from the ribosome (5). For Streptomyces collinus, a ribosomeassociated kinase was reported to phosphorylate several ribosomal proteins on Ser and Thr residues, which led to a significant reduction in protein synthesis (104,105). Finally, Ser/Thr phosphorylation of a number of other ribosomal and ribosome-associated proteins has been observed in phylogenetically diverse bacteria by use of phosphoproteomic methodologies (17,97,125,142,156,171,174).…”

Section: Estks In Bacteriamentioning

confidence: 99%

Eukaryote-Like Serine/Threonine Kinases and Phosphatases in Bacteria

Pereira

Goss

Dworkin

2011

Microbiol Mol Biol Rev

327

348

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SUMMARY Genomic studies have revealed the presence of Ser/Thr kinases and phosphatases in many bacterial species, although their physiological roles have largely been unclear. Here we review bacterial Ser/Thr kinases (eSTKs) that show homology in their catalytic domains to eukaryotic Ser/Thr kinases and their partner phosphatases (eSTPs) that are homologous to eukaryotic phosphatases. We first discuss insights into the enzymatic mechanism of eSTK activation derived from structural studies on both the ligand-binding and catalytic domains. We then turn our attention to the identified substrates of eSTKs and eSTPs for a number of species and to the implications of these findings for understanding their physiological roles in these organisms.

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Section: Estks In Bacteriamentioning

confidence: 99%

Eukaryote-Like Serine/Threonine Kinases and Phosphatases in Bacteria

Pereira

Goss

Dworkin

2011

Microbiol Mol Biol Rev

327

348

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“…The kinase Pkn14 of Myxococcus xanthus , on the other hand, is involved in growth and development via phosphorylation of transcriptional regulators []. Phosphorylation of ribosomal proteins has been shown to be involved in the regulation of translation in Streptomyces collinus []. Lastly, coordinated phosphorylation and dephosphorylation by protein kinases and phosphatases, respectively, have been shown to play critical roles in the cell wall architecture and cell division in Staphylococcus aureus [].…”

Section: Introductionmentioning

confidence: 99%

Close proximity of phosphorylation sites to ligand in the phosphoproteome of the extreme thermophile Thermus thermophilusHB8

et al. 2012

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We performed phosphoproteome analysis of proteins from the extremely thermophilic Gram-negative eubacterium Thermus thermophilus HB8 using gel-free mass spectrometric method. We identified 52 phosphopeptides from 48 proteins and determined 46 phosphorylation sites: 30 on serine, 12 on threonine, and 4 on tyrosine. The identified phosphoproteins are known to be involved in a wide variety of cellular processes. To help elucidate the functional roles of these phosphorylation events, we mapped the phosphorylation sites on the known tertiary structures of the respective proteins. In all, we succeeded in mapping 46 sites (approximately 88%) on the corresponding structures. Most of the phosphorylation sites were found to be located on loops and terminal regions of the secondary structures. Surprisingly, 28 of these sites were situated at or near the active site of the enzyme. In particular, 18 sites were within 4 Å of the ligand, including substrate or cofactor. Such structural locations suggest direct effects of the phosphorylation on the binding of ligand in addition to inducing a conformational change. Interestingly, 19 of these 28 phosphorylation sites were situated near the phosphate moiety of a substrate or cofactor. In oligomeric proteins, 5 phosphorylation sites were found at the subunit interface. Based on these results, we propose a regulatory mechanism that involves Ser/Thr/Tyr phosphorylation in T. thermophilus HB8.

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“…In addition to regulation of protein function, phosphorylation could also serve as a molecular switch for conformational changes during protein synthesis on the ribosome. In two earlier in vitro phosphorylation studies on E. coli and Streptomyces collinus ribosomes, the ribosomal proteins phosphorylated by a protein kinase from rabbit skeletal muscle and a protein kinase associated with the ribosomes were identified, respectively 13,14 . E. coli ribosomal proteins S4, S9, S18, S19, L2, L3, L5, L7/L12, L10, and L33 were found to be phosphorylated by the protein kinase from rabbit skeletal muscle at their Ser and Thr residues13 and S. collinus ribosomal proteins S3, S4, S12, S13, S14, S18, L2, L7/L12, L16, L17, and L23 were determined to be Ser and Thr phosphorylated by the protein kinase associated with the ribosomes 15.…”

Section: Introductionmentioning

confidence: 99%

Comprehensive Analysis of Phosphorylated Proteins of Escherichia coli Ribosomes

et al. 2009

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Phosphorylation of bacterial ribosomal proteins has been known for decades; however, there is still very limited information available on specific locations of the phosphorylation sites in ribosomal proteins and the role they might play in protein synthesis. In this study, we have mapped the specific phosphorylation sites in twenty-four E. coli ribosomal proteins by tandem mass spectrometry. Specific detection of phosphorylation was achieved by either phosphorylation specific visualization techniques, ProQ staining and antibodies for phospho-Ser, Thr, and Tyr, or by mass spectrometry equipped with a capability to detect addition and the loss of the phosphate moiety. Enrichment by immobilized metal affinity and/or strong cation exchange chromatography was used to improve the success of detection of the low abundance phosphopeptides. We found the small subunit (30S) proteins S3, S4, S5, S7, S11, S12, S13, S18, and S21 and the large subunit (50S) proteins L1, L2, L3, L5, L6, L7/L12, L13, L14, L16, L18, L19, L21, L22, L28, L31 to be phosphorylated at one or more residues. Potential roles for each specific site in ribosome function were deduced through careful evaluation of the given site of the phosphorylation in 3D-crystal structure models of ribosomes and the previous mutational studies of E. coli ribosomal proteins.

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Changes in Ribosome Function Induced by Protein Kinase Associated with Ribosomes of Streptomyces collinus Producing Kirromycin

Cited by 14 publications

References 38 publications

Eukaryote-Like Serine/Threonine Kinases and Phosphatases in Bacteria

Eukaryote-Like Serine/Threonine Kinases and Phosphatases in Bacteria

Close proximity of phosphorylation sites to ligand in the phosphoproteome of the extreme thermophile Thermus thermophilusHB8

Comprehensive Analysis of Phosphorylated Proteins of Escherichia coli Ribosomes

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