Protein Kinase Associated with Ribosomes Phosphorylates Ribosomal Proteins ofStreptomyces collinus

Mikulı́k, Karel; Janda, Ivan

doi:10.1006/bbrc.1997.7297

Cited by 12 publications

(14 citation statements)

References 21 publications

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“…We have shown previously that ribosomes of S. collinus associate with protein kinase activity that phosphorylates 11 ribosomal proteins (Mikulík and Janda, 1997). In the large subunits seven phosphoproteins were detected L2, L3, L7, L16, L21, L23, and L27.…”

mentioning

confidence: 84%

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

Mikulı́k¹,

Suchan²,

Bobek³

2001

Biochemical and Biophysical Research Communications

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confidence: 84%

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

Mikulı́k¹,

Suchan²,

Bobek³

2001

Biochemical and Biophysical Research Communications

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“…The extracts were combined with 2ϫ SDS sample buffer (2,36), and 30 l of each extract was loaded onto the wells for SDS-PAGE. To isolate membrane proteins from cytoplasmic and ribosomal fractions, we used a modification of the procedure of Mikulik and Janda (44). One milliliter of the starter culture (4-day culture in SpM) was inoculated into 50 ml of SpM.…”

Section: Methodsmentioning

confidence: 99%

Identification and Characterization of a Developmentally Regulated Protein, EshA, Required for Sporogenic Hyphal Branches in Streptomyces griseus

et al. 2001

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To identify sporulation-specific proteins that might serve as targets of developmental regulatory factors in Streptomyces, we examined total proteins of Streptomyces griseus by two-dimensional gel electrophoresis. Among five proteins that were present at high levels during sporulation but absent from vegetative cells, two of the proteins, P3 and P4, were absent from developmental mutants that undergo aberrant morphogenesis. The deduced amino acid sequence of the gene that encodes P3 (EshA) showed extensive similarity to proteins from mycobacteria and a cyanobacterium, Synechococcus, that are abundant during nutritional stress but whose functions are unknown. Uniquely among these proteins, EshA contains a cyclic nucleotide-binding domain, suggesting that the activity of EshA may be modulated by a cyclic nucleotide. The eshA gene was strongly expressed from a single transcription start site only during sporulation, and accumulation of the eshA transcript depended on a developmental gene, bldA. During submerged sporulation, a null mutant strain that produced no EshA could not extend sporogenic hyphae from new branch points but instead accelerated septation and spore maturation at the preexisting vegetative filaments. These results indicated that EshA is required for the growth of sporogenic hyphae and localization of septation and spore maturation but not for spore viability.Streptomyces is a gram-positive bacterium that undergoes morphological differentiation. In a nutritionally favorable condition, Streptomyces spores germinate to give rise to vegetative hyphae, which are characterized by filamentous, multigenomic cells called mycelia. Sporulation begins by the growth of aerial hyphae (or sporogenic hyphae when the sporulation process is induced in liquid culture; 34), which subsequently undergo septation to form chains of unicellular spores. We previously identified two types of sporogenic hyphae during sporulation of Streptomyces griseus (22): we suggest the term "distal" sporogenic hyphae for those that grow from the tips of preexisting vegetative filaments and the term "proximal" sporogenic hyphae for those that grow de novo within the vegetative hyphae at the onset of sporulation. Since both vegetative growth and spore formation are inherently polar processes similar to those observed in yeast and filamentous fungi (18), formation of sporogenic hyphae in Streptomyces is likely to require proteins that direct the location of sporogenic hyphae, establishment of polarity, and emergence of the sporogenic hyphae.To understand the molecular details of Streptomyces sporulation, researchers have identified developmental genes primarily by complementation of nonsporulating mutants. Most of the sporulation-specific genes that have been characterized appear to encode regulatory functions. Some, such as bldA, which encodes tRNA (38), are required for the production of aerial hyphae (35, 43) and antibiotics (3, 34, 43). Genes that specifically regulate spore formation include the whi genes, so named because mutations in ...

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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

322

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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Protein Kinase Associated with Ribosomes Phosphorylates Ribosomal Proteins ofStreptomyces collinus

Cited by 12 publications

References 21 publications

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

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

Identification and Characterization of a Developmentally Regulated Protein, EshA, Required for Sporogenic Hyphal Branches in Streptomyces griseus

Eukaryote-Like Serine/Threonine Kinases and Phosphatases in Bacteria

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