Phosphorylation of the integrase protein of coliphage HK022

Kolot, Mikhail; Gorovits, Rena; Silberstein, Nava; Fichtman, Boris; Yagil, Ezra

doi:10.1016/j.virol.2008.02.011

Cited by 19 publications

(25 citation statements)

References 43 publications

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“…While the small plaques and lower adsorption rate of the JACS-K mutant initially suggested that a single phosphorylation event is not optimal for infection to occur, the results for ⌽X174-100/101/102 suggest that additional conversion sites do not increase plaque size or adsorption rate. While lambda has several tyrosine residues that are phosphorylated during the lysogenic pathway, controlling the specific timing of cell lysis (13), it benefits by encoding a protein kinase that can autophosphorylate as well as dephosphorylate, allowing lambda to balance the lysogenization rate with its own growth rate (13). ⌽X174 does not encode a kinase, limiting its control of E. coli K-12 lysis.…”

Section: Vol 84 2010 Notes 4861mentioning

confidence: 99%

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confidence: 99%

“…Thus, the JACS-K mutant, in contrast with the JACS strain, has a very reactive threonine on its virion surface which can readily have its terminal hydroxyl group phosphorylated (13). In a recent study, it was found that the E. coli K-12 infecting coliphages HK022 and lambda are phosphorylated at one or more of their tyrosine residues (13), and the penetration of E. coli K-12 by these phages is dependent on the energy supplied by phosphorylation (1). To verify if indeed the phosphorylation of the new residue on the JACS-K mutant surface was responsible for the mutant's ability to infect E. coli K-12, analogous to the means in which HK022 and lambda infect this same host, we inhibited phosphorylation using carbonyl cyanide m-chlorophenylhydrazone (CCCP).…”

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Mechanisms Responsible for a ΦX174 Mutant's Ability To InfectEscherichia coliby Phosphorylation

Cox

Putonti

2010

J Virol

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The ability for a virus to expand its host range is dependent upon a successful mode of viral entry. As such, the host range of the well-studied ΦX174 bacteriophage is dictated by the presence of a particular lipopolysaccharide (LPS) on the bacterial surface. The mutant ΦX174 strain JACS-K, unlike its ancestor, is capable of infecting both its native host Escherichia coli C and E. coli K-12, which does not have the necessary LPS. The conversion of an alanine to a very reactive threonine on its virion surface was found to be responsible for the strain's expanded host range.

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Section: Vol 84 2010 Notes 4861mentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Mechanisms Responsible for a ΦX174 Mutant's Ability To InfectEscherichia coliby Phosphorylation

Cox

Putonti

2010

J Virol

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“…For example, Escherichia coli Wzc and Bacillus subtilis PtkA BY-kinases were found to phosphorylate UDP-glucose dehydrogenase enzymes (4,5), EpsD from Streptococcus thermophilus (6) and Wzc of Klebsiella pneumoniae (7) were found to phosphorylate the undecaprenylphosphate glycosyltransferases EpsE and WcaJ, respectively, and Cap5B2 from Staphylococcus aureus was found to phosphorylate the UDP-acetyl-mannosamine dehydrogenase Cap5O (8). In addition, BY-kinases have been demonstrated to have other cellular targets not related to polysaccharide biosynthesis, as is the case for the E. coli alternative heat shock sigma factor RpoH and the RpoE anti-sigma factor RseA (9), integrase proteins (Int) of coliphage HK022 (10), and single-stranded DNA-binding proteins SsbA and SsbB from Bacillus subtilis (11). Besides the genetic and biochemical analyses of individual targets of BY-kinases reported above, other bacterial tyrosine-phosphorylated proteins have been identified by gel-free proteomics approaches in organisms such as E. coli (12), B. subtilis (13,14), Listeria monocytogenes (15), Streptococcus pneumoniae (16), and Pseudomonas species (17), to name a few.…”

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Comparative Transcriptomic Analysis of the Burkholderia cepacia Tyrosine Kinase bceF Mutant Reveals a Role in Tolerance to Stress, Biofilm Formation, and Virulence

Ferreira

Silva

Oliveira

et al. 2013

Appl Environ Microbiol

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The bacterial tyrosine-kinase (BY-kinase) family comprises the major group of bacterial enzymes endowed with tyrosine kinase activity. We previously showed that the BceF protein from Burkholderia cepacia IST408 belongs to this BY-kinase family and is involved in the biosynthesis of the exopolysaccharide cepacian. However, little is known about the extent of regulation of this protein kinase activity. In order to examine this regulation, we performed a comparative transcriptome profile between the bceF mutant and wild-type B. cepacia IST408. The analyses led to identification of 630 genes whose expression was significantly changed. Genes with decreased expression in the bceF mutant were related to stress response, motility, cell adhesion, and carbon and energy metabolism. Genes with increased expression were related to intracellular signaling and lipid metabolism. Mutation of bceF led to reduced survival under heat shock and UV light exposure, reduced swimming motility, and alteration in biofilm architecture when grown in vitro. Consistent with some of these phenotypes, the bceF mutant demonstrated elevated levels of cyclic-di-GMP. Furthermore, BceF contributed to the virulence of B. cepacia for larvae of the Greater wax moth, Galleria mellonella. Taken together, BceF appears to play a considerable role in many cellular processes, including biofilm formation and virulence. As homologues of BceF occur in a number of pathogenic and plant-associated Burkholderia strains, the modulation of bacterial behavior through tyrosine kinase activity is most likely a widely occurring phenomenon. Bacterial tyrosine kinases (BY-kinases) are best characterized for regulating the biosynthesis and the export of bacterial extracellular carbohydrate polymers in both Gram-positive and Gram-negative bacteria. These proteins comprise two domains: a transmembrane activator domain with a large extracellular loop and an intracellular catalytic domain encompassing the ATPbinding site and tyrosine-rich region (1). These two domains can either be linked in a single polypeptide, such as in Proteobacteria and Actinobacteria, or split into two separate proteins encoded by adjacent genes, as in the Firmicutes (1). Resolution of the BYkinase tridimensional structures showed no resemblance to their mammalian counterparts, and therefore these proteins are seen as good targets for antibacterial drug design (2).A number of studies have shown the importance of BY-kinases in polysaccharide biosynthesis, mainly as components of a multienzymatic complex responsible for polysaccharide polymerization and export (3). Moreover, several enzymes involved in sugarnucleotide biosynthesis and repeat unit formation have also been identified as phosphorylation targets of BY-kinases. For example, Escherichia coli Wzc and Bacillus subtilis PtkA BY-kinases were found to phosphorylate UDP-glucose dehydrogenase enzymes (4, 5), EpsD from Streptococcus thermophilus (6) and Wzc of Klebsiella pneumoniae (7) were found to phosphorylate the undecaprenylphosphate glycosyltransf...

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“…In E. coli, the BY-kinase Wzc was found to phosphorylate integrase proteins (Int) of coliphages HK022 and . Overexpression of Wzc in tyrosinephosphatase deficient background resulted in a significantly reduced lysogenization, indicating that phosphorylation of Int down-regulates its activity [30]. Following the finding that heat shock response in E. coli is modulated by the activity of the BY-kinase Etk [19], a link between tyrosine phosphorylation and heat shock was also published for B. subtilis.…”

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confidence: 94%