Identification and characterization of phosphoenolpyruvate: fructose phosphotransferase systems in three Streptomyces species

Titgemeyer, Fritz; Walkenhorst, J.; Reizer, Jonathan; Stuiver, Maarten H.; Cui, Xuewen; Saier, Milton H.

doi:10.1099/00221287-141-1-51

Cited by 63 publications

(49 citation statements)

References 56 publications

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“…100,101 In S. coelicolor, there are at least four PTS transporters, all of which use the universal PTS energy-coupling enzymes enzyme I (EI, encoded by ptsI) and HPr (encoded by ptsH). [102][103][104] Two of the transporters have been characterized in detail, and are responsible for the transport of D-fructose and N-acetylglucosamine. 102,105 Glucose is not transported by the PTS, but through the specific GlcP permease, which is probably the main reason why PTS is not involved in glucose repression.…”

Section: Streptomycesmentioning

confidence: 99%

“…[102][103][104] Two of the transporters have been characterized in detail, and are responsible for the transport of D-fructose and N-acetylglucosamine. 102,105 Glucose is not transported by the PTS, but through the specific GlcP permease, which is probably the main reason why PTS is not involved in glucose repression. 106 Recently, a pleiotropic effect of N-acetylglucosamine (GlcNAc) uptake on development and production of the blue-pigmented polyketide antibiotic actinorhodin has been reported in S. coelicolor.…”

Section: Streptomycesmentioning

confidence: 99%

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Carbon source regulation of antibiotic production

et al. 2010

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Section: Streptomycesmentioning

confidence: 99%

Section: Streptomycesmentioning

confidence: 99%

Carbon source regulation of antibiotic production

et al. 2010

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“…Therefore, it should act as a PTS phosphotransferase. With respect to carbon source transport, it seems to be clear that IIA Crr is not an enzyme IIA Glc as streptomycetes appear to lack the glucose-specific PTS [15,17]. An analysis of the S. coelicolor genome revealed two loci, malX2-nagE1-nagE2 and malX1 2 , that encode PTS permeases of the glucose/ sucrose family [17,33].…”

Section: Discussionmentioning

confidence: 99%

“…This could be correlated with the variation of the phosphorylation state of IIA Glc . Recently, another cellular function for IIA Glc has been proposed that suggests that it may be involved in the linkage between carbon metabolism and stress response [14].We have described that the PTS is operative in streptomycetes [15,16]. Analysis of the S. coelicolor genome revealed the presence of nine genes that may encode four sugar-specific permeases, as well as the genes ptsH and ptsI Correspondence to F. Titgemeyer, Friedrich-Alexander-Universita¨t Erlangen-Nu¨rnberg, Lehrstuhl fu¨r Mikrobiologie, Staudtstrasse 5, 91058 Erlangen, Germany.…”

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The phosphotransferase system of Streptomyces coelicolor

Kamionka

Parche

Nothaft

et al. 2002

European Journal of Biochemistry

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We have investigated the crr gene of Streptomyces coelicolor that encodes a homologue of enzyme IIA Glucose of Escherichia coli, which, as a component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) plays a key role in carbon regulation by triggering glucose transport, carbon catabolite repression, and inducer exclusion. As in E. coli, the crr gene of S. coelicolor is genetically associated with the ptsI gene that encodes the general phosphotransferase enzyme I. The gene product IIA Crr was overproduced, purified, and polyclonal antibodies were obtained. Western blot analysis revealed that IIA Crr is expressed in vivo. The functionality of IIA Crr was demonstrated by phosphoenolpyruvate-dependent phosphorylation via enzyme I and the histidine-containing phosphoryl carrier protein HPr. Phosphorylation was abolished when His72, which corresponds to the catalytic histidine of E. coli IIA Glucose , was mutated. The capacity of IIA Crr to operate in sugar transport was shown by complementation of the E. coli glucose-PTS. The striking functional resemblance between IIA Crr and IIA Glucose was further demonstrated by its ability to confer inducer exclusion of maltose to E. coli. A specific interaction of IIA Crr with the maltose permease subunit MalK from Salmonella typhimurium was uncovered by surface plasmon resonance. These data suggest that this IIA Glucose -like protein may be involved in carbon metabolism in S. coelicolor.Keywords: inducer exclusion; protein phosphorylation; protein-protein interaction; Streptomyces; surface plasmon resonance.Streptomycetes undergo global changes in gene expression and enzyme activities in response to developmental stages, secondary metabolite production (antibiotics), carbon utilization, and stress conditions [1][2][3][4][5]. The focus of our research is the regulation of carbon source utilization (C-regulation) and how this influences the other abovementioned processes.Streptomyces coelicolor metabolizes a wide variety of nutrients. Their utilization is subject to C-regulation, in which glucose kinase appears to be of significant importance [6,7]. However, the signal transduction pathways are poorly understood. In many other bacteria, components of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) trigger C-regulation by mechanisms known as carbon catabolite repression and inducer exclusion [8,9]. One key element in Escherichia coli is enzyme IIA Glucose (IIA Glc ). IIA Glc becomes phosphorylated by the general PTS proteins, which are histidine-containing phosphoryl carrier protein (HPr) and enzyme I (EI). In turn, it phosphorylates the sugar-specific PTS permeases that catalyse the uptake of glucose, trehalose, and sucrose [8,10,11]. Mutations in the respective gene crr exhibit a pleiotropic catabolite repression resistant phenotype [12]. The underlying mechanisms are that unphosphorylated IIA Glc inhibits a set of catabolic enzymes and sugar permeases including the MalK subunit of the maltose permease by protein-protein interac...

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Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase

Jarling

Cauvet

Grundmeier

et al. 2004

J. Basic Microbiol.

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The gene mak1FN coding for maltokinase from Actinoplanes missouriensis is located in a cluster similar to glycogen metabolism clusters identified in Streptomyces coelicolor. Sequence comparisons demonstrate that mak1-related genes coding for homologous proteins are present in many bacterial genomes including taxonomic distantly related groups such as Rhodospirillales or green sulfur bacteria. More than 50% of the aligned sequences are longer than the mak1 gene from A. missouriensis, and the N-terminal portion of these putative maltokinases exhibit high sequence homologies with trehalose synthases. A more detailed sequence comparison indicates a relationship of maltokinases to aminoglycoside phospho-transferases and protein kinases. Transformation of S. lividans with plasmid vectors containing either the mak1 gene from A. missouriensis or the pep2 gene from S. coelicolor resulted in recombinant strains, which produced measurable amounts of maltokinase activity. The proteins Pep2 and Mak1 were over expressed with Streptomyces lividans 66 as a heterologous host and further characterized. The possible physiological function of maltokinases is discussed.

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Identification and characterization of phosphoenolpyruvate: fructose phosphotransferase systems in three Streptomyces species

Cited by 63 publications

References 56 publications

Carbon source regulation of antibiotic production

Carbon source regulation of antibiotic production

The phosphotransferase system of Streptomyces coelicolor

Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase

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