Regulatory interactions involving the proteins of the phosphotransferase system in enteric bacteria

Saier, Milton H.

doi:10.1002/jcb.240510112

Cited by 50 publications

(37 citation statements)

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“…The PTS consists of a protein phosphoryl transfer chain including two energy coupling proteins or protein domains, enzyme I and HPr, as well as the sugar-specific proteins, enzymes II (29). The PTS also functions in several regulatory capacities (1,25,26,30). In gram-positive bacteria, HPr is phosphorylated by an ATP-dependent, fructose-1,6-bisphosphate (FBP)-activated kinase on a seryl residue, serine 46, as well as by the PEPdependent, enzyme I-catalyzed reaction which derivatizes a histidyl residue, histidine 15 (14,18).…”

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Presence of protein constituents of the gram-positive bacterial phosphotransferase regulatory system in Acholeplasma laidlawii

et al. 1993

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Acholeplasma species have been reported to lack a functional phosphoenolpyruvate:sugar phosphotransferase system (PTS). We show here that Acholeplasma laidlawii possesses activities of enzyme I, HPr, HPr(ser) kinase, and HPr(ser-P) phosphatase but lacks detectable activities of enzymes II of the PTS. HPr from this organism was purified, and the regulatory properties of the kinase and phosphatase were characterized and shown to differ from those of previously studied bacteria. The results suggest the presence of an incomplete PTS in A. laidlawii which has the potential to function in a unique regulatory capacity.

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Presence of protein constituents of the gram-positive bacterial phosphotransferase regulatory system in Acholeplasma laidlawii

et al. 1993

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“…These have crr homologues as part of sugar-specific enzyme IIABC permeases that solely appear to fulfil transport function (F. Titgemeyer, unpublished data; [30][31][32]). For Gramnegative species a multiple role of IIA Glc has been documented and proposed [9,13,14,29].…”

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confidence: 99%

“…It appears that glucose kinase serves a global regulatory function, but how it senses and transmits carbon source signals is unclear. It has been demonstrated that IIA Glc of E. coli senses C-regulatory signals from both PTS and non-PTS carbon sources and responds via its phosphorylation state [9,13]. It would be of great interest to examine whether IIA Crr of S. coelicolor operates in a similar way.…”

Section: Discussionmentioning

confidence: 99%

“…At the same time the cellular cAMP level is low, because dephosphorylated IIA Glc is unable to stimulate adenylate cyclase. Under these conditions the cAMPdependent catabolite activator protein CAP, which serves as a global activator of many catabolite-controlled genes, remains in a switched off state [9]. IIA Glc further appears to be involved in carbon catabolite repression exerted by non-PTS substrates such as glucose 6-phosphate [13].…”

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“…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 ).…”

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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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Response regulators of bacterial signal transduction systems: Selective domain shuffling during evolution

1995

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Response regulators of bacterial sensory transduction systems generally consist of receiver module domains covalently linked to effector domains. The effector domains include DNA binding and/or catalytic units that are regulated by sensor kinase-catalyzed aspartyl phosphorylation within their receiver modules. Most receiver modules are associated with three distinct families of DNA binding domains, but some are associated with other types of DNA binding domains, with methylated chemotaxis protein (MCP) demethylases, or with sensor kinases. A few exist as independent entities which regulate their target systems by noncovalent interactions. In this study the molecular phylogenies of the receiver modules and effector domains of 49 fully sequenced response regulators and their homologues were determined. The three major, evolutionarily distinct, DNA binding domains found in response regulators were evaluated for their phylogenetic relatedness, and the phylogenetic trees obtained for these domains were compared with those for the receiver modules. Members of one family (family 1) of DNA binding domains are linked to large ATPase domains which usually function cooperatively in the activation of E. coli sigma 54-dependent promoters or their equivalents in other bacteria. Members of a second family (family 2) always function in conjunction with the E. coli sigma 70 or its equivalent in other bacteria. A third family of DNA binding domains (family 3) functions by an uncharacterized mechanism involving more than one sigma factor. These three domain families utilize distinct helix-turn-helix motifs for DNA binding. The phylogenetic tree of the receiver modules revealed three major and several minor clusters of these domains. The three major receiver module clusters (clusters 1, 2, and 3) generally function with the three major families of DNA binding domains (families 1, 2, and 3, respectively) to comprise three classes of response regulators (classes 1, 2, and 3), although several exceptions exist. The minor clusters of receiver modules were usually, but not always, associated with other types of effector domains. Finally, several receiver modules did not fit into a cluster. It was concluded that receiver modules usually diverged from common ancestral protein domains together with the corresponding effector domains, although domain shuffling, due to intragenic splicing and fusion, must have occurred during the evolution of some of these proteins. Multiple sequence alignments of the 49 receiver modules and their various types of effector domains, together with other homologous domains, allowed definition of regions of striking sequence similarity and degrees of conservation of specific residues. Sequence data were correlated with structure/function when such information was available.(ABSTRACT TRUNCATED AT 250 WORDS)

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Regulatory interactions involving the proteins of the phosphotransferase system in enteric bacteria

Cited by 50 publications

References 36 publications

Presence of protein constituents of the gram-positive bacterial phosphotransferase regulatory system in Acholeplasma laidlawii

Presence of protein constituents of the gram-positive bacterial phosphotransferase regulatory system in Acholeplasma laidlawii

The phosphotransferase system of Streptomyces coelicolor

Response regulators of bacterial signal transduction systems: Selective domain shuffling during evolution

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