A Lipid‐Anchored Binding Protein is a Component of an ATP‐Dependent Cellobiose/Cellotriose‐Transport System from the Cellulose Degrader <i>Streptomyces reticuli</i>

Schlösser, Andreas; Schrempf, Hildgund

doi:10.1111/j.1432-1033.1996.0332r.x

Cited by 62 publications

(91 citation statements)

References 51 publications

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“…The S. reticuli system has been extensively characterized. Genes cebEFG are induced by cellobiose, the encoded permease is a high-affinity uptake system for cellobiose and cellotriose, and since a cebE mutation abolishes this function, this ceb operon is the only system for these substrates (41). A palindromic sequence of 18 bp was found 128 bp upstream of both cebE1 and cebE2.…”

Section: Resultsmentioning

confidence: 99%

“…BLAST searches with the ceb genes of S. reticuli revealed two similar gene loci, ceb1 and ceb2, within the S. coelicolor genome with an identical gene order, cebREFGbglC⍀shl, and 47 to 66% identical proteins (exception, Shl1 and Shl2 with 11% identity) among each other ( Fig. 2A and B) (41). Both gene clusters encode a divergently transcribed regulator, CebR of the LacI family, a sugar-binding protein, CebE, two integral membrane proteins, CebF and CebG, the ␤-glucosidase BglC, and a putative sugar hydrolase, Shl.…”

Section: Resultsmentioning

confidence: 99%

“…When we started our analysis, there was only one ABC-type carbohydrate permease, MalEFG, described for S. coelicolor that transports maltodextrins and maltose (44,57). As a first step in the identification of further permeases, we screened the genome for the presence of such systems that were described for other Streptomyces species (18,39,41,42,59,64). This led to the identification of genes for two potential cellobiose-and cellotriose-specific permeases, ceb1 and ceb2, two potential ␤-xyloside-specific permeases, bxl1 and bxl2, two putative gene clusters that could account for uptake of ␣-glucosides, agl1 and agl2, and a gene locus containing genes for two adjacent ABC systems, one of which has been shown to translocate N-acetylglucosamine and chitobiose ( Fig.…”

Section: Resultsmentioning

confidence: 99%

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In Silico and Transcriptional Analysis of Carbohydrate Uptake Systems of Streptomyces coelicolor A3(2)

et al. 2004

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Streptomyces coelicolor is the prototype for the investigation of antibiotic-producing and differentiating actinomycetes. As soil bacteria, streptomycetes can metabolize a wide variety of carbon sources and are hence vested with various specific permeases. Their activity and regulation substantially determine the nutritional state of the cell and, therefore, influence morphogenesis and antibiotic production. We have surveyed the genome of S. coelicolor A3(2) to provide a thorough description of the carbohydrate uptake systems. Among 81 ATP-binding cassette (ABC) permeases that are present in the genome, we found 45 to encode a putative solute binding protein, an essential feature for carbohydrate permease function. Similarity analysis allowed the prediction of putative ABC systems for transport of cellobiose and cellotriose, ␣-glucosides, lactose, maltose, maltodextrins, ribose, sugar alcohols, xylose, and ␤-xylosides. A novel putative bifunctional protein composed of a substrate binding and a membrane-spanning moiety is likely to account for ribose or ribonucleoside uptake. Glucose may be incorporated by a proton-driven symporter of the major facilitator superfamily while a putative sodium-dependent permease of the solute-sodium symporter family may mediate uptake of galactose and a facilitator protein of the major intrinsic protein family may internalize glycerol. Of the predicted gene clusters, reverse transcriptase PCRs showed active gene expression in 8 of 11 systems. Together with the previously surveyed permeases of the phosphotransferase system that accounts for the uptake of fructose and N-acetylglucosamine, the genome of S. coelicolor encodes at least 53 potential carbohydrate uptake systems.Streptomycetes represent a major fraction of the bacterial soil population (20). They contribute substantially to carbon recycling by degrading a whole variety of biopolymers that stem from dead plant and animal material (16). These organic compounds, which include xylan, chitin, and cellulose, are broken down by exoenzymes. The products are funneled into the cell by specific carbohydrate importers that usually recognize mono-and disaccharides. The recent publication of the genome of the model organism Streptomyces coelicolor A3(2) revealed two interesting features concerning carbon utilization (7), that is, (i) a huge number of 172 genes encoding secreted proteins, such as hydrolases, chitinases, cellulases, lipases, nucleases, and proteases, and (ii) the occurrence of 81 ATPbinding cassette (ABC) permeases that are possibly used for the uptake of sugars, oligopeptides, and nucleosides as well as for drug export (46, 56). The numerousness of exoenzymes and ABC systems is 5-to 10-fold higher than that of other bacteria, underlining the broad metabolic capacity of streptomycetes (7).Canonical carbohydrate-specific ABC systems in gram-positive bacteria are oligoprotein assemblies: a membrane-anchored substrate-binding protein is exposed to the outside of the cell, scavenging for a specific substrate molecule (10) (Fi...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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In Silico and Transcriptional Analysis of Carbohydrate Uptake Systems of Streptomyces coelicolor A3(2)

et al. 2004

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“…MsiK could therefore be a potential candidate for regulation by IIA Crr . Initial attempts to demonstrate IIA Crr -MsiK binding by surface plasmon resonance failed probably because overproduced MsiK forms inclusion bodies yielding incorrectly folded protein (unpublished data) [37].…”

Section: Discussionmentioning

confidence: 99%

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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“…In some instances, the inducing substrate has been shown to be taken up into the cell by ABC transporters such as those encoded by the cebEFG operon for the cellobiose/cellotriose uptake of Streptomyces reticuli (Schlo¨sser et al 1999), by the malEFG operon for the uptake of maltose and maltodextrin by S. coelicolor (van Wezel et al 1997) or S. lividans (Schlo¨sser et al 2001) or by the ngcEFG operon for the import of N-acetylglucosamine and chitobiose by S. olivaceoviridis (Xiao et al 2002). Some of these transporters share a common energy provider, the ATPase MsiK (Hurtubise et al 1995), the gene for which is not linked to the transport operon (Schlo¨sser et al 1997(Schlo¨sser et al , 1999. MsiK has been shown to be involved in the transport of numerous disaccharides including xylobiose, cellobiose, maltose and trehalose (Hurtubise et al 1995;Schlo¨sser et al 1997;Schlo¨sser 2000).…”

Section: Introductionmentioning

confidence: 99%

Site-directed mutagenesis of conserved inverted repeat sequences in the xylanase C promoter region from Streptomyces sp. EC3

et al. 2003

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A Lipid‐Anchored Binding Protein is a Component of an ATP‐Dependent Cellobiose/Cellotriose‐Transport System from the Cellulose Degrader Streptomyces reticuli

Cited by 62 publications

References 51 publications

In Silico and Transcriptional Analysis of Carbohydrate Uptake Systems of Streptomyces coelicolor A3(2)

In Silico and Transcriptional Analysis of Carbohydrate Uptake Systems of Streptomyces coelicolor A3(2)

The phosphotransferase system of Streptomyces coelicolor

Site-directed mutagenesis of conserved inverted repeat sequences in the xylanase C promoter region from Streptomyces sp. EC3

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