ExbBD-Dependent Transport of Maltodextrins through the Novel MalA Protein across the Outer Membrane of<i>Caulobacter crescentus</i>

Neugebauer, Heidi; Herrmann, Christina; Kammer, Winfried; Schwarz, Gerold; Nordheim, Alfred; Braun, Volkmar

doi:10.1128/jb.187.24.8300-8311.2005

Cited by 100 publications

(144 citation statements)

References 65 publications

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“…Some species (such as Xanthomonas and Caulobacter) contain multiple copies of the chiP-II genes that are mostly controlled by NAG-dependent regulators. One of 67 hypothetical TonB-dependent receptors encoded in the C. crescentus genome was shown to be involved in the TonB-ExbBD-dependent uptake of maltodextrins (43). This allowed us to suggest a similar mechanism for the ChiP-II-mediated uptake of chito-oligosaccharides.…”

Section: Chitin Degradation and Uptake To The Periplasmmentioning

confidence: 73%

Comparative Genomics and Experimental Characterization of N-Acetylglucosamine Utilization Pathway of Shewanella oneidensis

Yang

Rodionov

et al. 2006

Journal of Biological Chemistry

126

154

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We used a comparative genomics approach implemented in the SEED annotation environment to reconstruct the chitin and GlcNAc utilization subsystem and regulatory network in most proteobacteria, including 11 species of Shewanella with completely sequenced genomes. Comparative analysis of candidate regulatory sites allowed us to characterize three different GlcNAc-specific regulons, NagC, NagR, and NagQ, in various proteobacteria and to tentatively assign a number of novel genes with specific functional roles, in particular new GlcNAc-related transport systems, to this subsystem. Genes SO3506 and SO3507, originally annotated as hypothetical in Shewanella oneidensis MR-1, were suggested to encode novel variants of GlcN-6-P deaminase and GlcNAc kinase, respectively. Reconstitution of the GlcNAc catabolic pathway in vitro using these purified recombinant proteins and GlcNAc-6-P deacetylase (SO3505) validated the entire pathway. Kinetic characterization of GlcN-6-P deaminase demonstrated that it is the subject of allosteric activation by GlcNAc-6-P. Consistent with genomic data, all tested Shewanella strains except S. frigidimarina, which lacked representative genes for the GlcNAc metabolism, were capable of utilizing GlcNAc as the sole source of carbon and energy. This study expands the range of carbon substrates utilized by Shewanella spp., unambiguously identifies several genes involved in chitin metabolism, and describes a novel variant of the classical three-step biochemical conversion of GlcNAc to fructose 6-phosphate first described in Escherichia coli.

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Section: Chitin Degradation and Uptake To The Periplasmmentioning

confidence: 73%

Comparative Genomics and Experimental Characterization of N-Acetylglucosamine Utilization Pathway of Shewanella oneidensis

Yang

Rodionov

et al. 2006

Journal of Biological Chemistry

126

154

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“…All three proteins were identified in a proteomic study of Caulobacter OMPs (Phadke et al, 2001), and CC0210 and CC2819 were also identified in a study of proteins enriched in Caulobacter stalks (Ireland et al, 2002). Finally, CC3013 and CC0210 were identified as OMPs that are abundant during growth on rich medium but not on minimal medium (Neugebauer et al, 2005). Because the levels of CpaC* and three abundant TonBdependent receptors are reduced in DbamE membranes, and because Caulobacter BamE associates with other BAM complex homologues, we propose that it participates in the assembly of these OMPs.…”

Section: Membranes Of Dbame Cells Are Deficient In Some Ompsmentioning

confidence: 99%

“…However, the genome encodes several proteins with homology to the monomeric porin OmpA as well as approximately 65 TonB-dependent receptors, which function in energy-dependent nutrient uptake (Postle & Larsen, 2007). TonB-dependent receptors transport siderophores (Pugsley & Reeves, 1976), cobalamin (Bassford & Kadner, 1977), maltodextrins (Neugebauer et al, 2005) and sucrose (Blanvillain et al, 2007), and members of this protein family may transport a wide variety of carbohydrates in plant pathogens and aquatic bacteria (Blanvillain et al, 2007). TonB-dependent receptors may also be particularly important for growth in dilute environments where passive diffusion through porins cannot satisfy the cell's nutritional requirements.…”

Section: Introductionmentioning

confidence: 99%

The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane β-barrel proteins in Caulobacter crescentus

2010

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The outer membrane of Gram-negative bacteria is an essential compartment containing a specific complement of lipids and proteins that constitute a protective, selective permeability barrier. Outer membrane β-barrel proteins are assembled into the membrane by the essential hetero-oligomeric BAM complex, which contains the lipoprotein BamE. We have identified a homologue of BamE, encoded by CC1365, which is located in the outer membrane of the stalked alpha-proteobacterium Caulobacter crescentus. BamE associates with proteins whose homologues in other bacteria are known to participate in outer membrane protein assembly: BamA (CC1915), BamB (CC1653) and BamD (CC1984). Caulobacter cells lacking BamE grow slowly in rich medium and are hypersensitive to anionic detergents, some antibiotics and heat exposure, which suggest that the membrane integrity of the mutant is compromised. Membranes of the ΔbamE mutant have normal amounts of the outer membrane protein RsaF, a TolC homologue, but are deficient in CpaC*, an aggregated form of the outer membrane secretin for type IV pili. ΔbamE membranes also contain greatly reduced amounts of three TonB-dependent receptors that are abundant in wild-type cells. Cells lacking BamE have short stalks and are delayed in stalk outgrowth during the cell cycle. Based on these findings, we propose that Caulobacter BamE participates in the assembly of outer membrane β-barrel proteins, including one or more substrates required for the initiation of stalk biogenesis.

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“…The C. crescentus genome contains 67 TBDRs and some of them have been identified as disaccharide or oligosaccharide transporters (Blanvillain et al, 2007;Eisenbeis et al, 2008;Lohmiller et al, 2008;Neugebauer et al, 2005). However, the substrate specificities of the majority of the TBDRs found in C. crescentus remain to be determined.…”

Section: Introductionmentioning

confidence: 99%

“…Despite the genomic indication of broader carbohydrate metabolism by C. crescentus (Nierman et al, 2001), most of the studies conducted thus far have been limited to either monosaccharides or easily hydrolysable disaccharides, including lactose, sucrose and maltose (Blanvillain et al, 2007;Hottes et al, 2004;Neugebauer et al, 2005;Stephens et al, 2007). Methods of nutrient acquisition from abundant cellulose-and xylan-derived oligosaccharides by C. crescentus have not been studied, except for a report of C. crescentus growth in cellobiose in minimal medium by Arellano et al (2010).…”

Section: Introductionmentioning

confidence: 99%

Extracellular gluco-oligosaccharide degradation by Caulobacter crescentus

et al. 2014

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The oligotrophic bacterium Caulobacter crescentus has the ability to metabolize various organic molecules, including plant structural carbohydrates, as a carbon source. The nature of b-glucosidase (BGL)-mediated gluco-oligosaccharide degradation and nutrient transport across the outer membrane in C. crescentus was investigated. All gluco-oligosaccharides tested (up to celloheptose) supported growth in M2 minimal media but not cellulose or CM-cellulose. The periplasmic and outer membrane fractions showed highest BGL activity, but no significant BGL activity was observed in the cytosol or extracellular medium. Cells grown in cellobiose showed expression of specific BGLs and TonB-dependent receptors (TBDRs). Carbonyl cyanide 3-chlorophenylhydrazone lowered the rate of cell growth in cellobiose but not in glucose, indicating potential cellobiose transport into the cell by a proton motive force-dependent process, such as TBDR-dependent transport, and facilitated diffusion of glucose across the outer membrane via specific porins. These results suggest that C. crescentus acquires carbon from cellulose-derived gluco-oligosaccharides found in the environment by extracellular and periplasmic BGL activity and TBDR-mediated transport. This report on extracellular degradation of gluco-oligosaccharides and methods of nutrient acquisition by C. crescentus supports a broader suite of carbohydrate metabolic capabilities suggested by the C. crescentus genome sequence that until now have not been reported.

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ExbBD-Dependent Transport of Maltodextrins through the Novel MalA Protein across the Outer Membrane ofCaulobacter crescentus

Cited by 100 publications

References 65 publications

Comparative Genomics and Experimental Characterization of N-Acetylglucosamine Utilization Pathway of Shewanella oneidensis

Comparative Genomics and Experimental Characterization of N-Acetylglucosamine Utilization Pathway of Shewanella oneidensis

The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane β-barrel proteins in Caulobacter crescentus

Extracellular gluco-oligosaccharide degradation by Caulobacter crescentus

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