ArticleJournal of bacteriology2008
NagA-dependent uptake of N-acetyl-glucosamine and N-acetyl-chitin oligosaccharides across the outer membrane of Caulobacter crescentus.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 62 citations in OpenAlex.
- Article
- Peptidoglycan recycling is critical for cell division, cell wall integrity, and β-lactam resistance ineLife · 2026Article
- Internal Ion Pairs Control Transport Through TonB-Dependent Siderophore Receptors.International journal of molecular sciences · 2026Article
- Selective benefit of the sucrose TonB-dependent receptor, SucA, inmicroPublication biology · 2025Article
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- Article
- Selection for Translational Efficiency in Genes Associated with Alphaproteobacterial Gene Transfer Agents.mSystems · 2022Article
- Metabolic cross-feeding structures the assembly of polysaccharide degrading communities.Science advances · 2022Article
- A Surface Exposed, Two-Domain Lipoprotein Cargo of a Type XI Secretion System Promotes Colonization of Host Intestinal Epithelia Expressing Glycans.Frontiers in microbiology · 2022Article
- The Fish Pathogen Aliivibrio salmonicida LFI1238 Can Degrade and Metabolize Chitin despite Gene Disruption in the Chitinolytic Pathway.Applied and environmental microbiology · 2021Article
- Resource partitioning of phytoplankton metabolites that support bacterial heterotrophy.The ISME journal · 2021Article
- Conformational rearrangements in the N-domain ofThe Journal of biological chemistry · 2020Article
- A TonB-dependent receptor constitutes the outer membrane transport system for a lignin-derived aromatic compound.Communications biology · 2019Article
- Ecological Functions of Agricultural Soil Bacteria and Microeukaryotes in Chitin Degradation: A Case Study.Frontiers in microbiology · 2019Article
- SucA-dependent uptake of sucrose across the outer membrane of Caulobacter crescentus.Journal of microbiology (Seoul, Korea) · 2018Article
- Polysaccharide Utilization Loci: Fueling Microbial Communities.Journal of bacteriology · 2017Review
- TonB-Dependent Heme/Hemoglobin Utilization by Caulobacter crescentus HutA.Journal of bacteriology · 2017Article
- Transcriptomic analysis of the stationary phase response regulator SpdR in Caulobacter crescentus.BMC microbiology · 2016Article
- Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Among the 67 predicted TonB-dependent outer membrane transporters of Caulobacter crescentus, NagA was found to be essential for growth on N-acetyl-beta-D-glucosamine (GlcNAc) and larger chitin oligosaccharides. NagA (93 kDa) has a predicted typical domain structure of an outer membrane transport protein: a signal sequence, the TonB box EQVVIT, a hatch domain of 147 residues, and a beta-barrel composed of 22 antiparallel beta-strands linked by large surface loops and very short periplasmic turns. Mutations in tonB1 and exbBD, known to be required for maltose transport via MalA in C. crescentus, and in two additional predicted tonB genes (open reading frames cc2327 and cc3508) did not affect NagA-mediated GlcNAc uptake. nagA is located in a gene cluster that encodes a predicted PTS sugar transport system and two enzymes that convert GlcNAc-6-P to fructose-6-P. Since a nagA insertion mutant did not grow on and transport GlcNAc, diffusion of GlcNAc through unspecific porins in the outer membrane is excluded. Uptake of GlcNAc into tonB and exbBD mutants and reduction but not abolishment of GlcNAc transport by agents which dissipate the electrochemical potential of the cytoplasmic membrane (0.1 mM carbonyl cyanide 3-chlorophenylhydrazone and 1 mM 2,4-dinitrophenol) suggest diffusion of GlcNAc through a permanently open pore of NagA. Growth on (GlcNAc)(3) and (GlcNAc)(5) requires ExbB and ExbD, indicating energy-coupled transport by NagA. We propose that NagA forms a small pore through which GlcNAc specifically diffuses into the periplasm and functions as an energy-coupled transporter for the larger chitin oligosaccharides.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.