ArticleJournal of bacteriology2008
Xylanase attachment to the cell wall of the hyperthermophilic bacterium Thermotoga maritima.
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 16 papers.
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Who cites it
16 citing papers in PubMed, 42 citations in OpenAlex.
- Terrabacteria: redefining bacterial envelope diversity, biogenesis and evolution.Nature reviews. Microbiology · 2025Review
- Genomic analysis of Oceanotoga teriensis strain UFV_LIMV02, a multidrug-resistant thermophilic bacterium isolated from an offshore oil reservoir.Access microbiology · 2024Article
- Bacterial xylan utilization regulons: systems for coupling depolymerization of methylglucuronoxylans with assimilation and metabolism.Journal of industrial microbiology & biotechnology · 2022Article
- Multidomain, Surface Layer-associated Glycoside Hydrolases Contribute to Plant Polysaccharide Degradation by Caldicellulosiruptor Species.The Journal of biological chemistry · 2016Article
- Hydrogen Production by the Thermophilic Bacterium Thermotoga neapolitana.International journal of molecular sciences · 2015Review
- Transcriptomic analysis of xylan utilization systems in Paenibacillus sp. strain JDR-2.Applied and environmental microbiology · 2015Article
- Expression of Heterologous Cellulases in Thermotoga sp. Strain RQ2.BioMed research international · 2015Article
- Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.The Journal of biological chemistry · 2012Article
- Domain-swapping of mesophilic xylanase with hyper-thermophilic glucanase.BMC biotechnology · 2012Article
- Article
- Comparative analyses imply that the enigmatic Sigma factor 54 is a central controller of the bacterial exterior.BMC genomics · 2011Article
- Phylogenetic, microbiological, and glycoside hydrolase diversities within the extremely thermophilic, plant biomass-degrading genus Caldicellulosiruptor.Applied and environmental microbiology · 2010Article
- The genus Thermotoga: recent developments.Environmental technology · 2010Article
- Cell surface xylanases of the glycoside hydrolase family 10 are essential for xylan utilization by Paenibacillus sp. W-61 as generators of xylo-oligosaccharide inducers for the xylanase genes.Journal of bacteriology · 2010Article
- Two alternative pathways for the synthesis of the rare compatible solute mannosylglucosylglycerate in Petrotoga mobilis.Journal of bacteriology · 2010Article
- Hyperthermostable acetyl xylan esterase.Microbial biotechnology · 2010Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cellular localization and processing of the endo-xylanases (1,4-beta-D-xylan-xylanohydrolase; EC 3.2.1.8) of the hyperthermophile Thermotoga maritima were investigated, in particular with respect to the unusual outer membrane ("toga") of this gram-negative bacterium. XynB (40 kDa) was detected in the periplasmic fraction of T. maritima cells and in the culture supernatant. XynA (120 kDa) was partially released to the surrounding medium, but most XynA remained cell associated. Immunogold labeling of thin sections revealed that cell-bound XynA was localized mainly in the outer membranes of T. maritima cells. Amino-terminal sequencing of purified membrane-bound XynA revealed processing of the signal peptide after the eighth residue, thereby leaving the hydrophobic core of the signal peptide attached to the enzyme. This mode of processing is reminiscent of type IV prepilin signal peptide cleavage. Removal of the entire XynA signal peptide was necessary for release from the cell because enzyme purified from the culture supernatant lacked 44 residues at the N terminus, including the hydrophobic part of the signal peptide. We conclude that toga association of XynA is mediated by residues 9 to 44 of the signal peptide. The biochemical and electron microscopic localization studies together with the amino-terminal processing data indicate that XynA is held at the cell surface of T. maritima via a hydrophobic peptide anchor, which is highly unusual for an outer membrane protein.
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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.