Alginate Lyase (AlgL) Activity Is Required for Alginate Biosynthesis in
            <i>Pseudomonas aeruginosa</i>

Albrecht, Mark T.; Schiller, Neal L.

doi:10.1128/jb.187.11.3869-3872.2005

Cited by 60 publications

(52 citation statements)

References 27 publications

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“…The gene encoding the P. aeruginosa periplasmic alginate lyase, algL, is located within the alginate biosynthesis cluster (12,57). Interestingly, alginate production and alginate lyase expression have been reported to be coregulated by the positive transcriptional regulator AlgB (57), and alginate lyase also plays a role in alginate biosynthesis in P. aeruginosa (1). A recent report also suggested the possible bifunctional roles of AlgL in a multiprotein secretion complex and in degrading free alginate polymers in the periplasm (31).…”

Section: Discussionmentioning

confidence: 99%

“…Polysaccharide lyases reported to date are (or have been predicted to be) extracellular or periplasmic (1,4,17,35,50,65). The TIGR-CMR database indicated the presence of a putative 31-amino-acid-long signal peptide in RbmB, but SignalP 3.0 (for signal peptide cleavage site prediction) did not have a strong prediction for a cleavage site (probability of cleavage between S31 and E32 is 0.319 by the SignalP-NN method and 0.023 by the SignalP-HMM method).…”

Section: Resultsmentioning

confidence: 99%

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The rbmBCDEF Gene Cluster Modulates Development of Rugose Colony Morphology and Biofilm Formation in Vibrio cholerae

2007

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Vibrio cholerae, the causative agent of cholera, can undergo phenotypic variation generating rugose and smooth variants. The rugose variant forms corrugated colonies and well-developed biofilms and exhibits increased levels of resistance to several environmental stresses. Many of these phenotypes are mediated in part by increased expression of the vps genes, which are organized into vps-I and vps-II coding regions, separated by an intergenic region. In this study, we generated in-frame deletions of the five genes located in the vps intergenic region, termed rbmB to -F (rugosity and biofilm structure modulators B to F) in the rugose genetic background, and characterized the mutants for rugose colony development and biofilm formation. Deletion of rbmB, which encodes a protein with low sequence similarity to polysaccharide hydrolases, resulted in an increase in colony corrugation and accumulation of exopolysaccharides relative to the rugose variant. RbmC and its homolog Bap1 are predicted to encode proteins with carbohydrate-binding domains. The colonies of the rbmC bap1 double deletion mutant and bap1 single deletion mutant exhibited a decrease in colony corrugation. Furthermore, the rbmC bap1 double deletion mutant was unable to form biofilms at the air-liquid interface after 2 days, while the biofilms formed on solid surfaces detached readily. Although the colony morphology of rbmDEF mutants was similar to that of the rugose variant, their biofilm structure and cell aggregation phenotypes were different than those of the rugose variant. Taken together, these results indicate that vps intergenic region genes encode proteins that are involved in biofilm matrix production and maintenance of biofilm structure and stability.

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Section: Discussionmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

The rbmBCDEF Gene Cluster Modulates Development of Rugose Colony Morphology and Biofilm Formation in Vibrio cholerae

2007

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“…The periplasmic C terminus of Alg44 shares homology with the membrane fusion proteins involved in the bridging of the periplasm in multidrug efflux pumps (11,43). The periplasmic alginate lyase, AlgL, appears to be required for the translocation of intact alginate across the periplasm (1,26). AlgE is an outer membrane, anion-selective channel protein through which alginate is presumably secreted (30).…”

mentioning

confidence: 99%

“…AlgX shows little homology to any known protein, and its role is unclear (14). Knockout mutants of AlgK, AlgG, and AlgX have nonmucoid phenotypes, although they produce short alginate fragments, due to the activity of the alginate lyase (AlgL), which degrades the nascent alginate (1,14,(19)(20)(21)36). AlgF, AlgI, and AlgJ are involved in acetylation of alginate, but they are not ultimately required for its production (12).…”

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confidence: 99%

Membrane Topology of Outer Membrane Protein AlgE, Which Is Required for Alginate Production in Pseudomonas aeruginosa

Hay

Rehman

Rehm

2010

Appl Environ Microbiol

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The ubiquitous opportunistic human pathogen Pseudomonas aeruginosa secretes a viscous extracellular polysaccharide, called alginate, as a virulence factor during chronic infection of patients with cystic fibrosis. In the present study, it was demonstrated that the outer membrane protein AlgE is required for the production of alginate in P. aeruginosa. An isogenic marker-free algE deletion mutant was constructed. This strain was incapable of producing alginate but did secrete alginate degradation products, indicating that polymerization occurs but that the alginate chain is subsequently degraded during transit through the periplasm. Alginate production was restored by introducing the algE gene. The membrane topology of the outer membrane protein AlgE was assessed by site-specific insertions of FLAG epitopes into predicted extracellular loop regions.

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“…For the latter, AlgL could be involved in the modification of oligomers and therefore in the process to export the polymer to the cell surface. Although it has been reported that mutants defective in AlgL appeared nonmucoid and produce only small amounts of alginate (48, 67), AlgL is essentially required for alginate biosyn- thesis (2). It has also been reported that Ca 2ϩ and Mn 2ϩ can selectively activate or inhibit alginate lyase and epimerization activity in algae (35).…”

Section: Resultsmentioning

confidence: 99%

Analysis of Lipid Export in Hydrocarbonoclastic Bacteria of the GenusAlcanivorax: Identification of Lipid Export-Negative Mutants ofAlcanivorax borkumensisSK2 andAlcanivorax jadensisT9

et al. 2010

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Triacylglycerols (TAGs), wax esters (WEs), and polyhydroxyalkanoates (PHAs) are the major hydrophobic compounds synthesized in bacteria and deposited as cytoplasmic inclusion bodies when cells are cultivated under imbalanced growth conditions. The intracellular occurrence of these compounds causes high costs for downstream processing. Alcanivorax species are able to produce extracellular lipids when the cells are cultivated on hexadecane or pyruvate as the sole carbon source. In this study, we developed a screening procedure to isolate lipid export-negative transposon-induced mutants of bacteria of the genus Alcanivorax for identification of genes required for lipid export by employing the dyes Nile red and Solvent Blue 38. Three transposoninduced mutants of A. jadensis and seven of A. borkumensis impaired in lipid secretion were isolated. All isolated mutants were still capable of synthesizing and accumulating these lipids intracellularly and exhibited no growth defect. In the A. jadensis mutants, the transposon insertions were mapped in genes annotated as encoding a putative DNA repair system specific for alkylated DNA (Aj17), a magnesium transporter (Aj7), and a transposase (Aj5). In the A. borkumensis mutants, the insertions were mapped in genes encoding different proteins involved in various transport processes, like genes encoding ( Almost all prokaryotes synthesize lipophilic storage substances as an integral part of their metabolism under limited nitrogen or phosphorus conditions if there is an excess of a suitable carbon source at the same time. The accumulated storage lipids serve as energy and carbon sources during starvation periods, and they are mobilized again under conditions of carbon and energy deficiency. The majority of the members of many genera synthesize hydrophobic polymers, such as poly(3-hydroxybutyrate) (PHB) or other types of polyhydroxyalkanoates (PHAs), whereas the accumulation of triacylglycerols (TAGs; trioxoesters of glycerol and long-chain fatty acids [FAs]) or wax esters (WEs; oxoesters of primary long-chain fatty acids and primary long-chain fatty alcohols) occurs in fewer prokaryotes (66). TAG accumulation has been reported for species of the genera Streptomyces, Mycobacterium, Nocardia, Rhodococcus (4,6,65), and recently also Alcanivorax and other hydrocarbonoclastic marine bacteria (32). Accumulation of WEs has been frequently reported for species of the genus Acinetobacter (66) but also for marine bacteria, such as Marinobacter (50) and Alcanivorax (11,32).In general, the accumulation of at least one type of these compounds occurs intracellularly under imbalanced growth conditions in almost all prokaryotes. The localization of neutral lipids in marine organisms is not restricted to the cell cytoplasm, as extracellular lipid deposition has been shown in studies with Alcaligenes sp. PHY9 and Pseudomonas nautica (24). The production of extracellular wax esters by Alcanivorax jadensis T9 growing on hexadecane was described a few years ago (11). Species of the genus Alcanivorax ...

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Alginate Lyase (AlgL) Activity Is Required for Alginate Biosynthesis in Pseudomonas aeruginosa

Cited by 60 publications

References 27 publications

The rbmBCDEF Gene Cluster Modulates Development of Rugose Colony Morphology and Biofilm Formation in Vibrio cholerae

The rbmBCDEF Gene Cluster Modulates Development of Rugose Colony Morphology and Biofilm Formation in Vibrio cholerae

Membrane Topology of Outer Membrane Protein AlgE, Which Is Required for Alginate Production in Pseudomonas aeruginosa

Analysis of Lipid Export in Hydrocarbonoclastic Bacteria of the GenusAlcanivorax: Identification of Lipid Export-Negative Mutants ofAlcanivorax borkumensisSK2 andAlcanivorax jadensisT9

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