Disease relevance of Pseudoalteromonas

• The elongation factor Ts was isolated from the psychrophilic Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125 strain (PhEF-Ts), and its functional properties were studied [1].
• The isolates constitute a new species, distinct from the other Alteromonas and Pseudoalteromonas species, as shown by DNA-DNA hybridization experiments and phylogenetic clustering of 16S rRNA gene sequences, for which the name Pseudoalteromonas bacteriolytica sp. nov [2].
• Arylsulfatase cloned from a marine aerobic Gram-negative bacterium, Pseudoalteromonas carrageenovora, was overexpressed in Escherichia coli with 10 microM IPTG induction [3].

High impact information on Pseudoalteromonas

• In this context, we have constructed a double mutant (Q58C/A99C) of the cold-active and heat-labile alpha-amylase from the Antarctic bacterium Pseudoalteromonas haloplanktis, defined on the basis of its strong similarity with the mesophilic enzyme from pig pancreas [4].
• We previously reported a new marine bacterium, Pseudoalteromonas phenolica sp. nov [5].
• Fifteen strains of polycyclic aromatic hydrocarbon (PAH)-catabolizing bacteria, identified as Pseudoalteromonas spp. were isolated from Eagle Harbor, Puget Sound, USA, using a most probable number procedure in which naphthalene or phenanthrene was the sole carbon and energy source [6].
• Cold-adapted beta-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis [7].
• Cycloprodigiosin hydrochloride (cPrG.HCl) obtained from a marine bacterium Pseudoalteromonas denitrificans induces apoptotic cell death in various cancerous cell lines. cPrG.HCl alone caused a little cytotoxicity in HeLa cells, but it enhanced the apoptotic process progressively when co-administered with tumor necrosis factor (TNF)alpha [8].

Chemical compound and disease context of Pseudoalteromonas

• These results suggest that Pseudoalteromonas sp. strain A28 produced an extracellular serine protease which was responsible for the algicidal activity of this marine bacterium [9].
• The phenotypic features of the isolates were similar to these of Pseudoalteromonas rubra ATCC 29570T, but they could be differentiated using 10 traits (growth at 37 degrees C, requirement for organic growth factors, bacteriolytic activity, utilization of sucrose, N-acetylglucosamine, fumarate, succinate, D-galactose, L-proline and acetate) [2].
• The phenotypic features of Pseudoalteromonas elyakovii strains were closely related to that of Pseudoalteromonas espejiana IAM 12640T, but utilization of three carbon compounds (D-mannose, L-tyrosine and trehalose) distinguished both species [10].
• According to the polyphasic evidence presented in this study, it is proposed that strain KMM 636T (= LMG 19692T = CIP 106859T) be classified as Pseudoalteromonas maricaloris sp. nov. and [P. aurantia] NCIMB 2033 be reclassified as Pseudoalteromonas flavipulchra NCIMB 2033T (= KMM 3630T = LMG 20361T) sp. nov [11].
• The effect of low mean power laser irradiations with short pulse duration from an Nd:YAG (neodymium-doped yttrium aluminium garnet) laser on a marine biofilm-forming bacterium, Pseudoalteromonas carrageenovora, was investigated in the laboratory [12].

Biological context of Pseudoalteromonas

• SIGNIFICANCE AND IMPACT OF THE STUDY: The production of glycosidases by Pseudoalteromonas issachenkonii KMM 3549(T) was significantly improved by using a simple nutrient medium containing peptone (2.5 g l(-1)) and xylose (5.0 g l(-1)) in 100% natural seawater [13].

Gene context of Pseudoalteromonas

• A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures [14].
• Purification and characterization of the recombinant arylsulfatase cloned from Pseudoalteromonas carrageenovora [3].
• Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis [15].
• The alpha-amylase precursor from the bacterium Pseudoalteromonas haloplanktis possesses a propeptide at the C-terminus possibly responsible for outer membrane translocation [16].

References