Assignment of Vibrio sp. strain ABE-1 to Colwellia maris sp. nov., a new psychrophilic bacterium

Yumoto, Isao; Kawasaki, Kohkichi; Iwata, Hidehisa; Matsuyama, Hidetoshi; Okuyama, Hidetoshi

doi:10.1099/00207713-48-4-1357

Cited by 70 publications

(43 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One additional report is from a sediment (Borin et al, 2009), but judging from the eutrophic coastal setting, manganese reduction is not likely to be important there either. Isolates of these two gammaproteobacterial taxa are mainly of marine origin (Deming et al, 1988;Gosink and Staley, 1995;Bowman et al, 1998;Yumoto et al, 1998;Hedlund et al, 1999;Nogi et al, 2004;Jung et al, 2006). Most isolates are facultative anaerobes, some are able to use acetate as sole carbon and energy source and to reduce nitrate.…”

Section: Resultsmentioning

confidence: 99%

Three manganese oxide-rich marine sediments harbor similar communities of acetate-oxidizing manganese-reducing bacteria

et al. 2012

View full text Add to dashboard Cite

Dissimilatory manganese reduction dominates anaerobic carbon oxidation in marine sediments with high manganese oxide concentrations, but the microorganisms responsible for this process are largely unknown. In this study, the acetate-utilizing manganese-reducing microbiota in geographically well-separated, manganese oxide-rich sediments from Gullmar Fjord (Sweden), Skagerrak (Norway) and Ulleung Basin (Korea) were analyzed by 16S rRNA-stable isotope probing (SIP). Manganese reduction was the prevailing terminal electron-accepting process in anoxic incubations of surface sediments, and even the addition of acetate stimulated neither iron nor sulfate reduction. The three geographically distinct sediments harbored surprisingly similar communities of acetateutilizing manganese-reducing bacteria: 16S rRNA of members of the genera Colwellia and Arcobacter and of novel genera within the Oceanospirillaceae and Alteromonadales were detected in heavy RNA-SIP fractions from these three sediments. Most probable number (MPN) analysis yielded up to 10 6 acetate-utilizing manganese-reducing cells cm À 3 in Gullmar Fjord sediment. A 16S rRNA gene clone library that was established from the highest MPN dilutions was dominated by sequences of Colwellia and Arcobacter species and members of the Oceanospirillaceae, supporting the obtained RNA-SIP results. In conclusion, these findings strongly suggest that (i) acetatedependent manganese reduction in manganese oxide-rich sediments is catalyzed by members of taxa (Arcobacter, Colwellia and Oceanospirillaceae) previously not known to possess this physiological function, (ii) similar acetate-utilizing manganese reducers thrive in geographically distinct regions and (iii) the identified manganese reducers differ greatly from the extensively explored iron reducers in marine sediments.

show abstract

Section: Resultsmentioning

confidence: 99%

Three manganese oxide-rich marine sediments harbor similar communities of acetate-oxidizing manganese-reducing bacteria

et al. 2012

View full text Add to dashboard Cite

show abstract

“…In a psychrophilic bacterium C. maris (12,13), dimeric IDH (CmIDH-I) is a typical mesophilic enzyme and the optimum temperature for activity is 45 o C. On the other hand, monomeric IDH (CmIDH-II) shows the maximum activity at 20 o C, and about a half of the 15 activity is lost even by incubation for 10 min at 30 o C (9,14). The low optimum temperature and thermolability for activity indicate that it is a cold-adapted enzyme.…”

Section: Introductionmentioning

confidence: 99%

Analysis of amino acid residues involved in cold activity of monomeric isocitrate dehydrogenase from psychrophilic bacteria, Colwellia maris and Colwellia psychrerythraea

Yasuda

Kobayashi

Takada

2013

Journal of Bioscience and Bioengineering

View full text Add to dashboard Cite

Monomeric isocitrate dehydrogenases from psychrophilic bacteria, Colwellia maris andColwellia psychrerythraea (CmIDH-II and CpIDH-M, respectively) are cold-adapted enzymes and show a high degree of amino acid sequential identity to each other (77%).However, maximum activity of CpIDH-M at optimum temperature is much less than that of 5 CmIDH-II. In the C-terminal Region 3 of these enzymes, which was suggested from previous study to be responsible for their distinct catalytic ability, several sequential differences of amino acid residue are present. Among them, ten amino acid residues were exchanged between them by site-directed mutagenesis and several properties of the mutated enzymes were examined in this study. The mutated enzymes of CmIDH-II substituted its 10 Gln671, Leu724 and Phe735 residues with the corresponding residues of CpIDH-M (termed Q671K, L724Q and F735L, respectively) showed lower specific activity and thermostability for activity than the wild-type enzyme. Furthermore, the decreased specific activity was also observed in L693F. In contrast, the corresponding mutants of CpIDH-M, F693L, Q724L and L735F, showed the increased specific activity and thermostability for activity. The catalytic 15 efficiency (k cat /K m ) values of these mutated CmIDH-II and CpIDH-M were lower and higher than those of their wild-type IDHs, respectively. These results suggest that the Gln671, Leu693, Leu724 and Phe735 residues of CmIDH-II are important for exerting its high catalytic ability.

show abstract

“…The following strains were used: Colwellia maris ABE-1 T [8], Moritella marina MP-1 T (ATCC15381 T ), Shewanella marinintestina IK-1 T [9], Shewanella pneumatophori SCRC-2738 T [10], Shewanella benthica (ATCC43992), Pseudomonas alcaliphila AL15-21 T [11] as marine bacteria; Pseudomonas psychrophila E-3 T [12], Vibrio rumoiensis S-1 T [13], Shewanella oneidensis MR-1 T (ATCC 700550 T ), Pseudomonas aeruginosa WatG [14], Rhodococcus erythropolis (laboratory strain isolated from soil), E. coli DH5 (Takara Bio, Tokyo, Japan), and Stenotrophomonas maltophilia (laboratory strain from soil) as nonmarine bacteria; a thraustochytrid-like microorganism strain 12B [15] and Schizochitrium limacinum SR21 [16] as marine eukaryotes; and a terrestrial eukaryote, Saccharomyces cerevisiae (baker's yeast). Nonmarine and marine bacteria were grown in Luria-Bertani (LB) medium and LB medium containing 30 g/L NaCl, respectively.…”

Section: Strains and Culture Conditions Of Bacteria And Eukaryotesmentioning

confidence: 99%

Possible Biosynthetic Pathways for all cis‐3,6,9,12,15,19,22,25,28‐Hentriacontanonaene in Bacteria

Sugihara

Hori

Nakanowatari

et al. 2009

Lipids

View full text Add to dashboard Cite

A very long chain polyunsaturated hydrocarbon, hentriacontanonaene (C31:9), was detected in an eicosapentaenoic acid (EPA)-producing marine bacterium, which was isolated from the mid-latitude seashore of Hokkaido, Japan, and was tentatively identified as mesophilic Shewanella sp. strain osh08 from 16S rRNA gene sequencing. The geometry and position of the double bonds in this compound were determined physicochemically to be all cis at positions 3, 6, 9, 12, 15, 19, 22, 25, and 28. Although C31:9 was detected in all of the seven EPA-or/and docosahexaenoic acid-producing bacteria tested, an EPA-deficient mutant (strain IK-18) of one of these bacteria had no C31:9. Strain IK-18 had defects in the pfaD gene, one of the five pfa genes responsible for the biosynthesis of EPA.Although Escherichia coli DH5 does not produce EPA or DHA inherently, cells transformed with the pfa genes responsible for the biosynthesis of EPA and DHA produced EPA and DHA, respectively, but not C31:9. These results suggest that the Pfa protein complex is involved in the biosynthesis of C31:9 and that pfa genes must not be the only genes responsible for the formation of C31:9. In this report, we determined for the first time the molecular structure of the C31:9 and discuss the possible biosynthetic pathways of this compound. Key words

show abstract

Assignment of Vibrio sp. strain ABE-1 to Colwellia maris sp. nov., a new psychrophilic bacterium

Cited by 70 publications

References 27 publications

Three manganese oxide-rich marine sediments harbor similar communities of acetate-oxidizing manganese-reducing bacteria

Three manganese oxide-rich marine sediments harbor similar communities of acetate-oxidizing manganese-reducing bacteria

Analysis of amino acid residues involved in cold activity of monomeric isocitrate dehydrogenase from psychrophilic bacteria, Colwellia maris and Colwellia psychrerythraea

Possible Biosynthetic Pathways for all cis‐3,6,9,12,15,19,22,25,28‐Hentriacontanonaene in Bacteria

Contact Info

Product

Resources

About