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William B. Whitman - One of the best experts on this subject based on the ideXlab platform.
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Solirubrobacter pauli gen. nov., sp. nov., a Mesophilic Bacterium within the Rubrobacteridae related to common soil clones
International Journal of Systematic and Evolutionary Microbiology, 2003Co-Authors: David R. Singleton, Michelle Furlong, Aaron D. Peacock, David C. White, David C. Coleman, William B. WhitmanAbstract:A novel Bacterium, strain B33D1T, isolated from agricultural soil, was characterized taxonomically and phylogenetically. Strain B33D1T was a Gram-positive, aerobic rod of medium length that formed long chains on a common laboratory medium. However, B33D1T grew poorly on the surface of agar plates and was sensitive to desiccation. The optimal growth temperature was 30 °C (range 19–38 °C). The organism grew well on a variety of sugars and was capable of utilizing a few amino acids as sole carbon sources. Phylogenetically, the most closely related described species to strain B33D1T was Rubrobacter xylanophilus, which possessed 86 % 16S rRNA sequence similarity. However, a number of 16S rRNA gene clones derived from soil samples possessed up to 93 % sequence similarity. These results placed strain B33D1T within the subclass Rubrobacteridae of the phylum Actinobacteria. The novel genus and species Solirubrobacter pauli gen. nov., sp. nov. is proposed, with strain B33D1T (=ATCC BAA-492T=DSM 14954T) as the type strain.
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Solirubrobacter pauli gen. nov., sp. nov., a Mesophilic Bacterium within the Rubrobacteridae related to common soil clones.
International journal of systematic and evolutionary microbiology, 2003Co-Authors: David R. Singleton, Aaron D. Peacock, David C. White, David C. Coleman, Michelle A Furlong, William B. WhitmanAbstract:A novel Bacterium, strain B33D1T, isolated from agricultural soil, was characterized taxonomically and phylogenetically. Strain B33D1T was a Gram-positive, aerobic rod of medium length that formed long chains on a common laboratory medium. However, B33D1T grew poorly on the surface of agar plates and was sensitive to desiccation. The optimal growth temperature was 30 degrees C (range 19-38 degrees C). The organism grew well on a variety of sugars and was capable of utilizing a few amino acids as sole carbon sources. Phylogenetically, the most closely related described species to strain B33D1T was Rubrobacter xylanophilus, which possessed 86% 16S rRNA sequence similarity. However, a number of 16S rRNA gene clones derived from soil samples possessed up to 93% sequence similarity. These results placed strain B33D1T within the subclass Rubrobacteridae of the phylum Actinobacteria. The novel genus and species Solirubrobacter pauli gen. nov., sp. nov. is proposed, with strain B33D1T (=ATCC BAA-492T =DSM 14954T) as the type strain.
Volker Müller - One of the best experts on this subject based on the ideXlab platform.
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a na a1ao atp synthase with a v type c subunit in a Mesophilic Bacterium
FEBS Journal, 2020Co-Authors: Dennis Litty, Volker MüllerAbstract:A1 AO ATP synthases with a V-type c subunit have only been found in hyperthermophilic archaea which makes bioenergetic analyses impossible due to the instability of liposomes at high temperatures. A search for a potential archaeal A1 AO ATP synthase with a V-type c subunit in a Mesophilic organism revealed an A1 AO ATP synthase cluster in the anaerobic, acetogenic Bacterium EuBacterium limosum KIST612. The enzyme was purified to apparent homogeneity from cells grown on methanol to a specific activity of 1.2 U·mg-1 with a yield of 12%. The enzyme contained subunits A, B, C, D, E, F, H, a, and c. Subunit c is predicted to be a typical V-type c subunit with only one ion (Na+ )-binding site. Indeed, ATP hydrolysis was strictly Na+ -dependent. N,N'-dicyclohexylcarbodiimide (DCCD) inhibited ATP hydrolysis, but inhibition was relieved by addition of Na+ . Na+ was shown directly to abolish binding of the fluorescence DCCD derivative, NCD-4, to subunit c, demonstrating a competition of Na+ and DCCD/NCD-4 for a common binding site. After incorporation of the A1 AO ATP synthase into liposomes, ATP-dependent primary transport of 22 Na+ as well as ΔµNa+ -driven ATP synthesis could be demonstrated. The Na+ A1 AO ATP synthase from E. limosum is the first ATP synthase with a V-type c subunit from a Mesophilic organism. This will enable future bioenergetic analysis of these unique ATP synthases.
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A Na+ A1AO ATP synthase with a V‐type c subunit in a Mesophilic Bacterium
FEBS Journal, 2019Co-Authors: Dennis Litty, Volker MüllerAbstract:A1 AO ATP synthases with a V-type c subunit have only been found in hyperthermophilic archaea which makes bioenergetic analyses impossible due to the instability of liposomes at high temperatures. A search for a potential archaeal A1 AO ATP synthase with a V-type c subunit in a Mesophilic organism revealed an A1 AO ATP synthase cluster in the anaerobic, acetogenic Bacterium EuBacterium limosum KIST612. The enzyme was purified to apparent homogeneity from cells grown on methanol to a specific activity of 1.2 U·mg-1 with a yield of 12%. The enzyme contained subunits A, B, C, D, E, F, H, a, and c. Subunit c is predicted to be a typical V-type c subunit with only one ion (Na+ )-binding site. Indeed, ATP hydrolysis was strictly Na+ -dependent. N,N'-dicyclohexylcarbodiimide (DCCD) inhibited ATP hydrolysis, but inhibition was relieved by addition of Na+ . Na+ was shown directly to abolish binding of the fluorescence DCCD derivative, NCD-4, to subunit c, demonstrating a competition of Na+ and DCCD/NCD-4 for a common binding site. After incorporation of the A1 AO ATP synthase into liposomes, ATP-dependent primary transport of 22 Na+ as well as ΔµNa+ -driven ATP synthesis could be demonstrated. The Na+ A1 AO ATP synthase from E. limosum is the first ATP synthase with a V-type c subunit from a Mesophilic organism. This will enable future bioenergetic analysis of these unique ATP synthases.
Hansjurgen Busse - One of the best experts on this subject based on the ideXlab platform.
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proposal of vibrionimonas magnilacihabitans gen nov sp nov a curved gram stain negative Bacterium isolated from lake water
International Journal of Systematic and Evolutionary Microbiology, 2014Co-Authors: Richard A Albert, Daniel Zitomer, Michael E Dollhopf, Anne Schauergimenez, Craig A Struble, Michael King, Stefan Langer, Hansjurgen BusseAbstract:A Mesophilic Bacterium appearing as curved rod-shaped cells was isolated from Lake Michigan water. It exhibited highest similarities with SediminiBacterium ginsengisoli DCY13T (94.4 %); SediminiBacterium salmoneum NJ-44T (93.6 %) and Hydrotalea flava CCUG 51397 T (93.1 %) while similarities with other recognized species were <92.0 %. The primary polar lipid was phosphatidylethanolamine, with moderate amounts of two unidentified glycolipids, three unknown polar lipids, one unknown aminophospholipid and one aminolipid. The primary respiratory quinone was MK-7 and sym-homospermidine was the primary polyamine. The major cellular fatty acids were iso-C15 : 1G, iso-C15 : 0, iso-C16 : 0 3-OH and iso-C17 : 0 3-OH, with moderate amounts of iso-C16 : 0. The presence of glycolipids differentiated the novel strains from related genera. The DNA mol% G+C content of the type strain MU-2T was 45.2. Results for other phenotypic and molecular analyses indicated that strain MU-2T is a representative of a novel genus and species for which the name Vibrionimonas magnilacihabitans is proposed. The type strain is MU-2T ( = NRRL B-59231 = DSM 22423).
David R. Singleton - One of the best experts on this subject based on the ideXlab platform.
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Solirubrobacter pauli gen. nov., sp. nov., a Mesophilic Bacterium within the Rubrobacteridae related to common soil clones
International Journal of Systematic and Evolutionary Microbiology, 2003Co-Authors: David R. Singleton, Michelle Furlong, Aaron D. Peacock, David C. White, David C. Coleman, William B. WhitmanAbstract:A novel Bacterium, strain B33D1T, isolated from agricultural soil, was characterized taxonomically and phylogenetically. Strain B33D1T was a Gram-positive, aerobic rod of medium length that formed long chains on a common laboratory medium. However, B33D1T grew poorly on the surface of agar plates and was sensitive to desiccation. The optimal growth temperature was 30 °C (range 19–38 °C). The organism grew well on a variety of sugars and was capable of utilizing a few amino acids as sole carbon sources. Phylogenetically, the most closely related described species to strain B33D1T was Rubrobacter xylanophilus, which possessed 86 % 16S rRNA sequence similarity. However, a number of 16S rRNA gene clones derived from soil samples possessed up to 93 % sequence similarity. These results placed strain B33D1T within the subclass Rubrobacteridae of the phylum Actinobacteria. The novel genus and species Solirubrobacter pauli gen. nov., sp. nov. is proposed, with strain B33D1T (=ATCC BAA-492T=DSM 14954T) as the type strain.
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Solirubrobacter pauli gen. nov., sp. nov., a Mesophilic Bacterium within the Rubrobacteridae related to common soil clones.
International journal of systematic and evolutionary microbiology, 2003Co-Authors: David R. Singleton, Aaron D. Peacock, David C. White, David C. Coleman, Michelle A Furlong, William B. WhitmanAbstract:A novel Bacterium, strain B33D1T, isolated from agricultural soil, was characterized taxonomically and phylogenetically. Strain B33D1T was a Gram-positive, aerobic rod of medium length that formed long chains on a common laboratory medium. However, B33D1T grew poorly on the surface of agar plates and was sensitive to desiccation. The optimal growth temperature was 30 degrees C (range 19-38 degrees C). The organism grew well on a variety of sugars and was capable of utilizing a few amino acids as sole carbon sources. Phylogenetically, the most closely related described species to strain B33D1T was Rubrobacter xylanophilus, which possessed 86% 16S rRNA sequence similarity. However, a number of 16S rRNA gene clones derived from soil samples possessed up to 93% sequence similarity. These results placed strain B33D1T within the subclass Rubrobacteridae of the phylum Actinobacteria. The novel genus and species Solirubrobacter pauli gen. nov., sp. nov. is proposed, with strain B33D1T (=ATCC BAA-492T =DSM 14954T) as the type strain.
Dennis Litty - One of the best experts on this subject based on the ideXlab platform.
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a na a1ao atp synthase with a v type c subunit in a Mesophilic Bacterium
FEBS Journal, 2020Co-Authors: Dennis Litty, Volker MüllerAbstract:A1 AO ATP synthases with a V-type c subunit have only been found in hyperthermophilic archaea which makes bioenergetic analyses impossible due to the instability of liposomes at high temperatures. A search for a potential archaeal A1 AO ATP synthase with a V-type c subunit in a Mesophilic organism revealed an A1 AO ATP synthase cluster in the anaerobic, acetogenic Bacterium EuBacterium limosum KIST612. The enzyme was purified to apparent homogeneity from cells grown on methanol to a specific activity of 1.2 U·mg-1 with a yield of 12%. The enzyme contained subunits A, B, C, D, E, F, H, a, and c. Subunit c is predicted to be a typical V-type c subunit with only one ion (Na+ )-binding site. Indeed, ATP hydrolysis was strictly Na+ -dependent. N,N'-dicyclohexylcarbodiimide (DCCD) inhibited ATP hydrolysis, but inhibition was relieved by addition of Na+ . Na+ was shown directly to abolish binding of the fluorescence DCCD derivative, NCD-4, to subunit c, demonstrating a competition of Na+ and DCCD/NCD-4 for a common binding site. After incorporation of the A1 AO ATP synthase into liposomes, ATP-dependent primary transport of 22 Na+ as well as ΔµNa+ -driven ATP synthesis could be demonstrated. The Na+ A1 AO ATP synthase from E. limosum is the first ATP synthase with a V-type c subunit from a Mesophilic organism. This will enable future bioenergetic analysis of these unique ATP synthases.
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A Na+ A1AO ATP synthase with a V‐type c subunit in a Mesophilic Bacterium
FEBS Journal, 2019Co-Authors: Dennis Litty, Volker MüllerAbstract:A1 AO ATP synthases with a V-type c subunit have only been found in hyperthermophilic archaea which makes bioenergetic analyses impossible due to the instability of liposomes at high temperatures. A search for a potential archaeal A1 AO ATP synthase with a V-type c subunit in a Mesophilic organism revealed an A1 AO ATP synthase cluster in the anaerobic, acetogenic Bacterium EuBacterium limosum KIST612. The enzyme was purified to apparent homogeneity from cells grown on methanol to a specific activity of 1.2 U·mg-1 with a yield of 12%. The enzyme contained subunits A, B, C, D, E, F, H, a, and c. Subunit c is predicted to be a typical V-type c subunit with only one ion (Na+ )-binding site. Indeed, ATP hydrolysis was strictly Na+ -dependent. N,N'-dicyclohexylcarbodiimide (DCCD) inhibited ATP hydrolysis, but inhibition was relieved by addition of Na+ . Na+ was shown directly to abolish binding of the fluorescence DCCD derivative, NCD-4, to subunit c, demonstrating a competition of Na+ and DCCD/NCD-4 for a common binding site. After incorporation of the A1 AO ATP synthase into liposomes, ATP-dependent primary transport of 22 Na+ as well as ΔµNa+ -driven ATP synthesis could be demonstrated. The Na+ A1 AO ATP synthase from E. limosum is the first ATP synthase with a V-type c subunit from a Mesophilic organism. This will enable future bioenergetic analysis of these unique ATP synthases.
