Strain 10R5-21 was isolated from lagoon sediments. Cells of strain 10R5-21 were Gram-reaction-negative, rod-shaped and motile by means of polar flagella. The strain was obligately aerobic and positive for catalase and oxidase activity. Strain 10R5-21 was able to grow at 10-37 ˚C (optimum 25-30 ˚C), at pH 5.0-9.0 (optimum pH 6.5-7.5) and in the presence of 0-0.5 % (w/v) NaCl (optimum 0 %). C16 : 1ω7c/C16 : 1ω6c, C16 : 0 and C12 : 0 were present as predominant (>5 %) fatty acids. Q-8 was identified as the major respiratory quinone. Diphosphatidylglycerol, phosphatidylglycerol and phosphatidylethanolamine were present as major polar lipids with minor amounts of unidentified aminophospholipids and unidentified aminolipids. The genomic G+C content of strain 10R5-21 was 64.1 mol%. 16S rRNA gene sequence analysis indicated that strain 10R5-21 belongs to the genus Pseudoduganella within the family Oxalobacteraceae of the class Betaproteobacteria. Strain 10R5-21 shared 98.8 % 16S rRNA gene sequence similarity with Pseudoduganella violaceinigra YIM 31327. DNA-DNA hybridization values between strain 10R5-21 and P. violaceinigra KACC 11669 were clearly below the 70 % threshold. Distinct morphological, biochemical, chemotaxonomic and genetic differences from previously described taxa support the classification of strain 10R5-21 as a representative of a novel species in the genus Pseudoduganella, for which the name Pseudoduganella eburnea sp. nov. is proposed. The type strain is 10R5-21 (=KEMB 563-061=JCM 31587).
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http://dx.doi.org/10.1099/ijsem.0.002460 | DOI Listing |
Chem Biodivers
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Yantai Institute of Coastal Zone Research, Coastal biology and Bioresource Utilization, 17 Chunhui Road, 264003, Yantai, CHINA.
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3rd Department of Internal Medicine-Metabolic Care and Gerontology, University Hospital and Medical Faculty in Hradec Kralove, Charles University in Prague, Hradec Kralove, Czech Republic.
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Cell Physiology and Molecular Biophysics Department, Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, Texas, USA.
Purifying membrane proteins has been the limiting step for studying their structure and function. The challenges of the process include the low expression levels in heterologous systems and the requirement for their biochemical stabilization in solution. The human voltage-gated proton channel (hH1) is a good example of that: the published protocols to express and purify hH1 produce low protein quantities at high costs, which is an issue for systematically characterizing its structure and function.
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