Colwellia psychrerythraea Strains from Distant Deep Sea Basins Show Adaptation to Local Conditions
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چکیده
منابع مشابه
Colwellia psychrerythraea Strains from Distant Deep Sea Basins Show Adaptation to Local Conditions
Department of Biological Sciences, Michigan Technological University, Houghton, MI, USA, Department of Civil and Environmental Engineering, University of Tennessee, Knoxville, TN, USA, Center for Environmental Biotechnology, University of Tennessee, Knoxville, TN, USA, 4 Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN, USA, Graduate School of Genome Science and Technology, Un...
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We examined the Arctic bacterium Colwellia psychrerythraea strain 34H for motility at temperatures from -1 to -15 degrees C by using transmitted-light microscopy in a temperature-controlled laboratory. The results, showing motility to -10 degrees C, indicate much lower temperatures to be permissive of motility than previously reported (5 degrees C), with implications for microbial activity in f...
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The nitrogen cycle in the marine environment is strongly affected by ammonia-oxidizing Thaumarchaeota. In some marine settings, Thaumarchaeotes can comprise a large percentage of the prokaryotic population. To better understand the biogeographic patterns of Thaumarchaeotes, we sought to investigate differences in their abundance and phylogenetic diversity between geographically distinct basins....
متن کاملCrystal structure and functional characterization of an isoaspartyl dipeptidase (CpsIadA) from Colwellia psychrerythraea strain 34H
Isoaspartyl dipeptidase (IadA) is an enzyme that catalyzes the hydrolysis of an isoaspartyl dipeptide-like moiety, which can be inappropriately formed in proteins, between the β-carboxyl group side chain of Asp and the amino group of the following amino acid. Here, we have determined the structures of an isoaspartyl dipeptidase (CpsIadA) from Colwellia psychrerythraea, both ligand-free and that...
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ژورنال
عنوان ژورنال: Frontiers in Environmental Science
سال: 2016
ISSN: 2296-665X
DOI: 10.3389/fenvs.2016.00033