Here, we report a draft genome sequence of a bacterial strain, F-183, isolated from a duckweed frond. Strain F-183 belongs to the family of the phylum , and its genomic information would contribute to understanding the ecophysiology of this abundant but rarely characterized phylum.
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| http://dx.doi.org/10.1128/mra.00453-21 | DOI Listing |
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Draft Genome Sequence of Strain F-183.
Microbiol Resour Announc
January 2022
Bioproduction Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, Japan.
Here, we report a draft genome sequence of a bacterial strain, F-183, isolated from a duckweed frond. Strain F-183 belongs to the family of the phylum , and its genomic information would contribute to understanding the ecophysiology of this abundant but rarely characterized phylum.
View Article and Find Full Text PDFNovel Plant-Associated Promotes Growth of Common Floating Aquatic Plants, Duckweeds.
Microorganisms
May 2021
Bioproduction Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba 305-8566, Ibaraki, Japan.
Duckweeds are small, fast growing, and starch- and protein-rich aquatic plants expected to be a next generation energy crop and an excellent biomaterial for phytoremediation. Despite such an importance, very little is known about duckweed-microbe interactions that would be a key biological factor for efficient industrial utilization of duckweeds. Here we first report the duckweed growth promoting ability of bacterial strains belonging to the phylum , the members of which are known to inhabit soils and terrestrial plants, but their ecological roles and plant-microbe interactions remain largely unclear.
View Article and Find Full Text PDFIdentification of two distinct antibacterial domains within the sequence of bovine alpha(s2)-casein.
Biochim Biophys Acta
August 1999
Department of Product Technology, Section of Structure and Functionality, NIZO food research, P.O. Box 20, 6710 BA, Ede, The Netherlands.
Two distinct domains with antibacterial activity were isolated from a peptic hydrolysate of bovine alpha(s2)-casein. The digested alpha(s2)-casein was fractionated by cation-exchange chromatography, after which the peptides in the two active fractions obtained were separated by high-performance liquid chromatography and sequenced by electrospray-ionization tandem mass spectrometry. The major component in each active fraction, f(183-207) and f(164-179), was further purified and the antibacterial activity of these components was tested against several microorganisms.
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