• Journal of Species Research
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• v.12 no.spc2
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• pp.45-53
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• 2023

In July 2018, solar saltern samples were collected from Siheung, Gyeonggi-do Province to obtain unrecorded haloarchaea in Korea. The samples were suspended in a 20% NaCl (w/v) solution, and serial dilution was performed in fresh DB Characterization media No. 2. The strains isolated in this study showed at least 98.7% sequence similarity or more compared to the previously reported. Finally, 16 haloarchaeal strains, which were not reported in Korea but validly published under the International Code of Nomenclature of Prokaryotes (ICNP), were obtained from a solar saltern in Siheung. These 16 isolates were allocated to the orders Halobacteriales and Haloferacales. The 10 Halobacteriales strains were classified into the family Halobacteriaceae and Haloarculaceae. Each family belonged to three genera, respectively. The other six Haloferacales belonged to the families Haloferacaceae and Halorubraceae. Each family belonged to genus genus, respectively. Collectively, the unrecorded haloarchaeal strains belonged to two orders, four families, and eight genera. During the research, the possibility of discovering previously unknown species in domestic solar saltern was established. Gram-staining, cell morphology, physiological and basic biochemical parameters, and phylogenetic analysis were all performed in this study and are described in detail for each strain.

• Journal of Microbiology and Biotechnology
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• v.26 no.8
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• pp.1375-1382
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• 2016

The extremely halophilic archaeon Halobacterium noricense is a member of the genus Halobacterium. Strain CBA1132 (= KCCM 43183, JCM 31150) was isolated from solar salt. The genome of strain CBA1132 assembled with 4 contigs, including three rRNA genes, 44 tRNA genes, and 3,208 open reading frames. Strain CBA1132 had nine putative CRISPRs and the genome contained genes encoding metal resistance determinants: copper-translocating P-type ATPase (CtpA), arsenical pump-driving ATPase (ArsA), arsenate reductase (ArsC), and arsenical resistance operon repressor (ArsR). Strain CBA1132 was related to Halobacterium noricense, with 99.2% 16S rRNA gene sequence similarity. Based on the comparative genomic analysis, strain CBA1132 has distinctly evolved; moreover, essential genes related to nitrogen metabolism were only detected in the genome of strain CBA1132 among the reported genomes in the genus Halobacterium. This genome sequence of Halobacterium noricense CBA1132 may be of use in future molecular biological studies.

• Journal of Photoscience
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• v.9 no.3
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• pp.45-48
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• 2002

Microbial rhodopsins, photoactive 7-transmembrane helix proteins that use retinal as their chromophore, were observed initially in the Archaea and appeared to be restricted to extreme halophilic environments. Our understanding of the abundance and diversity of this family has been radically transformed by findings over the past three years. Genome sequencing of cultivated microbes as well as environmental genomics have unexpectedly revealed archaeal rhodopsin homologs in the other two domains of life as well, namely Bacteria and Eucarya. Organisms containing these homologs inhabit such diverse environments as salt flats, soil, freshwater, and surface and deep ocean waters, and they comprise a broad phylogenetic range of microbial life, including haloarchaea, proteobacteria, cyanobacteria, fungi, and algae. Analysis of the new microbial rhodopsins and their expression and structural and functional characterization reveal that they fulfill both ion transport and sensory functions in various organisms, and use a variety of signaling mechanisms. We have obtained the first crystallographic structure for a photosensory member of this family, the phototaxis receptor sensory rhodopsin II (SRII, also known as phoborhodopsin) that mediates blue-light avoidance by the haloarchaeon Natronobacterium pharaonis. The structure obtained from x-ray diffraction of 3D crystals prepared in a cubic lipid phase reveals key features responsible for its spectral tuning and its sensory function. The mechanism of SRII signaling fits a unified model for transport and signaling in this widespread family of phototransducers.