Journal of Microbiology

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Sporosarcina jeotgali sp. nov., Sporosarcina oncorhynchi sp. nov., and Sporosarcina trichiuri sp. nov., Isolated from Jeotgal, a Traditional Korean Fermented Seafood: Ah-In Yang, Bora Kim, Sung-Hong Joe, Hae-In Joe, Hanna Choe, Ki Hyun Kim, Min Ok Jun, Na-Ri Shin; J. Microbiol. 2024;62(4):285-296. Published online April 8, 2024; DOI: https://doi.org/10.1007/s12275-024-00106-3

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Three novel, Gram-stain-positive, obligate aerobic, catalase- and oxidase-positive bacterial strains, designated B2O-1(T), T2O-4(T), and 0.2-SM1T-5(T), were isolated from jeotgal, a traditional Korean fermented seafood. Strains B2O-1(T), T2O-4(T), and 0.2-SM1T-5(T) exhibited distinct colony colors, characterized by pink, yellow, and red opaque circular colonies, respectively. Phylogenetic analysis revealed that three strains formed a paraphyletic clade within the genus Sporosarcina and shared < 99.0% similarity with Sporosarcina aquimarina KCTC 3840(T) and Sporosarcina saromensis KCTC 13119(T) in their 16S rRNA gene sequences. The three strains exhibiting Orthologous Average Nucleotide Identity values < 79.3% and digital DNA-DNA hybridization values < 23.1% within the genus Sporosarcina affirmed their distinctiveness. Strains B2O-1(T), T2O-4(T), and 0.2-SM1T-5(T) contained MK-7 as a sole respiratory menaquinone and A4α type peptidoglycan based on lysine with alanine, glutamic acid, and aspartic acid. The common polar lipids include diphosphatidylglycerol, phosphatidylglycerol, and phosphatidylethanolamine. Strain T2O-4(T) contained one unidentified phospholipid, whereas strain 0.2-SM1T-5(T) contained two unidentified phospholipids. Cellular fatty acid profiles, with C(15:0) anteiso as the major fatty acid, supported the affiliation of the three strains to the genus Sporosarcina. Based on the polyphasic characteristics, strains B2O-1(T) (= KCTC 43506(T) = JCM 36032(T)), T2O-4(T) (= KCTC 43489(T) = JCM 36031(T)), and 0.2-SM1T-5(T) (= KCTC 43519(T) = JCM 36034(T)) represent three novel species within the genus Sporosarcina, named Sporosarcina jeotgali sp. nov., Sporosarcina oncorhynchi sp. nov., and Sporosarcina trichiuri sp. nov., respectively.

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Notification of changes in taxonomic opinion previously published outside the IJSEM. List of Changes in Taxonomic Opinion no. 41
Aharon Oren, Markus Göker
International Journal of Systematic and Evolutionary Microbiology .2025;[Epub] CrossRef
Brevibacterium koreense sp. nov., a moderately halophilic bacterium isolated from jogae-jeotgal, a Korean fermented seafood
Sohee Nam, Yujin Kim, Min Ji Lee, Yeon Bee Kim, Jeong Ui Yun, Mi-Ja Jung, Hye Seon Song, Se Hee Lee, Seok-Jun Kim, Tae Woong Whon
International Journal of Systematic and Evolutionary Microbiology .2025;[Epub] CrossRef
Validation List no. 220. Valid publication of new names and new combinations effectively published outside the IJSEM
Aharon Oren, Markus Göker
International Journal of Systematic and Evolutionary Microbiology .2024;[Epub] CrossRef

Crystal structure of the inactive state of the receiver domain of Spo0A from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier: Chang Woo Lee , Sun-Ha Park , Sung Gu Lee , Seung Chul Shin , Se Jong Han , Han-Woo Kim , Hyun Ho Park , Sunghwan Kim , Hak Jun Kim , Hyun Park , HaJeung Park , Jun Hyuck Lee; J. Microbiol. 2017;55(6):464-474. Published online March 9, 2017; DOI: https://doi.org/10.1007/s12275-017-6599-9

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Abstract

The two-component phosphorelay system is the most pre-valent mechanism for sensing and transducing environ-mental signals in bacteria. Spore formation, which relies on the two-component phosphorelay system, enables the long- term survival of the glacial bacterium Paenisporosarcina sp. TG-14 in the extreme cold environment. Spo0A is a key re-sponse regulator of the phosphorelay system in the early stage of spore formation. The protein is composed of a regu-latory N-terminal phospho-receiver domain and a DNA- binding C-terminal activator domain. We solved the three- dimensional structure of the unphosphorylated (inactive) form of the receiver domain of Spo0A (PaSpo0A-R) from Paenisporosarcina sp. TG-14. A structural comparison with phosphorylated (active form) Spo0A from Bacillus stearo-thermophilus (BsSpo0A) showed minor notable differences. A molecular dynamics study of a model of the active form and the crystal structures revealed significant differences in the α4 helix and the preceding loop region where phosphorylation occurs. Although an oligomerization study of PaSpo0A-R by analytical ultracentrifugation (AUC) has shown that the protein is in a monomeric state in solution, both crosslinking and crystal-packing analyses indicate the possibility of weak dimer formation by a previously undocumented mechanism. Collectively, these observations provide insight into the me-chanism of phosphorylation-dependent activation unique to Spo0A.

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Identification of Functional Spo0A Residues Critical for Sporulation in Clostridioides difficile
Michael A. DiCandia, Adrianne N. Edwards, Joshua B. Jones, Grace L. Swaim, Brooke D. Mills, Shonna M. McBride
Journal of Molecular Biology.2022; 434(13): 167641. CrossRef

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