- Description of Polaribacter batillariae sp. nov., Polaribacter cellanae sp. nov., and Polaribacter pectinis sp. nov., novel bacteria isolated from the gut of three types of South Korean shellfish
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Su-Won Jeong , Jeong Eun Han , June-Young Lee , Ji-Ho Yoo , Do-Yeon Kim , In Chul Jeong , Jee-Won Choi , Yun-Seok Jeong , Jae-Yun Lee , So-Yeon Lee , Euon Jung Tak , Hojun Sung , Hyun Sik Kim , Pil Soo Kim , Dong-Wook Hyun , Jin-Woo Bae
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J. Microbiol. 2022;60(6):576-584. Published online April 18, 2022
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DOI: https://doi.org/10.1007/s12275-022-1604-3
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 Abstract
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Three aerobic, Gram-negative, and rod-shaped bacterial strains,
designated strains G4M1T, SM13T, and L12M9T, were isolated
from the gut of Batillaria multiformis, Cellana toreuma, and
Patinopecten yessoensis collected from the Yellow Sea in South
Korea. All the strains grew optimally at 25°C, in the presence
of 2% (w/v) NaCl, and at pH 7. These three strains, which
belonged to the genus Polaribacter in the family Flavobacteriaceae,
shared < 98.8% in 16S rRNA gene sequence and < 86.68%
in whole-genome sequence with each other. Compared with
the type strains of Polaribacter, isolates showed the highest
sequence similarity to P. haliotis KCTC 52418T (< 98.68%),
followed by P. litorisediminis KCTC 52500T (< 98.13%). All
the strains contained MK-6 as their predominant menaquinone
and iso-C15:0 as their major fatty acid. Moreover, all the
strains had phosphatidylethanolamine as their polar lipid
component. In addition, strain G4M1T had two unidentified
lipids and three unidentified aminolipids, strain SM13T had
three unidentified lipids and three unidentified aminolipids,
and strain L12M9T had three unidentified lipids and one unidentified
aminolipid. The DNA G + C contents of strains
G4M1T, SM13T, and L12M9T were 31.0, 30.4, and 29.7 mol%,
respectively. Based on phenotypic, phylogenetic, chemotaxonomic,
and genotypic findings, strains G4M1T (= KCTC 82388T
= DSM 112372T), SM13T (= KCTC 82389T = DSM 112373T),
and L12M9T (= KCTC 62751T = DSM 112374T) were classified
into the genus Polaribacter as the type strains of novel
species, for which the names Polaribacter batillariae sp. nov.,
Polaribacter cellanae sp. nov., and Polaribacter pectinis sp.
nov., respectively, have been proposed.
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Citations
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Current Microbiology.2025;[Epub] CrossRef - Isolation and characterization of Polaribacter sargassicola sp. nov. and Algibacter ulvanivorans sp. nov.: two novel species with ability to degrade algal polysaccharides
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Journal of Clinical Microbiology.2024;[Epub] CrossRef -
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Ju Hye Baek, Mahrukh Butt, Dong Min Han, Jeong Min Kim, Seohui Choi, Che Ok Jeon
International Journal of Systematic and Evolutionary Microbiology
.2024;[Epub] CrossRef - Rhodobacteraceae are Prevalent and Ecologically Crucial Bacterial Members in Marine Biofloc Aquaculture
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Journal of Microbiology.2024; 62(11): 985. CrossRef - Validation List no. 207. Valid publication of new names and new combinations effectively published outside the IJSEM
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International Journal of Systematic and Evolutionary Microbiology
.2022;[Epub] CrossRef -
Nocardioides palaemonis sp. nov. and Tessaracoccus palaemonis sp. nov., isolated from the gastrointestinal tract of lake prawn
Do-Yeon Kim, In-Chul Jeong, So-Yeon Lee, Yun-Seok Jeong, Jeong Eun Han, Euon Jung Tak, June-Young Lee, Pil Soo Kim, Dong-Wook Hyun, Jin-Woo Bae
International Journal of Systematic and Evolutionary Microbiology
.2022;[Epub] CrossRef
- Expression of the Promoter for the Maltogenic Amylase Gene in Bacillus subtilis 168
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Do-Yeon Kim , Choon-Hwan Cha , Wan-Seok Oh , Young-Jun Yoon , Jung-Wan Kim
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J. Microbiol. 2004;42(4):319-327.
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DOI: https://doi.org/2104 [pii]
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Abstract
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An additional amylase, besides the typical a-amylase, was detected for the first time in the cytoplasm of B. subtilis SUH4-2, an isolate from Korean soil. The corresponding gene (bbmA) encoded a maltogenic amylase (MAase) and its sequence was almost identical to the yvdF gene of B. subtilis 168, whose function was unknown. Southern blot analysis using bbmA as the probe indicated that this gene was ubiquitous among various B. subtilis strains. In an effort to understand the physiological function of the bbmA gene in B. subtilis, the expression pattern of the gene was monitored by measuring the [beta]-galactosidase activity produced from the bbmA promoter fused to the amino terminus of the lacZ structural gene, which was then integrated into the amyE locus on the B. subtilis 168 chromosome. The promoter was induced during the mid-log phase and fully expressed at the early stationary phase in defined media containing [beta]-cyclodextrin ([beta]-CD), maltose, or starch. On the other hand, it was kept repressed in the presence of glucose, fructose, sucrose, or glycerol, suggesting that catabolite repression might be involved in the expression of the gene. Production of the [beta]-CD hydrolyzing activity was impaired by the spo0A mutation in B. subtilis 168, indicating the involvement of an additional regulatory system exerting control on the promoter. Inactivation of yvdF resulted in a significant decrease of the [beta]-CD hydrolyzing activity, if not all. This result implied the presence of an additional enzyme(s) that is capable of hydrolyzing [beta]-CD in B. subtilis 168. Based on the results, MAase encoded by bbmA is likely to be involved in maltose and [beta]-CD utilization when other sugars, which are readily usable as an energy source, are not available during the stationary phase.
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