- Inferences in microbial structural signatures of acne microbiome and mycobiome
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Jubin Kim , Taehun Park , Hye-Jin Kim , Susun An , Woo Jun Sul
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J. Microbiol. 2021;59(4):369-375. Published online February 10, 2021
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DOI: https://doi.org/10.1007/s12275-021-0647-1
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Acne vulgaris, commonly known as acne, is the most common
skin disorder and a multifactorial disease of the sebaceous
gland. Although the pathophysiology of acne is still
unclear, bacterial and fungal factors are known to be involved
in. This study aimed to investigate whether the microbiomes
and mycobiomes of acne patients are distinct from those of
healthy subjects and to identify the structural signatures of
microbiomes related to acne vulgaris. A total of 33 Korean
female subjects were recruited (Acne group, n = 17; Healthy
group, n = 16), and microbiome samples were collected swabbing
the forehead and right cheek. To characterize the fungal
and bacterial communities, 16S rRNA V4–V5 and ITS1 region,
respectively, were sequenced and analysed using Qiime2.
There were no significant differences in alpha and beta diversities
of microbiomes between the Acne and Healthy groups.
In comparison with the ratio of Cutibacterium to Staphylococcus,
the acne patients had higher abundance of Staphylococcus
compared to Cutibacterium than the healthy individuals.
In network analysis with the dominant microorganism
amplicon sequence variants (ASV) (Cutibacterium, Staphylococcus,
Malassezia globosa, and Malassezia restricta) Cutibacterium
acnes was identified to have hostile interactions
with Staphylococcus and Malassezia globosa. Accordingly, this
results suggest an insight into the differences in the skin microbiome
and mycobiome between acne patients and healthy
controls and provide possible microorganism candidates that
modulate the microbiomes associated to acne vulgaris.
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- Enhanced Production of Carboxymethylcellulase by a Marine Bacterium, Bacillus velezensis A-68, by Using Rice Hulls in Pilot-scale Bioreactor under Optimized Conditions for Dissolved Oxygen
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Wa Gao , Hye-Jin Kim , Chung-Han Chung , Jin-Woo Lee
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J. Microbiol. 2014;52(9):755-761. Published online July 30, 2014
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DOI: https://doi.org/10.1007/s12275-014-4156-3
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550
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The optimal conditions for the production of carboxymethylcellulase (CMCase) by Bacillus velezensis A-68 at a flask scale have been previously reported. In this study, the parameters involved in dissolved oxygen in 7 and 100 L bioreactors were optimized for the pilot-scale production of CMCase. The optimal agitation speed and aeration rate for cell growth of B. velezensis A-68 were 323 rpm and 1.46 vvm in a 7 L bioreactor, whereas those for the production of CMCase were 380 rpm and 0.54 vvm, respectively. The analysis of variance (ANOVA) implied that the highly significant factor for cell growth was the aeration rate, whereas that for the production of CMCase was the agitation speed. The optimal inner pressures for cell growth and the production of CMCase by B. velezensis A-68 in a 100 L bioreactor were 0.00 and 0.04 MPa, respectively. The maximal production of CMCase in a 100 L bioreactor under optimized conditions using rice hulls was 108.1 U/ml, which was 1.8 times higher than that at a flask scale under previously optimized conditions.
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- Role of RNA Polymerase II Carboxy Terminal Domain Phosphorylation in DNA Damage Response
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Su-Jin Jeong , Hye-Jin Kim , Yong-Jin Yang , Ja-Hwan Seol , Bo-Young Jung , Jeong-Whan Han , Hyang-Woo Lee , Eun-Jung Cho
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J. Microbiol. 2005;43(6):516-522.
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DOI: https://doi.org/2296 [pii]
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Abstract
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The phosphorylation of C-terminal domain (CTD) of Rpb1p, the largest subunit of RNA polymerase II plays an important role in transcription and the coupling of various cellular events to transcription. In this study, its role in DNA damage response is closely examined in Saccharomyces cerevisiae, focusing specifically on several transcription factors that mediate or respond to the phosphorylation of the CTD. CTDK-1, the pol II CTD kinase, FCP1, the CTD phosphatase, ESS1, the CTD phosphorylation dependent cis-trans isomerase, and RSP5, the phosphorylation dependent pol II ubiquitinating enzyme, were chosen for the study. We determined that the CTD phosphorylation of CTD, which occurred predominantly at serine 2 within a heptapeptide repeat, was enhanced in response to a variety of sources of DNA damage. This modification was shown to be mediated by CTDK-1. Although mutations in ESS1 or FCP1 caused cells to become quite sensitive to DNA damage, the characteristic pattern of CTD phosphorylation remained unaltered, thereby implying that ESS1 and FCP1 play roles downstream of CTD phosphorylation in response to DNA damage. Our data suggest that the location or extent of CTD phosphorylation might be altered in response to DNA damage, and that the modified CTD, ESS1, and FCP1 all contribute to cellular survival in such conditions.
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