Journal of Microbiology

Journal Article

Core promoter mutation of nucleotides A1762T and G1764A of hepatitis B virus increases core promoter transactivation by hepatocyte nuclear factor 1: Mi So Seong , Hyeon Jeong Hwang , Eun Ah Jang , Jeong Ah Jang , Wah Wah Aung , Yi Yi Kyaw , JaeHun Cheong; J. Microbiol. 2022;60(10):1039-1047. Published online September 27, 2022; DOI: https://doi.org/10.1007/s12275-022-1675-1

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Abstract: Hepatitis B virus (HBV) infection highly increases the risk for liver cirrhosis and hepatocellular carcinoma (HCC). The clinical manifestation of HBV infection is determined by the mutual interplay of the viral genotype, host genetic factors, mode of transmission, adaptive mutations, and environmental factors. Core promoter activation plays a critical role in the pre-genomic RNA transcription of HBV for HBV replication. The mutations of core promoter have been implicated in HCC development. We had obtained HBV genes from Myanmar HBV infectants and identified gene variations at the core promoter region. For measuring the relative transactivation activity on core promoter, we prepared the core-promoter reporter construct. Both of A1762T and G1764A mutation were consistently found in the HBV genes with hepatocellular carcinoma. The A1762T/G1764A mutation was corresponding to K130M/V131I of HBx protein. We prepared the core promoter- luciferase reporter construct containing the double A1762T/G1764A mutation and the K130M/V131I HBx protein expression construct. The A1762T/G1764A mutation highly was responsive to core promoter transactivation by HBx, regardless of HBx mutation. The A1762T/G1764A mutation newly created hepatocyte nuclear factor 1 (HNF1) responsive element. Ectopic expression of HNF1 largely increased the HBV core promoter containing A1762T/G1764A mutation. In addition, hepatic rich fatty acid, palmitic acid and oleic acid, increased K130M/V131I HBx level by core promoter activation. These results provide biological properties and clinical significance of specific HBV core promoter mutants related with HCC development.

Review

Prokaryotic DNA methylation and its functional roles: Hoon Je Seong , Sang-Wook Han , Woo Jun Sul; J. Microbiol. 2021;59(3):242-248. Published online February 23, 2021; DOI: https://doi.org/10.1007/s12275-021-0674-y

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29 Citations

Abstract: DNA methylation is known as a universal mechanism of epigenetic regulation in all kingdoms of life. Particularly, given that prokaryotes lack key elements such as histones and nucleosomes that can structurally modify DNA, DNA methylation is considered a major epigenetic regulator in these organisms. However, because DNA methylation studies have focused primarily on eukaryotes, the mechanism of prokaryotic DNA methylation has been less studied than in eukaryotes. DNA methylation in prokaryotes plays an important role in regulating not only the host defense system, but also the cell cycle, gene expression, and virulence that can respond directly to the environment. Recent advances in sequencing techniques capable of detecting methylation signals have allowed for the characterization of prokaryotic genome-wide epigenetic regulation. In this review, we describe representative examples of cellular events regulated by DNA methylation in prokaryotes, from early studies to current applications.

Journal Article

A comprehensive in silico analysis of sortase superfamily: Adeel Malik , Seung Bum Kim; J. Microbiol. 2019;57(6):431-443. Published online May 27, 2019; DOI: https://doi.org/10.1007/s12275-019-8545-5

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16 Citations

Abstract: Sortases are cysteine transpeptidases that assemble surface proteins and pili in their cell envelope. Encoded by all Grampositive bacteria, few Gram-negative bacteria and archaea, sortases are currently divided into six classes (A-F). Due to the steep increase in bacterial genome data in recent years, the number of sortase homologues have also escalated rapidly. In this study, we used protein sequence similarity networks to explore the taxonomic diversity of sortases and also to evaluate the current classification of these enzymes. The resultant data suggest that sortase classes A, B, and D predominate in Firmicutes and classes E and F are enriched in Actinobacteria, whereas class C is distributed in both Firmicutes and Actinobacteria except Streptomyces family. Sortases were also observed in various Gram-negatives and euryarchaeota, which should be recognized as novel classes of sortases. Motif analysis around the catalytic cysteine was also performed and suggested that the residue at 2nd position from cysteine may help distinguish various sortase classes. Moreover, the sequence analysis indicated that the catalytic arginine is highly conserved in almost all classes except sortase F in which arginine is replaced by asparagine in Actinobacteria. Additionally, class A sortases showed higher structural variation as compared to other sortases, whereas inter-class comparisons suggested structures of class C and D2 exhibited best similarities. A better understanding of the residues highlighted in this study should be helpful in elucidating their roles in substrate binding and the sortase function, and successively could help in the development of strong sortase inhibitors.

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