Journal of Microbiology

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Crystal structure of the phage-encoded N-acetyltransferase in complex with acetyl-CoA, revealing a novel dimeric arrangement: Nayeon Ki , Inseong Jo , Yongseong Hyun , Jinwook Lee , Nam-Chul Ha , Hyun-Myung Oh; J. Microbiol. 2022;60(7):746-755. Published online July 4, 2022; DOI: https://doi.org/10.1007/s12275-022-2030-2

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Bacteriophages employ diverse mechanisms to facilitate the proliferation of bacteriophages. The Salmonella-infecting phage SPN3US contains a putative N-acetyltransferase, which is widely found in bacteriophages. However, due to low sequence similarity to the N-acetyltransferases from bacteria and eukaryotic cells, the structure and function of phage-encoded acetyltransferases are mainly unknown. This study determines the crystal structure of the putative N-acetyltransferase of SPN3US in complex with acetyl-CoA. The crystal structure showed a novel homodimeric arrangement stabilized by exchanging the C-terminal α-helix within the dimer. The following biochemical analyses suggested that the phageencoded acetyltransferase might have a very narrow substrate specificity. Further studies are required to reveal the biochemical activity, which would help elucidate the interaction between the phage and host bacteria in controlling pathogenic bacteria.

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Posttranslational modifications in bacteria during phage infection
Hannelore Longin, Nand Broeckaert, Vera van Noort, Rob Lavigne, Hanne Hendrix
Current Opinion in Microbiology.2024; 77: 102425. CrossRef

Heterologous expression and enzymatic characterization of γ-glutamyltranspeptidase from Bacillus amyloliquefaciens: Jung-Min Lee , Jaejung Lee , Gyeong-Hwa Nam , Byung-Sam Son , Myoung-Uoon Jang , So-Won Lee , Byung-Serk Hurh , Tae-Jip Kim; J. Microbiol. 2017;55(2):147-152. Published online January 26, 2017; DOI: https://doi.org/10.1007/s12275-017-6638-6

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Abstract

γ-Glutamyltranspeptidase (GGT) catalyzes the cleavage of γ- glutamyl compounds and the transfer of γ-glutamyl moiety to water or to amino acid/peptide acceptors. GGT can be utilized for the generation of γ-glutamyl peptides or glutamic acid, which are used as food taste enhancers. In the present study, Bacillus amyloliquefaciens SMB469 with high GGT activity was isolated from Doenjang, a traditional fermented soy food of Korea. The gene encoding GGT from B. amyloliquefaciens SMB469 (BaGGT469) was cloned from the isolate, and heterologously expressed in E. coli and B. subtilis. For comparison, three additional GGT genes were cloned from B. subtilis 168, B. licheniformis DSM 13, and B. amyloliquefaciens FZB42. The BaGGT469 protein was composed of 591 amino acids. The final protein comprises two separate polypeptide chains of 45.7 and 19.7 kDa, generated via autocatalytic cleavage. The specific activity of BaGGT469 was determined to be 17.8 U/mg with γ-L-glutamyl-p-nitroanilide as the substrate and diglycine as the acceptor. GGTs from B. amyloliquefaciens showed 1.4- and 1.7-fold higher transpeptidase activities than those from B. subtilis and B. licheniformis, respectively. Especially, recombinant B. subtilis expressing BaGGT469 demonstrated 11- and 23-fold higher GGT activity than recombinant E. coli and the native B. amyloliquefaciens, respectively, did. These results suggest that BaGGT469 can be utilized for the enzymatic production of various γ- glutamyl compounds.

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Exploring the capacity of Bacillus species for production of kokumi γ-glutamyl peptides: A comparative study
Qian Li, Longteng Zhang, Dennis Sandris Nielsen, Lene Jespersen, René Lametsch
LWT.2024; 206: 116542. CrossRef
Functional connexion of bacterioferritin in antibiotic production and morphological differentiation in Streptomyces coelicolor
Javier García-Martín, Laura García-Abad, Ramón I. Santamaría, Margarita Díaz
Microbial Cell Factories.2024;[Epub] CrossRef
Efficient expression of γ-glutamyl transpeptidase in Bacillus subtilis via CRISPR/Cas9n and its immobilization
Qianlin Chen, Bin Wang, Li Pan
Applied Microbiology and Biotechnology.2024;[Epub] CrossRef
Biochemical Characterization of γ-Glutamyl Transpeptidase from Bacillus altitudinis IHB B1644 and Its Application in the Synthesis of l-Theanine
Eshita Sharma, Milan Kumar Lal, Arvind Gulati, Ashu Gulati
Journal of Agricultural and Food Chemistry.2023; 71(14): 5592. CrossRef
Characterization of alkaline Bacillus amyloliquefaciens γ-glutamyltranspeptidase expressed in Bacillus subtilis and its application in enzymatic synthesis of L‑Theanine
Ran Zhang, Luhua Zheng, Licheng Zhou, Longbei Xiang, Bo Jiang, Tao Zhang, Jingjing Chen
Process Biochemistry.2023; 131: 125. CrossRef
Heterologous expression, on-column refolding and characterization of gamma-glutamyl transpeptidase gene from Bacillus altitudinis IHB B1644: A microbial bioresource from Western Himalayas
Eshita Sharma, Milan Kumar Lal, Arvind Gulati, Ashu Gulati
Process Biochemistry.2022; 116: 126. CrossRef
Expression of Bacillus amyloliquefaciens γ-Glutamyltransferase in Lactococcus lactis and Immobilization on Magnetic Nanoparticles
Tiange Ma, Xingjiang Li, Xuefeng Wu, Suwei Jiang, Zhi Zheng, Dongdong Mu
ACS Food Science & Technology.2021; 1(5): 778. CrossRef
Bacterial Gamma-Glutamyl Transpeptidase, an Emerging Biocatalyst: Insights Into Structure–Function Relationship and Its Biotechnological Applications
Meenu Saini, Amuliya Kashyap, Shruti Bindal, Kuldeep Saini, Rani Gupta
Frontiers in Microbiology.2021;[Epub] CrossRef
A chemical screening method for menaquinone-producing strains based on HPLC-UV technology
Sheng Cao, Xia Du, Pingyi Li, Ganjun Yuan, Shanjun Chen, Weiping Chen, Xiaoyuan Song, Bingdi Kuang
Journal of Microbiological Methods.2020; 172: 105907. CrossRef
γ-Glutamyltranspeptidase from Bacillus amyloliquefaciens: transpeptidation activity enhancement and L-theanine production
Zelong Li, Runtao Zhu, Yongqi Liu, Jiaqi Li, Haofeng Gao, Nan Hu
Enzyme and Microbial Technology.2020; 140: 109644. CrossRef
Secretion of Bacillus amyloliquefaciens γ-Glutamyltranspeptidase from Bacillus subtilis and Its Application in Enzymatic Synthesis of l-Theanine
Dongdong Mu, Haowen Li, Qi Chen, Jing Zhu, Xuefeng Wu, Shuizhong Luo, Yanyan Zhao, Lei Wang, Shaotong Jiang, Xingjiang Li, Zhi Zheng
Journal of Agricultural and Food Chemistry.2019; 67(51): 14129. CrossRef
High level extracellular production of recombinant γ-glutamyl transpeptidase from Bacillus licheniformis in Escherichia coli fed-batch culture
Shruti Bindal, Vikas Kumar Dagar, Meenu Saini, Yogender Pal Khasa, Rani Gupta
Enzyme and Microbial Technology.2018; 116: 23. CrossRef
γ-Glutamyl Cysteine Ligase of Lactobacillus reuteri Synthesizes γ-Glutamyl Dipeptides in Sourdough
Bowen Yan, Yuan Yao Chen, Weilan Wang, Jianxin Zhao, Wei Chen, Michael Gänzle
Journal of Agricultural and Food Chemistry.2018; 66(46): 12368. CrossRef
Inference of sigma factor controlled networks by using numerical modeling applied to microarray time series data of the germinating prokaryote
E. Strakova, A. Zikova, J. Vohradsky
Nucleic Acids Research.2014; 42(2): 748. CrossRef
The effectiveness of novel bacteriocin derived from Escherichia coli colonized in the fermented pineapple Ananas comosus (L.) Merr. against pathogenic bacteria isolated from aquaculture sites
S. W. Lee, W. Wendy, L. Montira, A. U. Siti Hazirah
Veterinary World.2014; 7(11): 1014. CrossRef

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Heterologous Expression of Polygalacturonase Genes Isolated from Galactomyces citri-aurantii IJ-1 in Pichia pastoris: Il Jae Cho , In-Cheol Yeo , Nam Keun Lee , Suk Hee Jung , Young Tae Hahm; J. Microbiol. 2012;50(2):332-340. Published online April 27, 2012; DOI: https://doi.org/10.1007/s12275-012-1290-7

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Abstract: The objective of this work was to isolate the polygalacturonase genes of Galactomyces citri-aurantii IJ-1 harvested from rotten citrus peels and to heterologously express these genes in Pichia pastoris. Two polygalacturonase (PG) genes from G. citri-aurantii IJ-1 were obtained and tentatively named PG1 and PG2. The genes were cloned into pPICZαC, and expressed in Pichia pastoris strain GS115 with a native signal peptide or the α-factor secretion signal peptide of Saccharomyces cerevisiae. All of the recombinant proteins were successfully secreted into the culture media and confirmed as a single band with a molecular weight of 35 to 38 kDa by SDS-PAGE. The specific enzyme activities of recombinant PG1 and PG2 purified by His-tag affinity resin were 4,749 and 6,719 U/mg, respectively, with an optimal pH and temperature of pH 4.0 and 50°C. The Michaelis- Menten kinetic constants for PG1 and PG2, Km, were confirmed to be 0.94 and 0.84 mM, respectively. In the presence of Mn2+, the activity of PG1 and PG2 were increased to 160.8 and 146.4% of normal levels, respectively. In contrast, Cu2+ and Fe3+ acted as strong inhibitors to the PGs.

Growth Inhibition of the Yeast Transformant by the Expression of a Chitinase from Coprinellus congregatus: Hyangsoon Lim , Hyoung T. Choi; J. Microbiol. 2010;48(5):706-708. Published online November 3, 2010; DOI: https://doi.org/10.1007/s12275-010-0272-x

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Abstract: Coprinellus congregatus generates several chitinases during its entire life cycle: at the growing hyphal stage and at the mushroom autolysis stage. We have isolated a chitinase gene (chi1) from the mushroom tissue at the autolysing stage, and constructed a chitinase expression vector to get large amount of enzyme protein. Chitinase 1 (chi1) cDNA was heterologously expressed in Saccharomyces cerevisiae by gal1 promoter. The transformants showed no specific change in growth characteristics under normal growth conditions. However the expression of the gene by the gal1 promoter in the yeast transformants resulted in complete growth inhibition, while laccase expression by the gal1 promoter showed normal growth. The chitinase activities from the transformants were also more than 3 times higher than that of the recipient strain, and the chitinase expression by the real time-PCR also showed increased expression of the chi1 in the yeast transformant. Expression of a chitinase which was produced at the mushroom autolysing stage of C. congregatus resulted in yeast growth inhibition.

Molecular Cloning of the Phospholipase D Gene from Streptomyces sp. YU100 and Its Expression in Escherichia coli: Ji-Seon Lee , Munkhtsetseg Bat-Ochir , Atanas V. Demirev , Doo Hyun Nam; J. Microbiol. 2009;47(1):116-122. Published online February 20, 2009; DOI: https://doi.org/10.1007/s12275-008-0161-8

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Abstract: The gene for phospholipase D (PLD) of Streptomyces sp. YU100 was cloned from λ phage library and heterologously expressed in Escherichia coli. Using an amplified gene fragment based on the consensus sequences of streptomycetes PLDs, λ phage library of Streptomyces sp. YU100 chromosomal DNA was screened. The sequencing result of BamHI-digested 3.8 kb fragment in a positive phage clone revealed the presence of an open reading frame of a full sequence of PLD gene encoding a 540-amino acid protein including 33-amino acid signal peptide. The deduced amino acid sequence showed a high homology with other Streptomyces PLDs, having the highly conserved ‘HKD’ motifs. The PLD gene excluding signal peptide sequence was amplified and subcloned into a pET-32b(+) expression vector in E. coli BL21(DE3). The recombinant PLD was purified by nickel affinity chromatography and compared the enzyme activity with wild-type PLD. The results imply that the recombinant PLD produced by E. coli had the nearly same enzyme activity as PLD from Streptomyces sp. YU100.

Fibroblast Growth Factor 11 Inhibits Hepatitis B Virus Gene Expression Through FXRα Suppression: Mi So Seong , Jeong Ah Jang , Ye Rim Jeong , Ye Bin Kim , Yi Yi Kyaw , Hee Jeong Kong , Jung-Hyun Lee , JaeHun Cheong; J. Microbiol. 2023;61(7): 693-702.; DOI: https://doi.org/10.1007/s12275-023-00065-1

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Abstract: Fibroblast growth factor 11 (FGF11) is a member of the intracellular FGF family, which shows different signal transmission compared with other FGF superfamily members. The molecular function of FGF11 is not clearly understood. In this study, we identified the inhibitory effect of FGF11 on hepatitis B virus (HBV) gene expression through transcriptional suppression. FGF11 decreased the mRNA and protein expression of HBV genes in liver cells. While the nuclear receptor FXRα1 increased HBV promoter transactivation, FGF11 decreased the FXRα-mediated gene induction of the HBV promoter by the FXRα agonist. Reduced endogenous levels of FXRα by siRNA and the dominant negative mutant protein (aa 1–187 without ligand binding domain) of FXRα expression indicated that HBV gene suppression by FGF11 is dependent on FXRα inhibition. In addition, FGF11 interacts with FXRα protein and reduces FXRα protein stability. These results indicate that FGF11 inhibits HBV replicative expression through the liver cell-specific transcription factor, FXRα, and suppresses HBV promoter activity. Our findings may contribute to the establishment of better regimens for the treatment of chronic HBV infections by including FGF11 to alter the bile acid mediated FXR pathway.

Cloning and Characterization of a Heterologous Gene Stimulating Antibiotic Production in Streptomyces lividans TK-24: Kwon, Hyung Jin , Lee, Seung Soo , Hong, Soon Kwang , Park, Uhn Mee , Suh, Joo Won; J. Microbiol. 1999;37(2):102-110.

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Abstract: Genetic determinant for the secondary metabolism was studied in heterologous expression in Streptomyces lividans TK-24 using Streptomyces griseus ATCC 10137 as a donor strain. Chromosomal DNA of S. griseus was ligated into the high-copy number Streptomyces shuttle plasmid, pWHM3, and introduced into S. lividans TK-24. A plasmid clone with 4.3-kb BamHI DNA of S. griseus (pMJJ201) was isolated by detecting for stimulatory effect on actinorhodin production by visual inspection. The 4.3-kb BamHI DNA was cloned into pWHM3 under the control of the strong constitutive ermEp promoter in both directions (pMJJ202); ermEp promoter-mediated transcription for coding sequence reading right to left: pMJJ203; ermEp promoter-mediated transcription for coding sequence reading left to right) and reintroduced into S. lividans TK-24. The production of actinorhodin was markedly stimulated due to introduction of pMJJ202 on regeneration agar. The introduction of pMJJ202 also stimulated production of actinorhodin and undecylproidigiosin in submerged culture employing the actinorhodin production medium. Introduction of pMJJ203 resulted in a marked decrease of production of the two pigments. Nucleotide sequence analysis of the 4.3-kb region revealed three coding sequences: two coding sequences reading left to right, ORF1 and ORF2, one coding sequence reading right to left, ORF3. Therefore, it was suggested that the ORF3 product was responsible for the stimulation of antibiotic production. The C-terminal region of ORF3 product showed a local alignment with Myb-related transcriptional factors, which implicated that the ORF3 product might be a novel DNA-binding protein related to the regulation of secondary metabolism in Streptomyces.

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