Journal of Microbiology

Doo-Byoung Oh

2 Articles

Probing the ArcA Regulon in the Rumen Bacterium Mannheimia succiniciproducens by Genome-Wide Expression Profiling: Seulgi Yun , Jong Moon Shin , Oh-Cheol Kim , Young Ryul Jung , Doo-Byoung Oh , Sang Yup Lee , Ohsuk Kwon; J. Microbiol. 2012;50(4):665-672. Published online July 21, 2012; DOI: https://doi.org/10.1007/s12275-012-2007-7

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In this study, the putative target genes of the Arc two-component system of the rumen bacterium Mannheimia succiniciproducens were determined by analyzing the transcriptome of the ArcA overexpression strain and by the in silico scanning of the entire genome sequence with the position weight matrix of the ArcA binding sequence developed for Escherichia coli. The majority of 79 repressed genes were involved in energy metabolism and carbohydrate transport and metabolism, while the majority of 82 induced genes were involved in hypothetical or unknown functions. Our results suggest that the Arc system in M. succiniciproducens has a specific function that differs from that in E. coli.

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The CpxRA Two-Component System is Involved in the Maintenance of the Integrity of the Cell Envelope in the Rumen Bacterium Mannheimia succiniciproducens
Seulgi Yun, Eun-Gyeong Lee, Sang-Yoon Kim, Jong Moon Shin, Won Seok Jung, Doo-Byoung Oh, Sang Yup Lee, Ohsuk Kwon
Current Microbiology.2015; 70(1): 103. CrossRef

Remodeling of the Glycosylation Pathway in the Methylotrophic Yeast Hansenula polymorpha to Produce Human Hybrid-Type N-Glycans: Seon Ah Cheon , Hyunah Kim , Doo-Byoung Oh , Ohsuk Kwon , Hyun Ah Kang; J. Microbiol. 2012;50(2):341-348. Published online April 27, 2012; DOI: https://doi.org/10.1007/s12275-012-2097-2

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As a step forward to achieve the generation of human complex- type N-glycans in the methylotrophic yeast Hansenula polymorpha, we here report the modification of the yeast glycosylation pathway by heterologous expression of the human gene encoding β-1,2-N-acetylglucosaminyltransferase I (GnTI). For the optimal expression of human GnTI in the yeast Golgi compartment, the catalytic domain of the GnTI was fused to various N-terminal leader sequences derived from the yeast type II membrane proteins. The vectors containing GnTI fusion constructs were introduced into the H. polymorpha och1Δ single and och1Δalg3Δ double mutant strains expressing the ER-targeted Aspergillus saitoi α-1,2 mannosidase, respectively. Both of the glycoengineered Hpoch1Δ and Hpoch1ΔHpalg3Δ strains were shown to produce successfully the hybrid-type glycans with a monoantennary N-acetylglucosamine (GlcNAc1Man5GlcNAc2 and GlcNAc1Man3GlcNAc2, respectively) by N-glycan profile analysis of cell wall proteins. Furthermore, by comparative analysis of byproduct formation and the glycosylation site occupancy, we propose that the Hpoch1Δ strain would be more suitable than the Hpoch1ΔHpalg3Δ strain as a host for the production of recombinant proteins with humanized glycans.

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