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Loss of ALG3 function (alg3) Leads to Enhanced ER Quality Control (ERQC) in Arabidopsis thaliana
Bo Hwa Son,Wahyu Indra Fanata,Jae Yong Yoo,Rikno Harmoko,Ki Seong Ko,Nirmal Kumar Ramasamy,Kyung Hwa Kim,Thiyagarajan Thulasinathan,Sang Yeol Lee,Kyun Oh Lee 한국당과학회 2012 한국당과학회 학술대회 Vol.2012 No.1
In plants, glycoproteins have been implicated in a wide variety of cellular processes including production of cell walls, pollination, pathogen defence and cell-to-cell communication. In addition, they have attracted considerable interest from the medical field as the main cause of food and pollen allergies. N-glycosylation is a complex process that encompasses the biosynthesis and modification of sugar moieties in the endoplasmic reticulum (ER) and Golgi. The core oligosaccharide Glc3Man9GlcNAc2 is assembled by a series of membrane-bound glycosyltransferases as the lipid carrier dolichylpyrophosphate-linked glycan in the endoplasmic reticulum (ER). The first step of this assembly pathway on the ER luminal side is mediated by ALG3 (asparagine-linked glycosylation 3), which is a highly conserved reaction among eukaryotic cells. In Arabidopsis ALG3 mutant (alg3), an immature lipid-linked oligosaccharide structure, M5ER, was synthesized and efficiently processed into complex-type glycans. Although no high-mannose-type glycoproteins are detected in alg3 plants, these plants do not show a growth phenotype under normal growth conditions. However, the glycosylation abnormalities result in activation of marker genes diagnostic of the unfolded protein response and alg3 mutant showed a stress sensitive phenotype. These results indicate that ALG3 is a critical factor for correct N-glycosylation of proteins and is involved in the ER stress response.
Bo Hwa Son,In Jung Jung,Jeong Chan Moon,Joo Mi Jeon,Wahyu Indra Fanata,Jae Yong Yoo,Jae Ho Cha,Je Hein Kim,Rikno Harmoko,Ki Seong Ko,Sang Yeol Lee,Kyun Oh Lee 한국당과학회 2009 한국당과학회 학술대회 Vol.2009 No.1
N-glycosylation is a major post-translational protein modification, which alters physicochemical properties of the protein, affecting the folding, distribution, stability and thus biological function and efficiency of protein. Plant type complex N-glycans are distinctive from those found in mammalian because they contain β1,2-xylose and core α 1,3-fucose residues attached to the pentasaccharide (Man3GlcNAc2) core structure but no sialic acid residues. The presence of β1,2-xylose and core α1,3-fucose residues on plant type complex N-glycans has long been an irritating limitation in the use of plant-made pharmaceuticals (PMPs) in human therapy, as these N-glycan epitopes are potentially immunogenic in mammals. In this study, to remove the plant specific sugar residues and humanize the N-glycosylation in plant, we isolated mutants of the corresponding plant specific glycosyltransferase genes (α1,3-fucosyltransferase I, α1,3-fucosyltransferase II, β 1,2-xylosyltransferase, β1,3-galactosyltransferase and α1,4-fucosyltransferase). We made double, triple and quadruple mutants by crossing the mutants, and quintuple mutant is on the construction. The triple (fuct1/fuct2/xylt) and quadruple (fuct1/fuct2/xylt/fuct3) mutants do not show significant developmental defects in a normal growth condition and they do not produce the plant specific sugar residues on the N-glycan. The resulting mutant will be transformed by human α1,6-fucosyltransferase and β1,4-galactosyltransferase genes to accomplish further humanized N-glycosylation in plant. [Supported by BK21 program]
Bo-Hwa Son,Chul-Gyoo Park,Dhruba Khakurel,Hae-Jun Hwang,Tea-Won Kim,Byeong-Gyun Jeon,Sung-Ho Lee 경상대학교 농업생명과학연구원 2022 농업생명과학연구 Vol.56 No.5
Protoplasts were isolated from the primary leaves of lettuce (Lactuca sativa L.) seedlings 10 days after in vitro germination. The leaves were stripped and incubated in an enzyme mixture consisting of 1.2% Cellulase R-10 and 0.3% Macerozyme R-10 in cell and protoplast washing solution (CPW) overnight. The average protoplast yield was 8.25 x 106 protoplasts per g of fresh leaf tissue. When protoplasts were cultured at a density of 3.0 × 105 protoplasts/mL in agarose solid KM8P/KM8 medium, first and second divisions were observed in the protoplasts within a week. Protoplast-derived microcolonies formed after 4 weeks of culture, and visible colonies were present after 3 months of culture. Protoplast-derived microcalli were transferred to Murashige and Skoog medium supplemented with 2.0 mg/L kinetin and 0.1 mg/L NAA and incubated in the light for 3 weeks. They grew into callus, which then regenerated into plants after 7 weeks of culture. The regenerated plants grew as apparently normal flowering fertile plants.
Bo Hwa Son,In Jung Jung,Jeong Chan Moon,Joo Mi Jeon,Wahyu Indra Fanata,Jae Yong Yoo,Jae Ho Cha,Je Hein Kim,Rikno Harmoko,Ki Seong Ko,Sang Yeol Lee,Kyun Oh Lee 한국당과학회 2009 한국당과학회 학술대회 Vol.2009 No.1
N-glycosylation is a major post-translational protein modification, which alters physicochemical properties of the protein, affecting the folding, distribution, stability and thus biological function and efficiency of protein. β1,2-xylose and core α1,3-fucose residues on plant type complex N-glycans are potentially immunogenic in mammals. In this study, to remove the plant specific sugar residues and humanize the N-glycosylation in plant, we isolated mutants corresponding plant glycosyltransferase genes (N-acetylglucosaminyltransferaseI, N-acetylglucosaminyltransferaseII, α 1,3-fucosyltransferaseI, α1,3-fucosyltransferaseII, β1,2-xylosyltransferase, β 1,3-galactosyltransferase, α1,4-fucosyltransferase). Double, triple, quadruple and quintuple mutants were made by crossing the mutants and two quadruple mutants (fuct1/fuct2/xylt/gntII), (fuct1/fuct2/xylt/galt) are on the construction. The triple (fuct1/fuct2/xylt) and quadruple (fuct1/fuct2/xylt/fuct3), quintuple (fuct1/fuct2/xylt/fuct3/galt) mutants did not show significant developmental defects in a normal growth condition and they did not produce the plant specific sugar residues on the N-glycan. [Supported by BK21 program]
[P423] Two cases of unilateral linear syringoma on trunk following Blaschko lines
( Bo Young Kim ),( Sook In Ryu ),( Ji Hyun Park ),( Seung Hyun Chun ),( Sang Wook Son ),( Hwa Jung Ryu ) 대한피부과학회 2017 대한피부과학회 학술발표대회집 Vol.69 No.1
Syringoma is a benign adnexal tumor arising from the ducts of eccrine sweat glands. They are flesh-colored or light brown small papules, localized most commonly on the lower eyelids and malar area. The lesions usually are bilateral and symmetrically distributed. We report two cases of unilateral linear syringoma following Blaschko`s line. We describe a 24-year-old male with mild itchy brownish papule on left upper flank of two years duration and 28-year-old female with a five-year history of asymptomatic brownish papules on left abdomen and flank. Histological examination showed multiple dilated eccrine ducts which were lined by two rows of epithelial cells. Some of the ducts had small comma-like tails of epithelial cells, giving them the appearance of tadpoles. The clinico-pathological features suggested the diagnosis of unilateral linear syringoma. Unilateral cases of syringoma following Blaschko`s lines are quite uncommon in the literature and have been reported to be localized on the extensor aspect of the right upper arm and the right chest. To our knowledge, this is the first case of unilateral linear syringoma on trunk following Blaschko`s lines. The development of syringoma following Blaschko`s lines suggests that a somatic mutation may underlie the pathogenesis of this dermatosis. Syringoma should be included in the differential diagnoses when we encounter linearly arranged skin lesions for the pathological examination.
( Hwa Jin Suh ),( Yeon Ju Kim ),( Hea Son Bang ),( Eun Young Yun ),( Seong Ryul Kim ),( Kwan Ho Park ),( Bo Ram Kang ),( Ik Soo Kim ),( Jae Pil Jeon ),( Jae Sam Hwang ) 한국잠사학회 2008 International Journal of Industrial Entomology Vol.17 No.2
A novel beetle antimicrobial protein from stimulated Copris tripartitus and the corresponding gene were isolated in parallel through differential display-PCR and expression in Escherichia coli. To find cDNA clones responsible for bacteria resistance, the suppression subtractive hybridization and GeneFishing differentially expressed genes system were employed in the dung beetle, Copris tripartitus immunized with lipopolysaccaride. One cDNA clone from eight subtracted clones was selected through dot blot analysis and confirmed by northern blot analysis. The 516-bp, selected cDNA clone was determined by 5` and 3` rapid amplication of cDNA ends and cloned into the GST fusion expression vector pGEX-4T-1 for expression of the protein. The expressed protein was predicted 14.7 kDa and inhibited the growth of gram-negative bacteria such as Escherichia coli and Pseudomonas aeruginosa. These results implied that the expressed protein is related to immune defense mechanism against microorganism.