• Title/Summary/Keyword: Subcellular

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Subcellular Location of Five Isozymes in Populus Species by Isozyme Analysis with Whole Plant and Mitochondria (포플러류(類)의 식물체(植物體)와 미토콘드리아의 동위효소(同位酵素) 분석(分析)에 의(依)한 몇 동위효소(同位酵素)의 세포소기관적(細胞小器管的) 위치(位置))

  • Ryu, Jang Bal;Noh, Eun Woon;Son, Doo Sik
    • Journal of Korean Society of Forest Science
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    • v.80 no.1
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    • pp.97-102
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    • 1991

  • Subcellular location of five isozymes in Populus species was studied by isozyme analysis with plant and mitochondria. Isozymes analyzed were ADH, 6-PGD, MDH, PGI, and Diaptrorase. ADH seems to be cytosolic isozyme encoded with nuclear genes at one locus, while 6-PGD seems to be mitochondrial one. MDH showed three hands in cytosol and four other bands in mitochondria. Three cytosolic hands were showed for PGI. Diaphorase showed one mitochodrial band and two cytosofic bands which seemed to the encoded by nuclear genes at one locus.

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Identification and Characterization of Two Novel Variants of the DUF1208 Protein FAM92A1

  • Ruan, Xu Zhi;Yan, Fei;Zhao, Xin Yu;Wang, Chung Ting;Song, Ming;Yang, Han Suo;Deng, Hong Xin;Wei, Yu Quan
    • Molecules and Cells
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    • v.23 no.3
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    • pp.391-397
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    • 2007

  • FAM92A1 (named FAM92A1-271) belongs to the family of proteins with conserved DUF1208 domains. Its function remains elusive. We identified two novel transcript variants (FAM92A1-251, FAM92A1-289) of FAM92A1. The presence of these transcripts in cancerous and normal cells, as well as their influence on cell prolifera-tion and apoptosis, were investigated. The subcellular location of FAM92A1 was determined by fluorescence microscopy. We found that FAM92A1-271 and FAM92A1-289 were highly expressed in both normal and cancerous cells, but FAM92A1-251 was only expressed at a mo-derate level in both types of cell. Overexpression of FAM92A1-271, FAM92A1-251 and FAM92A1-289 inhibited cell proliferation, caused S-phase arrest and induced apoptosis. Subcellular localization showed that FAM92A1 localizes to the nucleus. Our results show that FAM92A1 has different splicing variants, and that it may take part in regulating cell proliferation and apoptosis.

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Protein transduction of an antioxidant enzyme: subcellular localization of superoxide dismutase fusion protein in cells

  • Kim, Dae-Won;Kim, So-Young;Lee, Hwa;Lee, Yeum-Pyo;Lee, Min-Jung;Jeong, Min-Seop;Jang, Sang-Ho;Park, Jin-Seu;Lee, Kil-Soo;Kang, Tae-Cheon;Won, Moo-Ho;Cho, Sung-Woo;Kwon, Oh-Shin;Eum, Won-Sik;Choi, Soo-Young
    • BMB Reports
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    • v.41 no.2
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    • pp.170-175
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    • 2008

  • In protein therapy, it is important for exogenous protein to be delivered into the target subcellular localization. To transduce a therapeutic protein into its specific subcellular localization, we synthesized nuclear localization signal (NLS) and membrane translocation sequence signal (MTS) peptides and produced a genetic in-frame SOD fusion protein. The purified SOD fusion proteins were efficiently transduced into mammalian cells with enzymatic activities. Immunofluorescence and Western blot analysis revealed that the SOD fusion proteins successfully transduced into the nucleus and the cytosol in the cells. The viability of cells treated with paraquat was markedly increased by the transduced fusion proteins. Thus, our results suggest that these peptides should be useful for targeting the specific localization of therapeutic proteins in various human diseases.

  • https://doi.org/10.5483/BMBRep.2008.41.2.170 인용 PDF

Subcellular Localization of Novel Stress Protein VISP (새로운 스트레스 단백질인 VISP의 세포내 위치)

  • Moon, Chang-Hoon;Yoon, Won-Joon;Ko, Myoung-Seok;Kim, Hyun-Ju;Park, Jeong-Woo
    • Korean Journal of Microbiology
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    • v.42 no.4
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    • pp.271-276
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    • 2006

  • Previously we demonstrated that virus-inducible stress protein (VISP) is induced in fish cells by the infection of a fish rhabdovirus. In this paper, we investigated the subcellular localization of the VISP and determined the region of VISP responsible for the subcellular localization. The CHSE-214 cells were stained with monoclonal antibody raised against VISP and observed with confocal microscope to detect the endogenous VISP. The results showed that the VISP localizes to the perinuclear region as spots. A plasmid expressing VISP fused to enhanced green fluorescent protein (EGFP) was constructed. The transient expression of full-length VISP fused to EGFP in CHSE-214 cells confirmed the spot formation of the VISP at perinuclear region. To determine the region responsible for the perinuclear localization of the VISP, we constructed a series of deletion mutants and, by using these deletion mutants, we found that C-terminal region of the VISP (aa 612-710) is essential for the perinuclear distribution of VISP and that this region contained nuclear receptor binding motif (691-TLTSLLL-697). Our results suggest that VISP localizes to the perinuclear region and C-terminal regions are important for this localization. Further studies on the role of the perinuclear localization of VISP in IHNV growth mali reveal the novel mechanism of IHNV pathogenecity.

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