Yoshiko Iida

Prefectural University of Hiroshima

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Nobuo Nakanishi

Hamamatsu University School of Medicine

T Kameyama

Ajinomoto (Japan)

Masayo Kojima

National Center for Geriatrics and Gerontology

Kazuya Oguro

University of Thessaly

Hiroyuki Hasegawa

Saga University

Tadao Horiuchi

Kyushu University

Yasumi Ohshima

Kyushu University

Keiko Sawabe

Animal Husbandry and Veterinary Department

Motoo Matsuda

Azabu University

Takatsugu Yamada

Yamato Municipal Hospital

Cooperative Institutions

Kyushu University

University of Nottingham

Queen's Medical Centre

Kyushu University Hospital

Teikyo University of Science

Korea University of Science and Technology

Nihon University

University of Science and Technology

Biotechnology Research Center

Azabu University

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Electrophoretic characterization of low molecular weight RNAs from prokaryotic and eukaryotic cells.

SEIBUTSU BUTSURI KAGAKU (1986)

Motoo Matsuda Takatsugu Yamada Takahiro Nomura Yoshiko Iida T Kameyama

Low molecular weight RNAs (small RNAs=sRNAs) from prokaryotic and eukaryotic cells were analyzed parallely by electrophoresis in an agarose-polyacrylamide composite gel and a 7M urea-10% polyacrylamide gel.Induced by chloromycetin, three major sRNAs (approx. 190, 240 and 320 nucleotides long) were found to be synthesized during germination of Bacillus subtilis spores. These RNAs were distinct from the commonly occurring 4S, 4.5S and 5S RNAs.The U-series small nuclear RNAs (U-snRNAs) from KB cell nuclei were also separated by gel electrophoresis. The number of U-snRNA molecules in the cell nucleus was calculated using a reported value for U1 RNA as the standard. When the number of U1 RNA was 1×106 molecules in a cell, those of U2, U4, U5 and U6 RNAs were estimated to be 2.7×105, 1.3×105, 5.4×104 and 1.3×105 molecules, respectively.In F9 cells, a mouse teratocarcinoma cell line, U1a and U1b RNA were observed as to U1 RNA.In each gel electrophoresis, the logarithms of the (assummed) molecular weights of sRNAs were inversely proportional to the mobility.

Small nuclear RNA

Agarose gel electrophoresis

Agarose

10.2198/sbk.30.201

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Rapid Turnover of Tryptophan Hydroxylase: The Turnover Rate is Unaffected after Elevation of the Enzyme Amount Induced by Treatment of Cells with Calcium Ionophores and Protease Inhibitors

Pteridines (1996)

Masayo Kojima Yoshiko Iida Kazumasa Yamamoto Kazuya Oguro Nobuo Nakanishi

Article Rapid Turnover of Tryptophan Hydroxylase: The Turnover Rate is Unaffected after Elevation of the Enzyme Amount Induced by Treatment of Cells with Calcium Ionophores and Protease Inhibitors was published on August 1, 1996 in the journal Pteridines (volume 7, issue 3).

Protein turnover

Turnover

10.1515/pteridines.1996.7.3.94

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Citations (1)

Regulation of the lactose operon in vitro

MGG Molecular & General Genetics (1970)

Yoshiko Iida T Kameyama Yasumi Ohshima Tadao Horiuchi

Transcription

gal operon

Small nuclear RNA

10.1007/bf00324047

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Citations (9)

Regulation of the lactose operon in vitro

MGG Molecular & General Genetics (1970)

Yasumi Ohshima Tadao Horiuchi Yoshiko Iida T Kameyama

Inducer

Lac repressor

gal operon

L-arabinose operon

Enzyme Repression

Transcription

10.1007/bf00324048

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Citations (8)

Proteasome‐driven turnover of tryptophan hydroxylase is triggered by phosphorylation in RBL2H3 cells, a serotonin producing mast cell line

European Journal of Biochemistry (2002)

Yoshiko Iida Keiko Sawabe Masayo Kojima Kazuya Oguro Nobuo Nakanishi

We previously demonstrated in mast cell lines RBL2H3 and FMA3 that tryptophan hydroxylase (TPH) undergoes very fast turnover driven by 26S‐proteasomes [Kojima, M., Oguro, K., Sawabe, K., Iida, Y., Ikeda, R., Yamashita, A., Nakanishi, N. & Hasegawa, H. (2000) J. Biochem (Tokyo) 2000, 127 , 121–127]. In the present study, we have examined an involvement of TPH phosphorylation in the rapid turnover, using non‐neural TPH. The proteasome‐driven degradation of TPH in living cells was accelerated by okadaic acid, a protein phosphatase inhibitor. Incorporation of 32 P into a 53‐kDa protein, which was judged to be TPH based on autoradiography and Western blot analysis using anti‐TPH serum and purified TPH as the size marker, was observed in FMA3 cells only in the presence of both okadaic acid and MG132, inhibitors of protein phosphatase and proteasome, respectively. In a cell‐free proteasome system constituted mainly of RBL2H3 cell extracts, degradation of exogenous TPH isolated from mastocytoma P‐815 cells was inhibited by protein kinase inhibitors KN‐62 and K252a but not by H89. Consistent with the inhibitor specificity, the same TPH was phosphorylated by exogenous Ca 2+ /calmodulin‐dependent protein kinase II in the presence of Ca 2+ and calmodulin but not by protein kinase A (catalytic subunit). TPH protein thus phosphorylated by Ca 2+ /calmodulin‐dependent protein kinase II was digested more rapidly in the cell‐free proteasome system than was the nonphosphorylated enzyme. These results indicated that the phosphorylation of TPH was a prerequisite for proteasome‐driven TPH degradation.

MG132

Protein Degradation

10.1046/j.1432-1033.2002.03188.x

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Citations (21)

Stimulation of tryptophan hydroxylase production in a serotonin‐producing cell line (RBL2H3) by intracellular calcium mobilizing reagents

FEBS Letters (1996)

Hiroyuki Hasegawa Masayo Kojima Yoshiko Iida Kazuya Oguro Nobuo Nakanishi

RBL2H3 cells showed a remarkable increase in their level of tryptophan hydroxylase (up to 25‐fold), the rate‐limiting enzyme in serotonin biosynthesis, by stimulation with intracellular calcium mobilizers A23187, thapsigargin, and t BuBHQ as well as by stimulation with an antigen in the presence of IgE. The increase in the enzyme protein was visualized by Western blot analysis using anti‐tryptophan hydroxylase antiserum. The enzyme turnover (Hasegawa et al., FEBS Lett ., 368 (1995) 151–154) was not showed down during the rise in tryptophan hydroxylase. Actinomycin D prevented the stimulation‐induced elevation of the enzyme. These findings strongly suggest that this stimulation was achieved by the accelerated biosynthesis of tryptophan hydroxylase.

Tryptophan hydroxylase

Calcium in biology

10.1016/0014-5793(96)00834-4

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Comparison of Human Erythrocyte Filterability with Trapping Rate Obtained by Nickel Mesh Filtration Technique: Two Independent Parameters of Erythrocyte Deformability

International Blood Research & Reviews (2018)

Takeshi Arita Mitsuhiro Fukata Toru Maruyama Keita Odashiro Takehiko Fujino

Filtration (mathematics)

Erythrocyte deformability

10.9734/ibrr/2018/44667

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Roles of Multiple Flagellins in Flagellar Formation and Flagellar Growth Post Bdelloplast Lysis in Bdellovibrio bacteriovorus

Journal of Molecular Biology (2009)

Yoshiko Iida Laura Hobley Carey Lambert Andrew K. Fenton R. Elizabeth Sockett

Bdellovibrio bacteriovorus cells have a single polar flagellum whose helical pitch and diameter characteristically change near the midpoint, resulting in a tapered wave. There are six flagellin genes in the genome: fliC1 to fliC6. Accordingly, the flagellar filament is composed of several similar flagellin species. We have used knockout mutants of each gene and analyzed the mutational effects on the filament length and on the composition and localization of each flagellin species in the filament by electron microscopy and one- and two-dimensional polyacrylamide gel electrophoresis. The location and amounts of flagellins in a filament were determined to be as follows: a small amount of FliC3 at the proximal end, followed by a large amount of FliC5, a large amount of FliC1, a small amount of FliC2 in this order, and a large amount of FliC6 at the distal end. FliC4 was present at a low level, but the location was not determined. Filament lengths of newly born progeny cells increased during prolonged incubation in nutrient-deficient buffer. The newly formed part of the elongated filament was composed of mainly FliC6. Reverse transcription PCR analysis of flagellar gene expression over 5 days in buffer showed that fliC gene expression tailed off over 5 days in the wild-type cells, but in the fliC5 mutant, expression of the fliC2, fliC4, and fliC6 genes was elevated on day 5, suggesting that they may be expressed to compensate for the absence of a major component, FliC5.

Flagellin

Lysis buffer

10.1016/j.jmb.2009.10.003

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Citations (36)