Shin-ichi Yokota, Yuzo Yamamoto, Kenji Shimizu, Hirohito Momoi, Tatsuhiko Kamikawa, Yoshio Yamaoka, ...
Shin-ichi Yokota, Daisuke Hirata, Seiji Minota, Takanobu Higashiyama, Masashi Kurimoto, Hideki Yanagi, ...
Kaneda, Sumiko, Yura, Takashi, Yanagi, Hideki
150 kDa oxygen-regulated protein (ORP150) is one of the endoplasmic reticulum (ER)-resident stress proteins we have cloned and sequenced the entire human ORP150 gene covering over 15-kb. Analyses of...
Morita, Miyo Terao, Tanaka, Yoshiyuki, Kodama, Takashi S., Kyogoku, Yoshimasa, Yanagi, Hideki, Yura, Takashi
Fujita, Nobuyuki, Mori, Hirotada, Yura, Takashi, Ishihama, Akira
The complete sequence analysis of the E.coli genome was initiated as a collaborative study in Japan. Following the initial analysis of the 0–2.4 min region (Yura, T. et al. (1992) Nucleic Acids...
算数文章題の理解と解決に及ぼす要因について : 文章の記憶再認課題による検討 (1993)
岸, 学, 由良, 隆, キシ, マナブ, ユラ, タカ, Kishi, Manabu, Yura, Takashi, ...
Yuzawa, Harumi, Nagai, Hiroki, Mori, Hirotada, Yura, Takashi
Induction of heat shock proteins following transfer of E.coli cells from 30°C to 42°C depends on rapid accumulation of θ32, a minor θ factor specifically required for transcription of heat shock...
Systematic sequencing of the Escherichia coli genome: analysis of the 0 - 2.4 min region (1992)
Yura, Takashi, Mori, Hirotada, Nagai, Hiroki, Nagata, Toshio, Ishihama, Akira, Fujita, Nobuyuki, ...
A contiguous 111,402-nucleotide sequence corresponding to the 0 to 2.4 min region of the E.coli chromosome was determined as a first step to complete structural analysis of the genome. The resulting...
ISHIHAMA, Akira, IKEUCHI, Toshihiko, YURA, Takashi
Adenosinetriphosphatase (ATPase) [EC 3.6.1.3] activity has been found to exist in most preparations of DNA-dependent RNA polymerase [EC 2.7.7.6] obtained from Escherichia coli by a number of...
Mori, Kazutoshi, Ogawa, Naoki, Kawahara, Tetsushi, Yanagi, Hideki, Yura, Takashi
Eukaryotic cells control the levels of molecular chaperones and folding enzymes in the endoplasmic reticulum (ER) by a transcriptional induction process termed the unfolded protein response (UPR)...
Dynamic interplay between antagonistic pathways controlling the σ32 level in Escherichia coli
Morita, Miyo T., Kanemori, Masaaki, Yanagi, Hideki, Yura, Takashi
The heat-shock response in Escherichia coli depends primarily on the transient increase in the cellular level of heat-shock sigma factor σ32 encoded by the rpoH gene, which results from both...
Kawahara, Tetsushi, Yanagi, Hideki, Yura, Takashi, Mori, Kazutoshi
An intracellular signaling from the endoplasmic reticulum (ER) to the nucleus, called the unfolded protein response (UPR), is activated when unfolded proteins are accumulated in the ER under a...
Haze, Kyosuke, Yoshida, Hiderou, Yanagi, Hideki, Yura, Takashi, Mori, Kazutoshi
The unfolded protein response (UPR) controls the levels of molecular chaperones and enzymes involved in protein folding in the endoplasmic reticulum (ER). We recently isolated ATF6 as a candidate for...
Yoshida, Hiderou, Okada, Tetsuya, Haze, Kyosuke, Yanagi, Hideki, Yura, Takashi, Negishi, Manabu, ...
Transcription of genes encoding molecular chaperones and folding enzymes in the endoplasmic reticulum (ER) is induced by accumulation of unfolded proteins in the ER. This intracellular signaling,...
Overexpression of Trigger Factor Prevents Aggregation of Recombinant Proteins in Escherichia coli
Nishihara, Kazuyo, Kanemori, Masaaki, Yanagi, Hideki, Yura, Takashi
To examine the effects of overexpression of trigger factor (TF) on recombinant proteins produced in Escherichia coli, we constructed plasmids that permitted controlled expression of TF alone or...
Kurokawa, Yoichi, Yanagi, Hideki, Yura, Takashi
Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. By using a set of Dsb coexpression plasmids constructed...
Morita, Miyo, Kanemori, Masaaki, Yanagi, Hideki, Yura, Takashi
The heat shock response in Escherichia coli depends primarily on the increased synthesis and stabilization of otherwise scarce and unstable ς32 (rpoH gene product), which is required for the...
Kanemori, Masaaki, Yanagi, Hideki, Yura, Takashi
Escherichia coli mutants lacking activities of all known cytosolic ATP-dependent proteases (Lon, ClpAP, ClpXP, and HslVU), due to double deletions [ΔhslVU and Δ(clpPX-lon)], cannot grow at low...
Nakahigashi, Kenji, Ron, Eliora Z., Yanagi, Hideki, Yura, Takashi
The heat shock response in alpha proteobacteria is unique in that a combination of two regulators is involved: a positive regulator, RpoH (ς32 homolog), found in the alpha, beta, and gamma...
Nakahigashi, Kenji, Yanagi, Hideki, Yura, Takashi
RpoH (Escherichia coli ς32 and its homologs) is the central regulator of the heat shock response in gram-negative proteobacteria. Here we studied salient regulatory features of RpoH in Agrobacterium...
Yoshida, Hiderou, Okada, Tetsuya, Haze, Kyosuke, Yanagi, Hideki, Yura, Takashi, Negishi, Manabu, ...
The levels of molecular chaperones and folding enzymes in the endoplasmic reticulum (ER) are controlled by a transcriptional induction process termed the unfolded protein response (UPR). The...
Nishihara, Kazuyo, Kanemori, Masaaki, Kitagawa, Masanari, Yanagi, Hideki, Yura, Takashi
Plasmids that can be used for controlled expression of the DnaK-DnaJ-GrpE and/or GroEL-GroES chaperone team were constructed in order to facilitate assessment of the effects of these chaperone teams...
Nakahigashi, Kenji, Yanagi, Hideki, Yura, Takashi
The heat shock response in Escherichia coli is mediated primarily by the rpoH gene, encoding ς32, which is specifically required for transcription of heat shock genes. A number of ς32 homologs have...
Heat Shock Proteome of Agrobacterium tumefaciens: Evidence for New Control Systems
Rosen, Ran, Büttner, Knut, Becher, Dörte, Nakahigashi, Kenji, Yura, Takashi, Hecker, Michael, ...
The regulation of Agrobacterium tumefaciens heat shock genes involves a transcriptional activator (RpoH) and repressor elements (HrcA-CIRCE). Using proteome analysis and mutants in these control...
Temperature-sensitive Repression of the Tryptophan Operon in Escherichia coli
Ito, Koreaki, Hiraga, Sota, Yura, Takashi
Mutants of Escherichia coli exhibiting temperature-sensitive repression of the tryptophan operon have been isolated among the revertants of a tryptophan auxotroph, trpS5, that produces an altered...
Morita, Miyo Terao, Tanaka, Yoshiyuki, Kodama, Takashi S., Kyogoku, Yoshimasa, Yanagi, Hideki, Yura, Takashi
Induction of heat shock proteins in Escherichia coli is primarily caused by increased cellular levels of the heat shock σ-factor σ32 encoded by the rpoH gene. Increased σ32 levels result from both...
Increased expression of cytosolic chaperonin CCT in human hepatocellular and colonic carcinoma
Yokota, Shin-ichi, Yamamoto, Yuzo, Shimizu, Kenji, Momoi, Hirohito, Kamikawa, Tatsuhiko, Yamaoka, Yoshio, ...
The chaperonin-containing t-complex polypeptide 1 (CCT) is a hetero-oligomeric molecular chaperone that assists in the folding of actin, tubulin, and other cytosolic proteins. We recently reported...
Horikoshi, Mina, Yura, Takashi, Tsuchimoto, Sachie, Fukumori, Yoshihiro, Kanemori, Masaaki
Escherichia coli heat shock transcription factor σ32 is rapidly degraded in vivo, with a half-life of about 1 min. A set of proteins that includes the DnaK chaperone team (DnaK, DnaJ, GrpE) and...
Yokota, Shin-ichi, Hirata, Daisuke, Minota, Seiji, Higashiyama, Takanobu, Kurimoto, Masashi, Yanagi, Hideki, ...
Chaperonin CCT containing t-complex polypeptide 1 is a cytosolic molecular chaperone that assists in the folding of actin, tubulin, and other proteins and is a member of the 60-kDa heat shock protein...
A temperature-sensitive DNA replication mutant of E. coli K-12 was isolated among the mutants selected for phenethyl alcohol resistance at low temperatures. This mutation, designated as dnaP18,...
Mori, Kazutoshi, Ogawa, Naoki, Kawahara, Tetsushi, Yanagi, Hideki, Yura, Takashi
Eukaryotic cells control the levels of molecular chaperones and folding enzymes in the endoplasmic reticulum (ER) by a transcriptional induction process termed the unfolded protein response (UPR)...
Dynamic interplay between antagonistic pathways controlling the σ32 level in Escherichia coli
Morita, Miyo T., Kanemori, Masaaki, Yanagi, Hideki, Yura, Takashi
The heat-shock response in Escherichia coli depends primarily on the transient increase in the cellular level of heat-shock sigma factor σ32 encoded by the rpoH gene, which results from both...
Kawahara, Tetsushi, Yanagi, Hideki, Yura, Takashi, Mori, Kazutoshi
An intracellular signaling from the endoplasmic reticulum (ER) to the nucleus, called the unfolded protein response (UPR), is activated when unfolded proteins are accumulated in the ER under a...
Haze, Kyosuke, Yoshida, Hiderou, Yanagi, Hideki, Yura, Takashi, Mori, Kazutoshi
The unfolded protein response (UPR) controls the levels of molecular chaperones and enzymes involved in protein folding in the endoplasmic reticulum (ER). We recently isolated ATF6 as a candidate for...
Yoshida, Hiderou, Okada, Tetsuya, Haze, Kyosuke, Yanagi, Hideki, Yura, Takashi, Negishi, Manabu, ...
Transcription of genes encoding molecular chaperones and folding enzymes in the endoplasmic reticulum (ER) is induced by accumulation of unfolded proteins in the ER. This intracellular signaling,...
Overexpression of Trigger Factor Prevents Aggregation of Recombinant Proteins in Escherichia coli
Nishihara, Kazuyo, Kanemori, Masaaki, Yanagi, Hideki, Yura, Takashi
To examine the effects of overexpression of trigger factor (TF) on recombinant proteins produced in Escherichia coli, we constructed plasmids that permitted controlled expression of TF alone or...
Kurokawa, Yoichi, Yanagi, Hideki, Yura, Takashi
Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. By using a set of Dsb coexpression plasmids constructed...
Morita, Miyo, Kanemori, Masaaki, Yanagi, Hideki, Yura, Takashi
The heat shock response in Escherichia coli depends primarily on the increased synthesis and stabilization of otherwise scarce and unstable ς32 (rpoH gene product), which is required for the...
Kanemori, Masaaki, Yanagi, Hideki, Yura, Takashi
Escherichia coli mutants lacking activities of all known cytosolic ATP-dependent proteases (Lon, ClpAP, ClpXP, and HslVU), due to double deletions [ΔhslVU and Δ(clpPX-lon)], cannot grow at low...
Nakahigashi, Kenji, Ron, Eliora Z., Yanagi, Hideki, Yura, Takashi
The heat shock response in alpha proteobacteria is unique in that a combination of two regulators is involved: a positive regulator, RpoH (ς32 homolog), found in the alpha, beta, and gamma...
Nakahigashi, Kenji, Yanagi, Hideki, Yura, Takashi
RpoH (Escherichia coli ς32 and its homologs) is the central regulator of the heat shock response in gram-negative proteobacteria. Here we studied salient regulatory features of RpoH in Agrobacterium...
Yoshida, Hiderou, Okada, Tetsuya, Haze, Kyosuke, Yanagi, Hideki, Yura, Takashi, Negishi, Manabu, ...
The levels of molecular chaperones and folding enzymes in the endoplasmic reticulum (ER) are controlled by a transcriptional induction process termed the unfolded protein response (UPR). The...
Nishihara, Kazuyo, Kanemori, Masaaki, Kitagawa, Masanari, Yanagi, Hideki, Yura, Takashi
Plasmids that can be used for controlled expression of the DnaK-DnaJ-GrpE and/or GroEL-GroES chaperone team were constructed in order to facilitate assessment of the effects of these chaperone teams...
Nakahigashi, Kenji, Yanagi, Hideki, Yura, Takashi
The heat shock response in Escherichia coli is mediated primarily by the rpoH gene, encoding ς32, which is specifically required for transcription of heat shock genes. A number of ς32 homologs have...
Heat Shock Proteome of Agrobacterium tumefaciens: Evidence for New Control Systems
Rosen, Ran, Büttner, Knut, Becher, Dörte, Nakahigashi, Kenji, Yura, Takashi, Hecker, Michael, ...
The regulation of Agrobacterium tumefaciens heat shock genes involves a transcriptional activator (RpoH) and repressor elements (HrcA-CIRCE). Using proteome analysis and mutants in these control...
Temperature-sensitive Repression of the Tryptophan Operon in Escherichia coli
Ito, Koreaki, Hiraga, Sota, Yura, Takashi
Mutants of Escherichia coli exhibiting temperature-sensitive repression of the tryptophan operon have been isolated among the revertants of a tryptophan auxotroph, trpS5, that produces an altered...
Yokota, Shin-ichi, Hirata, Daisuke, Minota, Seiji, Higashiyama, Takanobu, Kurimoto, Masashi, Yanagi, Hideki, ...
Chaperonin CCT containing t-complex polypeptide 1 is a cytosolic molecular chaperone that assists in the folding of actin, tubulin, and other proteins and is a member of the 60-kDa heat shock protein...
Morita, Miyo Terao, Tanaka, Yoshiyuki, Kodama, Takashi S., Kyogoku, Yoshimasa, Yanagi, Hideki, Yura, Takashi
Induction of heat shock proteins in Escherichia coli is primarily caused by increased cellular levels of the heat shock σ-factor σ32 encoded by the rpoH gene. Increased σ32 levels result from both...
Increased expression of cytosolic chaperonin CCT in human hepatocellular and colonic carcinoma
Yokota, Shin-ichi, Yamamoto, Yuzo, Shimizu, Kenji, Momoi, Hirohito, Kamikawa, Tatsuhiko, Yamaoka, Yoshio, ...
The chaperonin-containing t-complex polypeptide 1 (CCT) is a hetero-oligomeric molecular chaperone that assists in the folding of actin, tubulin, and other cytosolic proteins. We recently reported...
Horikoshi, Mina, Yura, Takashi, Tsuchimoto, Sachie, Fukumori, Yoshihiro, Kanemori, Masaaki
Escherichia coli heat shock transcription factor σ32 is rapidly degraded in vivo, with a half-life of about 1 min. A set of proteins that includes the DnaK chaperone team (DnaK, DnaJ, GrpE) and...
A temperature-sensitive DNA replication mutant of E. coli K-12 was isolated among the mutants selected for phenethyl alcohol resistance at low temperatures. This mutation, designated as dnaP18,...
Yura, Takashi, Guisbert, Eric, Poritz, Mark, Lu, Chi Zen, Campbell, Elizabeth, Gross, Carol A.
Protein quality control is accomplished by inducing chaperones and proteases in response to an altered cellular folding state. In Escherichia coli, expression of chaperones and proteases is...
Guisbert, Eric, Yura, Takashi, Rhodius, Virgil A., Gross, Carol A.
Summary: The heat shock response (HSR) is a homeostatic response that maintains the proper protein-folding environment in the cell. This response is universal, and many of its components are well...