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Article: Moonlighting functions of polypeptide elongation factor 1: from actin bundling to zinc finger protein R1-associated nuclear localization.

Ejiri, Shin-ichiro

Bioscience, biotechnology, and biochemistry

2002 Volume 66, Issue 1, Page(s) 1–21

Abstract: Eukaryotic polypeptide elongation factor EF-1 is not only a major translational factor, but also one of the most important multifunctional (moonlighting) proteins. EF-1 consists of four different subunits collectively termed EF-1alphabeta beta'gamma and ... ...

Abstract	Eukaryotic polypeptide elongation factor EF-1 is not only a major translational factor, but also one of the most important multifunctional (moonlighting) proteins. EF-1 consists of four different subunits collectively termed EF-1alphabeta beta'gamma and EF-1alphabeta gammadelta in plants and animals, respectively. EF-1alpha x GTP catalyzes the binding of aminoacyl-tRNA to the A-site of the ribosome. EF-1beta beta'gamma (EF-1beta and EF-1beta'), catalyzes GDP/GTP exchange on EF-1alpha x GDP to regenerate EF-1alpha x GTP. EF-1gamma has recently been shown to have glutathione S-transferase activity. EF-2 catalyzes the translocation of peptidyl-tRNA from the A-site to the P-site on the ribosome. Recently, molecular mimicry among tRNA, elongation factors, releasing factor (RF), and ribosome recycling factor (RRF) has been demonstrated and greatly improved our understanding of the mechanism of translation. Moreover, eukaryotic elongation factors have been shown to be concerned or likely to be concerned in various important cellular processes or serious diseases, including translational control, signal transduction, cytoskeletal organization, apoptosis, adult atopic dermatitis, oncogenic transformation, nutrition, and nuclear processes such as RNA synthesis and mitosis. This article aims to overview the recent advances in protein biosynthesis, concentrating on the moonlighting functions of EF-1.
MeSH term(s)	Actins/metabolism ; Animals ; Apoptosis ; Carrier Proteins/metabolism ; Cell Nucleus/metabolism ; Cold Temperature ; Cysteine Endopeptidases ; Cytoskeleton ; HIV-1 ; Herpesvirus 1, Human ; Humans ; Molecular Mimicry ; Multienzyme Complexes ; Peptide Elongation Factor 1/genetics ; Peptide Elongation Factor 1/metabolism ; Peptide Elongation Factor 1/physiology ; Peptides ; Proteasome Endopeptidase Complex ; Protein Biosynthesis ; Protein Disulfide-Isomerases/metabolism ; Selenocysteine/metabolism ; Signal Transduction ; West Nile virus ; Zinc Fingers
Chemical Substances	Actins ; Carrier Proteins ; Multienzyme Complexes ; Peptide Elongation Factor 1 ; Peptides ; ZPR1 protein, human ; Selenocysteine (0CH9049VIS) ; Cysteine Endopeptidases (EC 3.4.22.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Protein Disulfide-Isomerases (EC 5.3.4.1)
Language	English
Publishing date	2002-02-04
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1271/bbb.66.1
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Article: Moonlighting Functions of Polypeptide Elongation Factor 1: From Actin Bundling to Zinc Finger Protein R1-Associated Nuclear Localization

EJIRI, Shin-ichiro

Bioscience, biotechnology, and biochemistry. 2002 Jan. 1, v. 66, no. 1

2002

Abstract	Eukaryotic polypeptide elongation factor EF-1 is not only a major translational factor, but also one of the most important multifunctional (moonlighting) proteins. EF-1 consists of four different subunits collectively termed EF-1αββ′γ and EF-1αβγδ in plants and animals, respectively. EF-1α•GTP catalyzes the binding of aminoacyl-tRNA to the A-site of the ribosome. EF-1ββ′γ (EF-1β and EF-1β′), catalyzes GDP/GTP exchange on EF-1α•GDP to regenerate EF-1α•GTP. EF-1γ has recently been shown to have glutathione S-transferase activity. EF-2 catalyzes the translocation of peptidyl-tRNA from the A-site to the P-site on the ribosome. Recently, molecular mimicry among tRNA, elongation factors, releasing factor (RF), and ribosome recycling factor (RRF) has been demonstrated and greatly improved our understanding of the mechanism of translation. Moreover, eukaryotic elongation factors have been shown to be concerned or likely to be concerned in various important cellular processes or serious diseases, including translational control, signal transduction, cytoskeletal organization, apoptosis, adult atopic dermatitis, oncogenic transformation, nutrition, and nuclear processes such as RNA synthesis and mitosis. This article aims to overview the recent advances in protein biosynthesis, concentrating on the moonlighting functions of EF-1.
Keywords	actin ; adults ; apoptosis ; atopic dermatitis ; biotechnology ; cytoskeleton ; glutathione transferase ; mitosis ; molecular mimicry ; nutrition ; peptide elongation factors ; polypeptides ; protein synthesis ; ribosomes ; signal transduction ; zinc finger motif
Language	English
Dates of publication	2002-0101
Size	p. 1-21.
Publishing place	Japan Society for Bioscience, Biotechnology, and Agrochemistry
Document type	Article
Note	NAL-light
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1271/bbb.66.1
Database	NAL-Catalogue (AGRICOLA)

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Article: Localization of actin filaments on mitotic apparatus in tobacco BY-2 cells.

Yasuda, Hiroshi / Kanda, Katsuhiro / Koiwa, Hiroyuki / Suenaga, Kayoko / Kidou, Shin-Ichiro / Ejiri, Shin-Ichiro

Planta

2005 Volume 222, Issue 1, Page(s) 118–129

Abstract: Actin filaments are among the major components of the cytoskeleton, and participate in various cellular dynamic processes. However, conflicting results had been obtained on the localization of actin filaments on the mitotic apparatus and their ... ...

Abstract	Actin filaments are among the major components of the cytoskeleton, and participate in various cellular dynamic processes. However, conflicting results had been obtained on the localization of actin filaments on the mitotic apparatus and their participation in the process of chromosome segregation. We demonstrated by using rhodamine-phalloidin staining, the localization of actin filaments on the mitotic spindles of tobacco BY-2 cells when the cells were treated with cytochalasin D. At prophase, several clear spots were observed at or near the kinetochores of the chromosomes. At anaphase, the actin filaments that appeared to be pulling chromosomes toward the division poles were demonstrated. However, as there was a slight possibility that these results might have been the artifacts of cytochalasin D treatment or the phalloidin staining, we analyzed the localization of actin filaments at the mitotic apparatus immunologically. We cloned a novel BY-2 alpha-type actin cDNA and prepared a BY-2 actin antibody. The fluorescence of the anti-BY-2 actin antibody was clearly observed at the mitotic apparatus in both non-treated and cytochalasin D-treated BY-2 cells during mitosis. The facts that similar results were obtained in both actin staining with rhodamine-phalloidin and immunostaining with actin antibody strongly indicate the participation of actin in the organization of the spindle body or in the process of chromosome segregation. Furthermore, both filamentous actin and spindle bodies disappeared in the cells treated with propyzamide, which depolymerizes microtubules, supporting the notion that actin filaments are associated with microtubules organizing the spindle body.
MeSH term(s)	Actin Cytoskeleton/chemistry ; Actin Cytoskeleton/drug effects ; Actin Cytoskeleton/metabolism ; Actins/chemistry ; Actins/genetics ; Actins/immunology ; Actins/metabolism ; Amino Acid Sequence ; Animals ; Benzamides/pharmacology ; Cells, Cultured ; Cytochalasin D/pharmacology ; Humans ; Mitosis ; Molecular Sequence Data ; Phylogeny ; Sequence Homology, Amino Acid ; Spindle Apparatus/drug effects ; Spindle Apparatus/metabolism ; Nicotiana/cytology
Chemical Substances	Actins ; Benzamides ; Cytochalasin D (22144-77-0) ; pronamide (2EZ95375S0)
Language	English
Publishing date	2005-04-27
Publishing country	Germany
Document type	Journal Article
ZDB-ID	208909-9
ISSN	1432-2048 ; 0032-0935 ; 1866-2749
ISSN (online)	1432-2048
ISSN	0032-0935 ; 1866-2749
DOI	10.1007/s00425-005-1522-8
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Localization of actin filaments on mitotic apparatus in tobacco BY-2 cells

Yasuda, Hiroshi / Kanda, Katsuhiro / Koiwa, Hiroyuki / Suenaga, Kayoko / Kidou, Shin-ichiro / Ejiri, Shin-ichiro

Planta. 2005 Sept., v. 222, no. 1

2005

Abstract	Actin filaments are among the major components of the cytoskeleton, and participate in various cellular dynamic processes. However, conflicting results had been obtained on the localization of actin filaments on the mitotic apparatus and their participation in the process of chromosome segregation. We demonstrated by using rhodamine-phalloidin staining, the localization of actin filaments on the mitotic spindles of tobacco BY-2 cells when the cells were treated with cytochalasin D. At prophase, several clear spots were observed at or near the kinetochores of the chromosomes. At anaphase, the actin filaments that appeared to be pulling chromosomes toward the division poles were demonstrated. However, as there was a slight possibility that these results might have been the artifacts of cytochalasin D treatment or the phalloidin staining, we analyzed the localization of actin filaments at the mitotic apparatus immunologically. We cloned a novel BY-2 α-type actin cDNA and prepared a BY-2 actin antibody. The fluorescence of the anti-BY-2 actin antibody was clearly observed at the mitotic apparatus in both non-treated and cytochalasin D-treated BY-2 cells during mitosis. The facts that similar results were obtained in both actin staining with rhodamine-phalloidin and immunostaining with actin antibody strongly indicate the participation of actin in the organization of the spindle body or in the process of chromosome segregation. Furthermore, both filamentous actin and spindle bodies disappeared in the cells treated with propyzamide, which depolymerizes microtubules, supporting the notion that actin filaments are associated with microtubules organizing the spindle body.
Keywords	actin ; anaphase ; antibodies ; chromosome segregation ; complementary DNA ; cytochalasin D ; fluorescence ; kinetochores ; microfilaments ; microtubules ; mitosis ; poles ; prophase ; propyzamide ; tobacco
Language	English
Dates of publication	2005-09
Size	p. 118-129.
Publishing place	Springer-Verlag
Document type	Article
ZDB-ID	208909-9
ISSN	1432-2048 ; 0032-0935
ISSN (online)	1432-2048
ISSN	0032-0935
DOI	10.1007/s00425-005-1522-8
Database	NAL-Catalogue (AGRICOLA)

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Article: Interaction between elongation factors 1beta and 1gamma from Bombyx mori silk gland.

Kamiie, Katsuyoshi / Yamashita, Tetsuro / Taira, Hideharu / Kidou, Shin-ichiro / Ejiri, Shin-ichiro

Bioscience, biotechnology, and biochemistry

2003 Volume 67, Issue 7, Page(s) 1522–1529

Abstract: Elongation factor 1 (EF-1) from the silk gland of Bombyx mori consists of four subunits: alpha (51 kDa), beta (26 kDa), gamma (49 kDa), and delta (33 kDa). The EF-1alpha subunit catalyzes the binding of aminoacyl-tRNA to the ribosome concomitant with the ...

Abstract	Elongation factor 1 (EF-1) from the silk gland of Bombyx mori consists of four subunits: alpha (51 kDa), beta (26 kDa), gamma (49 kDa), and delta (33 kDa). The EF-1alpha subunit catalyzes the binding of aminoacyl-tRNA to the ribosome concomitant with the hydrolysis of GTP. The EF-1alpha-bound GDP is then exchanged for GTP by the EF-1betagammadelta complex. To facilitate analysis of the roles of the individual EF-1beta, gamma, and delta subunits in GDP/GTP exchange on EF-1alpha, we cloned the cDNAs for these subunits and expressed them in Escherichia coli. EF-1beta, EF-1gamma, and the carboxyl-terminal half of EF-1delta were expressed, purified, and examined for protein:protein interactions by gel filtration chromatography and by a quartz-crystal microbalance method. An 80-kDa species containing EF-1beta and gamma subunits in a 1:1 molar ratio was detected by gel filtration. A higher molecular weight species containing an excess of EF-1gamma relative to EF-1beta was also detected. The amino-terminal region of EF-1beta (amino acid residues 1-129) was sufficient for binding to EF-1gamma. The carboxyl-terminal half of EF-1delta did not appear to form a complex with EF-1gamma.
MeSH term(s)	Amino Acid Sequence ; Animals ; Bombyx/chemistry ; Chromatography, Gel ; Conserved Sequence ; Insect Proteins/secretion ; Molecular Sequence Data ; Peptide Elongation Factor 1/chemistry ; Peptide Elongation Factor 1/genetics ; Peptide Elongation Factor 1/metabolism ; Protein Binding ; Protein Subunits/chemistry ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Silk ; Species Specificity ; Weights and Measures
Chemical Substances	Insect Proteins ; Peptide Elongation Factor 1 ; Protein Subunits ; Recombinant Proteins ; Silk
Language	English
Publishing date	2003-07
Publishing country	England
Document type	Journal Article
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1271/bbb.67.1522
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Article: Interaction between Elongation Factors 1β and 1γ from Bombyx mori Silk Gland

KAMIIE, Katsuyoshi / YAMASHITA, Tetsuro / TAIRA, Hideharu / KIDOU, Shin-ichiro / EJIRI, Shin-ichiro

Bioscience, biotechnology, and biochemistry. 2003 Jan. 1, v. 67, no. 7

2003

Abstract: Elongation factor 1 (EF-1) from the silk gland of Bombyx mori consists of four subunits: α (51 kDa), β (26 kDa), γ (49 kDa), and δ (33 kDa). The EF-1α subunit catalyzes the binding of aminoacyl-tRNA to the ribosome concomitant with the hydrolysis of GTP. ...

Abstract	Elongation factor 1 (EF-1) from the silk gland of Bombyx mori consists of four subunits: α (51 kDa), β (26 kDa), γ (49 kDa), and δ (33 kDa). The EF-1α subunit catalyzes the binding of aminoacyl-tRNA to the ribosome concomitant with the hydrolysis of GTP. The EF-1α-bound GDP is then exchanged for GTP by the EF-1βγδ complex. To facilitate analysis of the roles of the individual EF-1β, γ, and δ subunits in GDP/GTP exchange on EF-1α, we cloned the cDNAs for these subunits and expressed them in Escherichia coli. EF-1β, EF-1γ, and the carboxyl-terminal half of EF-1δ were expressed, purified, and examined for protein:protein interactions by gel filtration chromatography and by a quartz-crystal microbalance method. An 80-kDa species containing EF-1β and γ subunits in a 1:1 molar ratio was detected by gel filtration. A higher molecular weight species containing an excess of EF-1γ relative to EF-1β was also detected. The amino-terminal region of EF-1β (amino acid residues 1-129) was sufficient for binding to EF-1γ. The carboxyl-terminal half of EF-1δ did not appear to form a complex with EF-1γ.
Keywords	Bombyx mori ; Escherichia coli ; biotechnology ; gel chromatography ; hydrolysis ; molecular weight ; peptide elongation factors ; quartz crystal microbalance ; ribosomes ; silk glands
Language	English
Dates of publication	2003-0101
Size	p. 1522-1529.
Publishing place	Japan Society for Bioscience, Biotechnology, and Agrochemistry
Document type	Article
Note	NAL-light
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1271/bbb.67.1522
Database	NAL-Catalogue (AGRICOLA)

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Article: Expression of Elongation Factor 1β′ in Escherichia coli and Its Interaction with Elongation Factor 1α from Silk Gland

KAMIIE, Katsuyoshi / TAIRA, Hideharu / KOBAYASHI, Kohmei / YAMASHITA, Tetsuro / KIDOU, Shin-ichiro / EJIRI, Shin-ichiro

Bioscience, biotechnology, and biochemistry. 1999 Jan. 1, v. 63, no. 4

1999

Abstract: Silk gland elongation factor 1 (EF-1) consists of four subunits: α, β, β′, and γ. EF-1ββ′γ catalyzes the exchange of GDP for GTP on EF-1α and stimulates the binding of EF-1α-dependent aminoacyl-tRNA to ribosomes. The carboxy-terminal regions of the EF-1β ...

Abstract	Silk gland elongation factor 1 (EF-1) consists of four subunits: α, β, β′, and γ. EF-1ββ′γ catalyzes the exchange of GDP for GTP on EF-1α and stimulates the binding of EF-1α-dependent aminoacyl-tRNA to ribosomes. The carboxy-terminal regions of the EF-1β subunits from various species are highly conserved. We examined the region of EF-1β′ that binds to EF-1α by in vitro binding assays, and examined the GDP/GTP exchange activity using deletion mutants of a GST-EF1β′ fusion protein. We thereby suggested a pivotal amino acid region, residues 189-222, of EF-1β′ for binding to EF-1α.
Keywords	Escherichia coli ; biotechnology ; peptide elongation factors ; ribosomes ; silk glands
Language	English
Dates of publication	1999-0101
Size	p. 666-671.
Publishing place	Japan Society for Bioscience, Biotechnology, and Agrochemistry
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1271/bbb.63.666
Database	NAL-Catalogue (AGRICOLA)

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Article: Cloning and expression of Bombyx mori silk gland elongation factor 1gamma in Escherichia coli.

Kamiie, Katsuyoshi / Nomura, Yoshitaka / Kobayashi, Satoru / Taira, Hideharu / Kobayashi, Kohmei / Yamashita, Tetsuro / Kidou, Shin-ichiro / Ejiri, Shin-ichiro

Bioscience, biotechnology, and biochemistry

2002 Volume 66, Issue 3, Page(s) 558–565

Abstract: Elongation factor 1 (EF-1) from the silk gland of Bombyx mori consists of alpha-, beta-, gamma-, and delta-subunits. EF-1alpha GTP catalyzes the binding of aminoacyl-tRNA to ribosomes concomitant with the hydrolysis of GTP. EF-1betagammadelta catalyzes ... ...

Abstract	Elongation factor 1 (EF-1) from the silk gland of Bombyx mori consists of alpha-, beta-, gamma-, and delta-subunits. EF-1alpha GTP catalyzes the binding of aminoacyl-tRNA to ribosomes concomitant with the hydrolysis of GTP. EF-1betagammadelta catalyzes the exchange of EF-1alpha-bound GDP for exogenous GTP and stimulates the EF-1alpha-dependent binding of aminoacyl-tRNA to ribosomes. EF-1gamma cDNA, which contains an open reading frame (ORF) encoding a polypeptide of 423 amino acid residues, was amplified and cloned by PCR from a silk gland cDNA library. The calculated molecular mass and predicted pI of the product were 48,388 Da and 5.84, respectively. The silk gland EF-1gamma shares 67.3% amino acid identity with Artemia salina EF-lgamma. The N-terminal domain (amino acid residues 1-211) of silk gland EF-lgamma is 29.3% identical to maize glutathione S-transferase. We demonstrated that silk gland EF-lgamma bound to glutathione Sepharose, suggesting that the N-terminal domain of EF-1gamma may have the capacity to bind to glutathione.
MeSH term(s)	Amino Acid Sequence ; Animals ; Base Sequence ; Bombyx/metabolism ; Chromatography, Ion Exchange ; Cloning, Molecular ; Conserved Sequence ; DNA, Complementary/biosynthesis ; DNA, Complementary/genetics ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/metabolism ; Exocrine Glands/metabolism ; Glutathione/chemistry ; Glutathione Transferase/genetics ; Glutathione Transferase/metabolism ; Molecular Sequence Data ; Peptide Elongation Factor 1/biosynthesis ; Peptide Elongation Factor 1/genetics ; Reverse Transcriptase Polymerase Chain Reaction
Chemical Substances	DNA, Complementary ; Peptide Elongation Factor 1 ; Glutathione Transferase (EC 2.5.1.18) ; Glutathione (GAN16C9B8O)
Language	English
Publishing date	2002-03
Publishing country	England
Document type	Journal Article
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1271/bbb.66.558
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Eukaryotic translation elongation factor 1A induces anoikis by triggering cell detachment.

Itagaki, Keisuke / Naito, Toshihiko / Iwakiri, Ryota / Haga, Makoto / Miura, Shougo / Saito, Yohei / Owaki, Toshiyuki / Kamiya, Sadahiro / Iyoda, Takuya / Yajima, Hirofumi / Iwashita, Shintaro / Ejiri, Shin-ichiro / Fukai, Fumio

The Journal of biological chemistry

2012 Volume 287, Issue 19, Page(s) 16037–16046

Abstract: Anoikis, apoptosis because of loss of cell anchorage, is crucial for tissue homeostasis. Fibronectin not only provides a scaffold for cell anchorage but also harbors a cryptic antiadhesive site capable of inducing β1-integrin inactivation. In this study, ...

Abstract	Anoikis, apoptosis because of loss of cell anchorage, is crucial for tissue homeostasis. Fibronectin not only provides a scaffold for cell anchorage but also harbors a cryptic antiadhesive site capable of inducing β1-integrin inactivation. In this study, this cryptic antiadhesive site is implicated in spontaneous induction of anoikis. Nontransformed fibroblasts (NIH3T3) adhering to a fibronectin substratum underwent anoikis during serum starvation culture. This anoikis was caused by proteolytic exposure of the cryptic antiadhesive site in fibronectin by matrix metalloproteinase. Eukaryotic elongation factor 1A (eEF1A) was identified as a membrane receptor for the exposed antiadhesive site. Serum starvation raised the membrane residence of eEF1A, and siRNA-based disruption of this increase rendered cells anoikis-resistant. By contrast, cells became more susceptible to anoikis in parallel with increased membrane residence of eEF1A by enforced expression. These results demonstrate that eEF1A acts as a membrane receptor for the cryptic antiadhesive site of fibronectin, which contributes to cell regulation, including anoikis, through negative regulation of cell anchorage.
MeSH term(s)	Amino Acid Sequence ; Animals ; Anoikis/drug effects ; Anoikis/physiology ; Binding Sites ; Cell Adhesion/drug effects ; Cell Adhesion/physiology ; Cell Line ; Cell Line, Tumor ; Cell Membrane/metabolism ; Cell Survival/drug effects ; Cell Survival/physiology ; Culture Media, Serum-Free/pharmacology ; Electrophoresis, Polyacrylamide Gel ; Eukaryotic Initiation Factor-1/genetics ; Eukaryotic Initiation Factor-1/metabolism ; Eukaryotic Initiation Factor-1/physiology ; Extracellular Matrix/metabolism ; Extracellular Matrix/physiology ; Fibronectins/metabolism ; Fibronectins/physiology ; Humans ; K562 Cells ; Mice ; Microscopy, Confocal ; Molecular Sequence Data ; NIH 3T3 Cells ; Peptide Elongation Factor 1/genetics ; Peptide Elongation Factor 1/metabolism ; Peptide Elongation Factor 1/physiology ; RNA Interference
Chemical Substances	Culture Media, Serum-Free ; Eukaryotic Initiation Factor-1 ; Fibronectins ; Peptide Elongation Factor 1 ; eukaryotic peptide initiation factor-1A
Language	English
Publishing date	2012-03-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.308122
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Article: Cloning and Expression of Bombyx mori Silk Gland Elongation Factor 1γ in Escherichia coli

KAMIIE, Katsuyoshi / NOMURA, Yoshitaka / KOBAYASHI, Satoru / TAIRA, Hideharu / KOBAYASHI, Kohmei / YAMASHITA, Tetsuro / KIDOU, Shin-ichiro / EJIRI, Shin-ichiro

Bioscience, biotechnology, and biochemistry. 2002 Jan. 1, v. 66, no. 3

2002

Abstract: Elongation factor 1 (EF-1) from the silk gland of Bombyx mori consists of α-, β-, γ-, and δ-subunits. EF-1α•GTP catalyzes the binding of aminoacyl-tRNA to ribosomes concomitant with the hydrolysis of GTP. EF-1βγδ catalyzes the exchange of EF-1α-bound GDP ...

Abstract	Elongation factor 1 (EF-1) from the silk gland of Bombyx mori consists of α-, β-, γ-, and δ-subunits. EF-1α•GTP catalyzes the binding of aminoacyl-tRNA to ribosomes concomitant with the hydrolysis of GTP. EF-1βγδ catalyzes the exchange of EF-1α-bound GDP for exogenous GTP and stimulates the EF-1α-dependent binding of aminoacyl-tRNA to ribosomes. EF-1γ cDNA, which contains an open reading frame (ORF) encoding a polypeptide of 423 amino acid residues, was amplified and cloned by PCR from a silk gland cDNA library. The calculated molecular mass and predicted pI of the product were 48,388 Da and 5.84, respectively. The silk gland EF-1γ shares 67.3% amino acid identity with Artemia salina EF-1γ. The N-terminal domain (amino acid residues 1–211) of silk gland EF-1γ is 29.3% identical to maize glutathione S-transferase. We demonstrated that silk gland EF-1γ bound to glutathione Sepharose, suggesting that the N-terminal domain of EF-1γ may have the capacity to bind to glutathione.
Keywords	Artemia salina ; Bombyx mori ; Escherichia coli ; agarose ; biotechnology ; cDNA libraries ; corn ; glutathione ; glutathione transferase ; hydrolysis ; molecular weight ; peptide elongation factors ; polypeptides ; ribosomes ; silk glands
Language	English
Dates of publication	2002-0101
Size	p. 558-565.
Publishing place	Japan Society for Bioscience, Biotechnology, and Agrochemistry
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1271/bbb.66.558
Database	NAL-Catalogue (AGRICOLA)

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Bonn / Germany

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In stock of ZB MED Bonn / Germany

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED