Complementary DNA Encoding nm23/NDP Kinase Gene from the Korean Tiger Shark Scyliorhinus torazame

Cho, Jung Jong; Lee, Jae Hyung; Kim, Se‐Kwon; Choi, Tae-Jin; Kim, Young Tae

doi:10.1007/pl00011760

Cited by 5 publications

(4 citation statements)

References 32 publications

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“…Approximately 1 × 10 5 plaques were screened. Positive plaques recovered from the first screening were confirmed with a second screening (Kim and Richardson, 1994;Cho et al, 1999). The positive plaques were recovered from the second screening, and the phagemids containing inserts were excised (Lee et al, 2003).…”

Section: Screening For Astaxanthin Biosynthesis Genesmentioning

confidence: 99%

Cloning and characterization of the astaxanthin biosynthesis gene cluster from the marine bacterium Paracoccus haeundaensis

Lee

Kim

2006

Gene

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Section: Screening For Astaxanthin Biosynthesis Genesmentioning

confidence: 99%

Cloning and characterization of the astaxanthin biosynthesis gene cluster from the marine bacterium Paracoccus haeundaensis

Lee

Kim

2006

Gene

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“…In view of the potent inhibition of serpentine receptormediated PtdIns (3,4,5) P3 production and cell responses by wortmannin, the inactivation mechanism of PI3Kγ by this substance was investigated. When GST-p110a / p85a and P] ATP.…”

Section: Enzyme Activity Of Pi3kγmentioning

confidence: 99%

“…The flounder (Paralichthys olivaceus), one of the most evolved teleosts, is a commercially important marine aquaculture species in Korea and has been the object of studies on various functional genes at the molecular level [5,6,15]. The present study focuses on the isolation of cDNA encoding the flounder PI3Kγ and characterization of the cloned gene.…”

Section: Introductionmentioning

confidence: 99%

Cloning and Characterization of Phosphoinositide 3-Kinase γ cDNA from Flounder (Paralichthys olivaceus)

Jeong¹,

Youn²,

Ji³

et al. 2014

Journal of Life Science

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Phosphoinositide 3-kinase (PI3K) plays a central role in cell signaling and leads to cell proliferation, survival, motility, exocytosis, and cytoskeletal rearrangements, as well as specialized cell responses, superoxide production, and cardiac myocyte growth. PI3K is divided into three classes; type I PI3K is preferentially expressed in leukocytes and activated by βγ subunits of heterotrimeric G-proteins. In this study, the cDNAs encoding the PI3Kγ gene were isolated from a brain cDNA library constructed using the flounder (Paralichthys olivaceus). The sequence of the isolated PI3Kγ was 1341 bp, encoding 447 amino acids. The nucleotide sequence of the PI3Kγ gene was analyzed with that of other species, including Oreochromis niloticus and Danio rerio, and it turned out to be well conserved during evolution. The PI3Kγ gene was subcloned into the expression vector pET-44a(+), and expressed in the E. coli BL21 (DE3) codon plus cell. The resulting protein was expressed as a fusion protein of approximately 49 kDa containing a C-terminal six-histidine extension that was derived from the expression vector. The expressed protein was purified to homogeneity by His-tag affinity chromatography and showed enzymatic activity corresponding to PI3Kγ. The binding of wortmannin to PI3Kγ, as detected by anti-wortmannin antisera, closely followed the inhibition of the kinase activities. The results obtained from this study will provide a wider base of knowledge on the primary structure and characterization of the PI3Kγ at the molecular level.

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“…Approximately 1 × 10 5 plaques from the cDNA library were screened with the above probe. Positive plaques recovered from the first screening were further confirmed by the second screening [31][32][33]. Positive plaques were recovered from the second screening, and the phagemid containing the insert was excised according to the manufacturer's instructions (Stratagene, La Jolla, USA).…”

Section: Screening Cph Cdna and Dna Sequencingmentioning

confidence: 99%

Molecular characterization and tissue expression of carboxypeptidase H (CPH) gene in flounder (Paralichthys olivaceus)

Seo

Hwang

Kim

2011

Biotechnol Bioproc E

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Carboxypeptidase H (CPH) is one of several enzymes required for the processing of peptide hormone precursors and removal of basic amino acids from intermediates during protein biosynthesis. The CPH gene was isolated from a flounder (Paralichthys olivaceus) brain cDNA library and was found to consist of 1,590 bp encoding 455 amino acids residues. The nucleotide sequence of the CPH gene was compared with those of other species, including zebrafish and mouse, and turned out to be conserved during evolution. Expression of CPH mRNA was confirmed by both Reverse transcription polymerase Chain Reaction (RT-PCR) and Northern blot analysis. A recombinant protein of approximately 50 kDa, which corresponds to CPH, was functionally expressed in E. coli. Biochemical studies on the expressed protein were performed. We report here the molecular characteristics and tissue expression of newly identified CPH cDNA from flounder (P. olivaceus).

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Complementary DNA Encoding nm23/NDP Kinase Gene from the Korean Tiger Shark Scyliorhinus torazame

Cited by 5 publications

References 32 publications

Cloning and characterization of the astaxanthin biosynthesis gene cluster from the marine bacterium Paracoccus haeundaensis

Cloning and characterization of the astaxanthin biosynthesis gene cluster from the marine bacterium Paracoccus haeundaensis

Cloning and Characterization of Phosphoinositide 3-Kinase γ cDNA from Flounder (Paralichthys olivaceus)

Molecular characterization and tissue expression of carboxypeptidase H (CPH) gene in flounder (Paralichthys olivaceus)

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