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KMID : 0578319930030010027
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Molecules and Cells
1993 Volume.3 No. 1 p.27 ~ p.33
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Molecular Cloning of chicken Elongation Factor 2 (EF-2)
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Kim, Choong Won
Kim, Yeon Woong/Kang, Kee Ryeon/Eom, Mi-Ok/Jung, Eun Joo/Kim, Jong Chul/Ahn, Hong Joon
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Abstract
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Chicken elongation factor 2 (EF-2) cDNA was isolated from a chicken intestine cDNA library and its nucleotide sequence was determined. The probe for the screening of library was prepared by polymerase chain reaction (PCR) using two degenerate oligonucleotide primers encoding an NH2-terminal region (residues 9-14) of chicken EF-2 and a conserved GTP-binding domain (residues 80-84) of hamster EF-2. The sequence of amplified 228-bp product was identical to that of hamster EF-2 (residues 9-84). One of the five positive clones, pCEK4, consisted of 3,144 nucleotides with 2,574-bp open reading frame coding for 858 amino acid residues. The M, 95,361 of the protein calculated from the amino acid sequence agreed well with the molecular weight of chicken EF-2 (95,000) measured by SDS-PAGE. Sequence identity between chicken and other mammalian EF-2s (human, hamster and rat) was 97%, while the sequence of GTP-binding/hydrolysis domain was 99% identical. This result indicates that EF-2 is one of the highly conserved proteins and its structure has not changed significantly during evolution. When expression of EF-2 in various stages of chicken embryo development was estimated by measuring mRNA and protein of EF-2, the result showed that the levels of EF-2 mRNA and protein were the highest in day 3 embryo and then decreased gradually.
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