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한국식물학회 / v.48, no.1, 2005년, pp.16-24 
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( cDNA Cloning and Expression Analysis of a CTP:Phosphoethanolamine Cytidylyltransferase from Barley ) |
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| To elucidate the relationship between the structure and function of CTP:phosphoethanolamine cytidylyltransferases (ECf, EC 2.7.7.14) in plants, we cloned and characterized the cDNA of an ECT from Hordeum vulgare. This HvECT1 cDNA is 1783 bp long, and includes an open reading frame (ORF) of 1263 b that encodes a protein of 421 amino acids. The predicted protein sequence of HvECT1 is $73%$ identical to and $84%$ similar with Arabidopsis thaliana AtECT1; it also shares 57, 55, and $37%$ similarities with human, rat, and yeast ECTs, respectively. Its 252-b 5'-noncoding leader contains a putative upstream ORF of 36 nucleotides, possibly encoding a putative peptide enriched in Ala and Pro residues. Alignment of the N-terminal and C-terminal halves of HvECT1 revealed a large internal repetitive sequence. Both halves contain the HXGH motif known to be involved in the catalytic activity of cytidylyltransferases. The RTXGVSTT sequence and Asp residues are also conserved. Our hydropathy profile showed that HvECT1 contains a signal sequence that is absent in yeast or animal ECTs. Results from reverse transcriptase-PCR indicated that HvECT1 is expressed highly in the leaves, stems, and roots of one-week-old plants; its expression is not regulated by low temperatures. After transforming a yeast mutant ect1 and labeling those transformants with radioactive ethanolamine, we identified HvECT1 cDNA through in vivo analyses of the enzymatic reaction products. |
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Journal of Plant Biology / v.48, no.1, 2005년, pp.16-24
한국식물학회
ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO200532217900596)
언어 : 영어 |
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| 논문 제공 : KISTI 한국과학기술정보연구원 |
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