Chicken alpha-enolase but not beta-enolase has a Src-dependent tyrosine-phosphorylation site: cDNA cloning and nucleotide sequence analysis.
Chicken alpha-enolase but not beta-enolase has a Src-dependent tyrosine-phosphorylation site: cDNA cloning and nucleotide sequence analysis.
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发表时间：
1995
影响因子：
2.7
通讯作者：
M. Tanaka;K. Maeda;K. Nakashima
中科院分区：
文献类型：
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作者：
M. Tanaka;K. Maeda;K. Nakashima
鸡α-和β-烯醇化酶cDNA已被克隆和分析，以揭示α-而不是β-烯醇化酶具有Src依赖的磷酸化位点。氨基酸序列分析表明，鸡α-烯醇化酶与其它脊椎动物α-烯醇化酶，包括两栖动物（Xenopus laevis）α-like enolase的同源性均在90%以上。另一方面，鸡β-烯醇化酶与哺乳动物β-烯醇化酶共有84-85%的氨基酸序列同源性。这些鸡烯醇化酶也显示出超过70%的序列同一性与昆虫（果蝇）烯醇化酶和约60%的两个酵母烯醇化酶。鸡α-烯醇化酶第33 ~ 50位残基的氨基酸序列与已报道的兔β-烯醇化酶胰蛋白酶肽段序列一致，后者的酪氨酸残基在体外可被肉瘤病毒酪氨酸激酶磷酸化。本研究结果表明，在鸡α-烯醇化酶的44位的酪氨酸残基是酪氨酸激酶的磷酸化位点。另一方面，在鸡β-烯醇化酶中，发现相应的酪氨酸残基被组氨酸残基取代，这与先前的观察结果一致，即鸡β-烯醇化酶在体内或体外均不磷酸化。北方印迹分析表明，α-烯醇化酶mRNA可以在广泛的鸡组织中表达，并且在发育中的鸡肌肉中在孵化后立即发生从α-烯醇化酶到β-烯醇化酶的基因表达切换。
Chicken alpha- and beta-enolase cDNAs have been cloned and analyzed to reveal that alpha- but not beta-enolase has a Src-dependent phosphorylation site. The deduced amino acid sequence of the chicken alpha-enolase showed more than 90% homologies with those of other vertebrate alpha-enolases including amphibian (Xenopus laevis) alpha-like enolase. The chicken beta-enolase, on the other hand, shares 84-85% amino acid sequence homology with mammalian beta-enolases. These chicken enolases also showed more than 70% sequence identity with an insect (Drosophila melanogaster) enolase and around 60% with two yeast enolases. The amino acid sequence between residues 33 and 50 in chicken alpha-enolase coincided with the reported tryptic peptide sequence of rabbit beta-enolase, the tyrosine residue in which was phosphorylated in vitro by Rous-sarcoma-virus tyrosine kinase. The present finding suggested that the tyrosine residue at position 44 in chicken alpha-enolase is the phosphorylation site by the tyrosine kinase. In chicken beta-enolase, on the other hand, the corresponding tyrosine residue was found to be replaced with a histidine residue, in accordance with the previous observation that chicken beta-enolase was not phosphorylated in vivo or in vitro. Northern blot analysis indicated that alpha-enolase mRNA can be expressed in a wide range of chicken tissues, and that the gene expression switch from alpha to beta-enolase occurs just after hatching in developing chicken muscle.