嘌呤霉素
酪氨酸转氨酶
环己酰亚胺
信使核糖核酸
多形体
生物
蛋白质生物合成
酪氨酸
分子生物学
生物化学
丙氨酸
酶
核糖体
酶诱导剂
核糖核酸
氨基酸
基因
作者
Charles D. Stiles,Kai‐Lin Lee,Francis T. Kenney
标识
DOI:10.1073/pnas.73.8.2634
摘要
Through the use of an assay that measures cellular capacity for specific enzyme synthesis, mRNA of alanine aminotransferase (EC 2.6.1.2; L-alanine:2-oxoglutarate aminotransferase) was found to be degraded with a half-life of 12-14 hr in cultured Reuber H-35 cells; mRNA of tyrosine aminotransferase (EC 2.6.1.5; L-tyrosine:2-oxoglutarate aminotransferase) has a half-life of 2 hr in the same cells. Rates of degradation of the mRNAs are the same whether new mRNA accumulation is blocked by removal of the steroid inducer or by inhibition of mRNA synthesis (actinomycin). Cycloheximide inhibits the normally rapid turnover of tyrosine aminotransferase mRNA, but agents such as puromycin and sodium fluoride, which disrupt polysome structure, do not alter the turnover rate of the tyrosine and alanine aminotransferase mRNAs. The tyrosine and alanine aminotransferase mRNAs appear to be translated at equivalent rates. The data suggest that the degradation rate of these two mRNAs is determined by the polynucleotide structure of the mRNA molecules at or near the site for ribosome binding and initiation.
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