TERMINAL RIBOADENYLATE TRANSFERASE IN HUMAN LYMPHOCYTES
TERMINAL RIBOADENYLATE TRANSFERASE IN HUMAN LYMPHOCYTES
复制标题
DOI:
10.1038/248407a0
复制
发表时间:
1974-01-01
期刊:
影响因子:
64.8
通讯作者:
BOLLUM, FJ
中科院分区:
文献类型:
--
作者:
COLEMAN, MS;HUTTON, JJ;BOLLUM, FJ
TERMINAL riboadenylate transferase (TrT) catalyses the transfer of adenylate residues from ATP to the 3′-hydroxyl group of certain polyribonucleotides in the presence of Mn2+. Enzymes of this kind may be involved in the processing of heterogeneous nuclear RNA to mRNA in eukaryotic cells, since many types of mRNA have terminal poly (A) sequences. Evidence for this is rather fragmentary and is complicated by reports of several forms of poly (A)-polymerising activities in both nucleus and cytoplasm1–10. Clearer evidence might be obtained from systems that could be experimentally manipulated to show variation in the levels of activity of poly(A) polymerases and rates of mRNA synthesis. We have found that human lymphocytes exhibit increased TrT activity as part of their response to stimulation by phytohaemagglutinin (PHA)in vitro. This is the first mammalian, non-viral system in which increases in TrT activity have been observed with changes in the physiological state of the cell. The PHA-stimulated lymphocyte may be suitable for combined polymerase–mRNA turnover studies designed to clarify enzymatic steps in mRNA processing and terminal poly (A) addition, since Rosenfeldet al.11have reported increases in poly (A)-rich mRNA during lymphocyte transformation by PHA.