Depurination of plant ribosomes by pokeweed antiviral protein.
Depurination of plant ribosomes by pokeweed antiviral protein.
复制标题
商陆抗病毒蛋白对植物核糖体进行脱嘌呤。
DOI：
10.1016/0014-5793(90)81070-5
复制
发表时间：
1990
期刊：
影响因子：
3.5
通讯作者：
Irvin,JD
中科院分区：
文献类型：
--
作者：
Taylor,BE;Irvin,JD
哺乳动物的核糖体被核糖体失活蛋白（RIP）通过特异性的rRNA脱嘌呤作用进行酶促修饰。在这里，我们报告说，核糖体分离小麦胚芽含有完整的和underpinated rRNA和脱嘌呤美洲商陆抗病毒蛋白（PAP）。将在相同条件下分离的美洲商陆核糖体脱嘌呤。从美洲商陆中提取的总RNA在强变性剂存在下被发现部分脱嘌呤。我们得出结论，小麦胚芽核糖体对内源性RIP、三羟甲基氨基甲烷具有抗性，但对PAP敏感，并且美洲商陆核糖体可以在分离过程中被内源性PAP的N-糖苷酶活性脱嘌呤。
Mammalian ribosomes have been shown to be enzymatically modified by ribosomal inactivating protein (RIPs) via specific depurination of rRNA. Here we report that ribosomes isolated from wheat germ contain intact and undepurinated rRNA and are depurinated by pokeweed antiviral protein (PAP). Pokeweed ribosomes isolated under the same conditions are depurinated. Total RNA isolated from pokeweed in the presence of strong denaturants was found to pbe partially depurinated. We conclude that wheat germ ribosomes are resistant to the endogenous RIP, tritin, but are sensitive to PAP and that pokeweed ribosomes can be depurinated by the N‐glycosidase activity of endogenous PAP during isolation.