v-rel癌基因产物/pp40复合物的丝氨酸磷酸化

Serine phosphorylation of the v-rel oncogene product/pp40 complex.

作者信息

Tung H Y, Bargmann W J, Bose H R

机构信息

Clayton Foundation Biochemical Institute, University of Texas, Austin 78712.

出版信息

Biochem Biophys Res Commun. 1988 Apr 15;152(1):441-8. doi: 10.1016/s0006-291x(88)80733-2.

DOI:10.1016/s0006-291x(88)80733-2

PMID:2833896

Abstract

The transforming protein encoded by the v-rel oncogene of reticuloendotheliosis virus has been purified from REV-T transformed lymphoid cells by sequential DEAE-Sepharose and immunoaffinity chromatography. The purified preparation consisted of pp59v-rel and the 40 kDa cellular protein which is complexed with the v-rel oncogene product in transformed cells as well as some minor proteins. Incubation of this purified preparation in the presence of Mg2+ and (gamma-32P)ATP resulted in phosphorylation of both pp59v-rel and the 40 kDa protein. This preparation was also able to phosphorylate casein on serine residues. Immunoprecipitates obtained from extracts of REV-T transformed lymphoid cells labeled with 32P-orthophosphate contained 59 and 40 kDa phosphoproteins. Both pp59v-rel and the 40 kDa protein were phosphorylated on serine residues in transformed cells.

摘要

通过连续的二乙氨基乙基琼脂糖（DEAE - Sepharose）和免疫亲和层析，从网状内皮组织增生症病毒（REV）的v-rel癌基因编码的转化蛋白已从REV - T转化的淋巴细胞中纯化出来。纯化后的制剂由pp59v-rel和40 kDa细胞蛋白组成，该细胞蛋白在转化细胞中与v-rel癌基因产物复合，还有一些次要蛋白质。在Mg2+和（γ-32P）ATP存在的情况下，将这种纯化制剂进行温育，导致pp59v-rel和40 kDa蛋白都发生磷酸化。该制剂还能够使酪蛋白的丝氨酸残基磷酸化。从用32P - 正磷酸盐标记的REV - T转化淋巴细胞提取物中获得的免疫沉淀物含有59 kDa和40 kDa的磷蛋白。在转化细胞中，pp59v-rel和40 kDa蛋白的丝氨酸残基都发生了磷酸化。