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禽白血病病毒E26的v-ets癌基因的5'末端编码的氨基酸序列并非源自主要的c-ets编码的细胞蛋白。

The 5' extremity of the v-ets oncogene of avian leukemia virus E26 encodes amino acid sequences not derived from the major c-ets-encoded cellular proteins.

作者信息

Gegonne A, Leprince D, Pognonec P, Dernis D, Raes M B, Stehelin D, Ghysdael J

出版信息

Virology. 1987 Jan;156(1):177-80. doi: 10.1016/0042-6822(87)90450-8.

Abstract

Antibodies were prepared against bacterially expressed polypeptides corresponding to various portions of the v-ets-encoded domain of P135gag-myb-ets, the transforming protein of avian leukemia virus E26. Immunoprecipitation analyses show that ca. 80 v-ets-encoded amino-acids located immediately after the v-myb/v-ets junction are not found in P54/56c-ets, the translation product of the c-ets proto-oncogene, nor in a set of cellular proteins of 64, 62, and 60 kDa related to but distinct from P54/56c-ets. In addition, Northern blot analyses show that these 5' v-ets sequences neither derive from the nontranslated region of the known cellular transcripts hybridizing to a v-ets probe nor from the c-myb transcript or the helper virus genetic information. Tryptic peptide analyses furthermore indicate that, except for these sequences and the last 16 carboxy terminal amino acids of P135gag-myb-ets, the amino acids encoded by v-ets are essentially colinear with those of P54c-ets.

摘要

制备了针对与禽白血病病毒E26的转化蛋白P135gag-myb-ets的v-ets编码结构域各部分相对应的细菌表达多肽的抗体。免疫沉淀分析表明,在c-ets原癌基因的翻译产物P54/56c-ets中,以及在一组与P54/56c-ets相关但不同的64、62和60 kDa细胞蛋白中,均未发现紧邻v-myb/v-ets连接处之后的约80个v-ets编码氨基酸。此外,Northern印迹分析表明,这些5' v-ets序列既不源自与v-ets探针杂交已知细胞转录本的非翻译区,也不源自c-myb转录本或辅助病毒遗传信息。胰蛋白酶肽分析进一步表明,除了这些序列以及P135gag-myb-ets的最后16个羧基末端氨基酸外,v-ets编码的氨基酸与P54c-ets的氨基酸基本共线。

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