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西葫芦黄花叶病毒新加坡分离株外壳蛋白基因的核苷酸序列显示一个改变的DAG基序。

Nucleotide sequence of a Singapore isolate of zucchini yellow mosaic virus coat protein gene revealed an altered DAG motif.

作者信息

Lee S C, Wu M, Wong S M

机构信息

Department of Botany, National University of Singapore.

出版信息

Virus Genes. 1993 Dec;7(4):381-7. doi: 10.1007/BF01703393.

Abstract

A cDNA clone of zucchini yellow mosaic virus (ZYMV) RNA was mapped to the 3' terminal region. The nucleotide sequence revealed a single open reading frame of 1035 nucleotides followed by a 3' noncoding region of 215 nucleotides. The putative protease cleavage site for the release of coat protein (CP) was deduced to be between Glu-Ser (at amino acid position 66-67), which would result in a protein of 279 amino acids. This non-aphid-transmissible Singapore isolate of ZYMV showed a change of DAG to GAG triplet near the N-terminal of the CP. The CP gene was expressed as a protein fused to the beta-galactosidase in Escherichia coli and as an unfused protein in Saccharomyces cerevisiae.

摘要

西葫芦黄花叶病毒(ZYMV)RNA的一个cDNA克隆被定位到3'末端区域。核苷酸序列显示有一个1035个核苷酸的单一开放阅读框,后面跟着一个215个核苷酸的3'非编码区。推测的用于释放外壳蛋白(CP)的蛋白酶切割位点推断在Glu-Ser之间(氨基酸位置66-67),这将产生一个279个氨基酸的蛋白质。这种非蚜虫传播的ZYMV新加坡分离株在CP的N末端附近显示出DAG三联体变为GAG三联体。CP基因在大肠杆菌中作为与β-半乳糖苷酶融合的蛋白质表达,在酿酒酵母中作为未融合的蛋白质表达。

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