Demler S A, de Zoeten G A
Department of Plant Pathology, University of Wisconsin, Madison 53706.
J Gen Virol. 1991 Aug;72 ( Pt 8):1819-34. doi: 10.1099/0022-1317-72-8-1819.
An examination of the genomic strategy of pea enation mosaic virus (PEMV) RNA 1 has verified strong organizational and sequence relationships between PEMV and the beet western yellows-potato leafroll luteovirus subgroup. Sequence analysis of RNA 1 demonstrated five predominant open reading frames (ORFs). The extreme 5' ORF encodes a 34K product of unknown function. The second ORF encodes an 84K product which overlaps 90% of ORF 1 (in a unique reading frame) and is expressed by internal initiation beginning at the second start codon from the 5' terminus. This protein contains a protease-like motif characteristic of serine- and cysteine-based proteases, suggesting involvement in post-translational processing of viral translation products. The third ORF is characterized by a number of RNA polymerase motifs and a helicase-like motif typical of RNA-dependent RNA polymerases. It overlaps (out of frame) the ORF 2 product and is proposed to be expressed by a frameshift fusion of the ORF 2 and ORF 3 products. The fourth ORF encodes the viral coat protein, and is immediately followed in frame by a 33K ORF thought to represent the aphid transmission subunit of the PEMV virion. Northern blot analysis of polysome-associated RNA suggests that both products are expressed from an 1800 nucleotide subgenomic mRNA, with the 33K product expressed as a read-through fusion with the coat protein monomer.
对豌豆耳突花叶病毒(PEMV)RNA 1的基因组策略进行的研究证实了PEMV与甜菜西方黄化病毒-马铃薯卷叶黄化病毒亚组之间存在很强的组织和序列关系。RNA 1的序列分析显示有五个主要的开放阅读框(ORF)。最末端的5' ORF编码一个功能未知的34K产物。第二个ORF编码一个84K产物,它与ORF 1有90%的重叠(在一个独特的阅读框中),并通过从5'末端的第二个起始密码子开始的内部起始来表达。该蛋白质含有丝氨酸和半胱氨酸蛋白酶特有的蛋白酶样基序,表明其参与病毒翻译产物的翻译后加工。第三个ORF的特征是有许多RNA聚合酶基序和一个典型的依赖RNA的RNA聚合酶的解旋酶样基序。它与ORF 2产物重叠(移码),并被认为是由ORF 2和ORF 3产物的移码融合来表达的。第四个ORF编码病毒外壳蛋白,紧接着在框架内是一个33K的ORF,被认为代表PEMV病毒粒子的蚜虫传播亚基。对多聚核糖体相关RNA的Northern印迹分析表明,这两种产物都是从一个1800个核苷酸的亚基因组mRNA表达而来,33K产物作为与外壳蛋白单体的通读融合来表达。