Gamberi C, Contreas G, Romanelli M G, Morandi C
Istituto di Scienze Biologiche, Facoltà di Medicina e Chirurgia, Università di Verona, Italy.
Gene. 1994 Oct 11;148(1):59-66. doi: 10.1016/0378-1119(94)90233-x.
The yeast nucleolar protein-encoding gene NSR1 was isolated by low-stringency screening of a yeast genomic library with the human heterogeneous nuclear ribonucleoprotein type A1 (hnRNP A1) cDNA probe, and was mapped to chromosome VII. RNA abundance was determined and the transcription start point and polyadenylation site were mapped. A comparison between the Nsr1 and hnRNP A1 proteins, based on homopolymer RNA binding to their structural domains in vitro, revealed a striking biochemical similarity. When the N-terminal, lysine- and arginine-rich domain of Nsr1 was removed, the truncated protein behaved similarly to hnRNP A1; furthermore, the two RRM (RNA recognition motif) domains of Nsr1 behaved in the same manner as the two RRM domains of hnRNP A1. The biochemical data, therefore, would support the hypothesis that the two RRM domains in hnRNP A1 and Nsr1 interact with RNA in a similar manner in both mammalian and yeast cells, respectively.
通过用人源不均一核核糖核蛋白A1（hnRNP A1）cDNA探针低严谨性筛选酵母基因组文库，分离出酵母核仁蛋白编码基因NSR1，并将其定位到第七条染色体上。测定了RNA丰度，并确定了转录起始点和聚腺苷酸化位点。基于体外同聚物RNA与Nsr1和hnRNP A1蛋白结构域的结合，对二者进行比较，发现了显著的生化相似性。当去除Nsr1富含赖氨酸和精氨酸的N端结构域时，截短的蛋白表现得与hnRNP A1相似；此外，Nsr1的两个RRM（RNA识别基序）结构域的行为与hnRNP A1的两个RRM结构域相同。因此，生化数据支持这样的假说，即hnRNP A1和Nsr1中的两个RRM结构域分别在哺乳动物细胞和酵母细胞中以相似的方式与RNA相互作用。
