Triana L, Ferreras A C, Cayama E, Correia H, Fraile G, Chakraburtty K, Herrera F
Centro de Investigaciones Biomédicas (BIOMED), Facultad de Ciencias dela Salud, Universidad de Carabobo, Maracay, Venezuela.
Arch Biochem Biophys. 1997 Aug 1;344(1):1-10. doi: 10.1006/abbi.1997.0173.
A yeast 50-kDa mRNA-binding protein (50mRNP) is found selectively associated with the 48S and 80S initiation complexes. This protein is structurally related to the translational elongation factor EF-1alpha. The protein reacts with antibodies directed against EF-1alpha and, similarly, EF-1alpha recognizes antibodies against the 50mRNP protein. This is evidence that they share at least one epitope which allows a similar antigenic behavior. In addition, both proteins show similar cleavage patterns upon treatment with the endoproteinase Lys-C. A murine antibody raised against 50mRNP inhibits both 48S and 80S initiation complex formation. The inhibitory effect is relieved by preincubating anti-50mRNP with EF-1alpha. Antibody to EF-1alpha manifests a similar inhibitory pattern for the formation of 48S and 80S complexes. These data strongly suggest that 50mRNP is an EF-1alpha-like polypeptide essential for the formation of the above complexes.
一种酵母50 kDa mRNA结合蛋白（50mRNP）被发现与48S和80S起始复合物选择性结合。该蛋白在结构上与翻译延伸因子EF-1α相关。该蛋白能与针对EF-1α的抗体发生反应，同样，EF-1α也能识别针对50mRNP蛋白的抗体。这证明它们至少共享一个表位，从而表现出相似的抗原行为。此外，用内肽酶Lys-C处理后，这两种蛋白显示出相似的裂解模式。一种针对50mRNP产生的鼠源抗体可抑制48S和80S起始复合物的形成。用EF-1α预孵育抗50mRNP可减轻这种抑制作用。针对EF-1α的抗体对48S和80S复合物的形成表现出类似的抑制模式。这些数据有力地表明，50mRNP是一种对上述复合物形成至关重要的类EF-1α多肽。
