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N-ras蛋白的生化及生物学活性

Biochemical and biological activities of N-ras proteins.

作者信息

Geis A M, Nicolson M, Goldman R A

出版信息

Biochem Biophys Res Commun. 1986 Sep 14;139(2):771-9. doi: 10.1016/s0006-291x(86)80057-2.

Abstract

Recombinant N-ras proteins, expressed and produced from synthetic genes cloned into E. coli, have been tested in vitro for GTPase and autophosphorylation activity. The genes corresponding to the assayed proteins were tested for their ability to transform NIH 3T3 cells. Mutations of glutamine to lysine at amino acid position 61 and glycine to valine at position 12 were both found to activate the ability of the N-ras gene to transform NIH 3T3 cells while significantly reducing the GTPase activity of the corresponding protein. N-ras proteins were also found to autophosphorylate in the presence of GTP when a threonine acceptor amino acid is provided at position 59.

摘要

从克隆到大肠杆菌中的合成基因表达并产生的重组N-ras蛋白,已在体外测试其GTP酶和自磷酸化活性。对与所检测蛋白对应的基因进行了转化NIH 3T3细胞能力的测试。发现第61位氨基酸的谷氨酰胺突变为赖氨酸以及第12位的甘氨酸突变为缬氨酸,均能激活N-ras基因转化NIH 3T3细胞的能力,同时显著降低相应蛋白的GTP酶活性。当在第59位提供苏氨酸受体氨基酸时,还发现N-ras蛋白在GTP存在的情况下会发生自磷酸化。

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