Effect of basic and nonbasic amino acid substitutions on transport induced by simian virus 40 T-antigen synthetic peptide nuclear transport signals.

Effect of basic and nonbasic amino acid substitutions on transport induced by simian virus 40 T-antigen synthetic peptide nuclear transport signals.
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碱性和非碱性氨基酸取代对猿病毒40 T抗原合成肽核转运信号诱导转运的影响。

DOI:
10.1128/mcb.8.7.2722-2729.1988
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发表时间:
1988
影响因子:
5.3
通讯作者:
Kanda,P
Kanda,P
中科院分区:
生物学2区
文献类型:
--
作者:
Lanford,RE;White,RG;Dunham,RG;Kanda,P

文献摘要

被引文献

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先前的一项研究表明,与猿猴病毒40 T抗原核转运信号同源的合成肽能够诱导载体蛋白的核转运,并且肽诱导的转运依赖于T抗原第128位氨基酸对应的赖氨酸上的正电荷。在这项研究中,利用合成肽来检查 T 抗原核转运信号中氨基酸取代对转运的影响。将蛋白质-肽缀合物显微注射到哺乳动物细胞的细胞质中后,通过免疫荧光评估核转运。 128 位其他碱性氨基酸的取代揭示了核运输的层次结构。当赖氨酸位于 128 位时,核转运速率最快,其次是精氨酸、D-赖氨酸、鸟氨酸和对氨基苯丙氨酸。肽诱导的核转运依赖于位置 128 和 129 处带正电荷的氨基酸,因为这些位置处的中性天冬酰胺的取代消除了转运。然而,当大量肽与载体蛋白缀合时,在128位具有天冬酰胺的肽中观察到部分转运。
A previous study demonstrated the ability of a synthetic peptide homologous to the simian virus 40 T-antigen nuclear transport signal to induce the nuclear transport of carrier proteins and the dependence of peptide-induced transport on a positive charge at the lysine corresponding to amino acid 128 of T antigen. In this investigation synthetic peptides were utilized to examine the effect on transport of amino acid substitutions within the T-antigen nuclear transport signal. Nuclear transport was evaluated by immunofluorescence after microinjection of protein-peptide conjugates into the cytoplasm of mammalian cells. Substitution of other basic amino acids at position 128 revealed a hierarchy for nuclear transport. The rate of nuclear transport was most rapid when a lysine was at position 128 followed in descending order by arginine, D-lysine, ornithine, andp-aminophenylalanine. Peptide-induced nuclear transport was dependent upon a positively charged amino acid at positions 128 and 129, since substitutions of neutral asparagines at these positions abolished transport. However, partial transport was observed with the peptide having an asparagine at position 128 when a high number of peptides were conjugated to the carrier protein.