IDENTIFICATION OF THE HUMAN C-MYC PROTEIN NUCLEAR TRANSLOCATION SIGNAL
IDENTIFICATION OF THE HUMAN C-MYC PROTEIN NUCLEAR TRANSLOCATION SIGNAL
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DOI：
10.1128/mcb.8.10.4048
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发表时间：
1988-10-01
影响因子：
5.3
通讯作者：
LEE, WMF
中科院分区：
文献类型：
--
作者：
DANG, CV;LEE, WMF
我们确定并表征了人类c-myc蛋白的两个区域，它们将蛋白质靶向细胞核。使用突变的c-myc蛋白质和蛋白质融合部分的c-myc鸡肌肉丙酮酸激酶，我们发现，残基320至328（PAAKRVKLD;肽M1）诱导完全核定位，和他们的去除c-myc导致突变蛋白质，分布在细胞核和细胞质，但保留大鼠胚胎细胞共转化活性。残基364至374（RQQRRNELKRSP;肽M2）仅诱导部分核靶向，并且它们从c-myc中去除导致突变蛋白保持核但无共转化活性。我们将含有M1或M2的合成肽与人血清白蛋白偶联，并将偶联物显微注射到Vero细胞的细胞质中。含有M1的肽引起快速和完全的核积累，而含有M2的肽引起较慢且仅部分的核定位。因此，M1作为c-myc的核定位信号发挥作用，而M2则发挥其他一些重要功能。
We identified and characterized two regions of the human c-myc protein that target proteins into the nucleus. Using mutant c-myc proteins and proteins that fuse portions of c-myc to chicken muscle pyruvate kinase, we found that residues 320 to 328 (PAAKRVKLD; peptide M1) induced complete nuclear localization, and their removal from c-myc resulted in mutant proteins that distributed in both the nucleus and cytoplasm but retained rat embryo cell cotransforming activity. Residues 364 to 374 (RQQRRNELKRSP; peptide M2) induced only partial nuclear targeting, and their removal from c-myc resulted in mutant proteins that remained nuclear but were cotransformationally inactive. We conjugated synthetic peptides containing M1 or M2 to human serum albumin and microinjected the conjugate into the cytoplasm of Vero cells. The peptide containing M1 caused rapid and complete nuclear accumulation, whereas that containing M2 caused slower and only partial nuclear localization. Thus, M1 functions as the nuclear localization signal of c-myc, and M2 serves some other and essential function.