Matsubae M, Kurihara T, Tachibana T, Imamoto N, Yoneda Y
Department of Cell Biology, Osaka University, 2-2 Yamada-oka, Suita, Osaka, Japan.
FEBS Lett. 2000 Feb 25;468(2-3):171-5. doi: 10.1016/s0014-5793(00)01218-7.
We previously reported that the nuclear localization signal (NLS) peptides stimulate the in vitro phosphorylation of several proteins, including a 34 kDa protein. In this study, we show that this specific 34 kDa protein is a novel murine leucine-rich acidic nuclear protein (LANP)-like large protein (mLANP-L). mLANP-L was found to have a basic type NLS. The co-injection of Q69LRan-GTP or SV40 T-antigen NLS peptides prevented the nuclear import of mLANP-L. mLANP-L NLS bound preferentially to Rch1 and NPI-1, but not to the Qip1 subfamily of importin alpha. These findings suggest that mLANP-L is transported into the nucleus by Rch1 and/or NPI-1.
我们之前报道过，核定位信号（NLS）肽可刺激几种蛋白质的体外磷酸化，包括一种34 kDa的蛋白质。在本研究中，我们表明这种特定的34 kDa蛋白质是一种新型的富含亮氨酸的酸性核蛋白（LANP）样大蛋白（mLANP-L）。发现mLANP-L具有一种碱性类型的NLS。共注射Q69LRan-GTP或SV40 T抗原NLS肽可阻止mLANP-L的核输入。mLANP-L NLS优先与Rch1和NPI-1结合，但不与输入蛋白α的Qip1亚家族结合。这些发现表明mLANP-L通过Rch1和/或NPI-1转运到细胞核中。
