Characterization of the nuclear transport of a novel leucine‐rich acidic nuclear protein‐like protein

[摘要]

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 α. These findings suggest that mLANP-L is transported into the nucleus by Rch1 and/or NPI-1.

[学科分类] 生物化学/生物物理

[关键词] Nuclear protein import;Nuclear localization signal;Importin α;Leucine-rich acidic nuclear protein;Ataxin-1;NLS;nuclear localization signal;WGA;wheat germ agglutinin;LANP;leucine-rich acidic nuclear protein;NPC;nuclear pore complex