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Characterization of the nuclear transport of a novel leucine‐rich acidic nuclear protein‐like protein
Author(s) -
Matsubae Masami,
Kurihara Toshinao,
Tachibana Taro,
Imamoto Naoko,
Yoneda Yoshihiro
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01218-7
Subject(s) - chemistry , leucine , nuclear protein , characterization (materials science) , nuclear transport , biochemistry , nuclear pore , amino acid , cell nucleus , materials science , nanotechnology , cytoplasm , transcription factor , gene
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.