Identification of multiple nuclear localization signals in murine Elf3, an ETS transcription factor.
We investigated nuclear localization signal (NLS) determinants within the AT-hook and ETS DNA-binding domains of murine Elf3 (mElf3), a member of the subfamily of epithelium-specific ETS transcription factors. Deletion mutants containing the AT-hook, ETS domain or both localized strictly in the nucleus, suggesting that these individual domains contain independent NLS motif(s). Within the AT-hook domain, four basic residues (244KRKR247) were critical for strong NLS activity, and two potent bipartite NLS motifs (236-252 and 249-267) were sufficient for nuclear import of mElf3, although less efficient than the full domain. In addition, one stretch of basic residues (318KKK320) within the ETS domain appears to be essential for mElf3 nuclear localization. Taken together, mElf3 contains multiple NLS motifs, which may function cooperatively to effect efficient nuclear transport.
Do
Hyun-Jin
HJ
Chabiotech Co. Ltd., Seoul 135-907, South Korea.
Song
Hyuk
H
Yang
Heung-Mo
HM
Kim
Dong-Ku
DK
Kim
Nam-Hyung
NH
Kim
Jin-Hoi
JH
Cha
Kwang-Yul
KY
Chung
Hyung-Min
HM
Kim
Jae-Hwan
JH
D021581:Active Transport, Cell Nucleus; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019556:COS Cells; D002522:Chlorocebus aethiops; D004268:DNA-Binding Proteins / Q000737:chemistry*; D049452:Green Fluorescent Proteins; D051379:Mice; D008853:Microscopy; D019913:Nuclear Localization Signals / Q000737:chemistry*; D050784:Proto-Oncogene Protein c-ets-1 / Q000737:chemistry*; D014157:Transcription Factors / Q000737:chemistry*; D014162:Transfection
D004268:DNA-Binding Proteins; C494436:Elf3 protein, mouse; D019913:Nuclear Localization Signals; D050784:Proto-Oncogene Protein c-ets-1; D014157:Transcription Factors; D049452:Green Fluorescent Proteins