The nuclear import of RNA helicase A is mediated by importin-{alpha}3

Journal Article · Fri Feb 03 00:00:00 EST 2006 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2005.11.161· OSTI ID:20798777

Aratani, Satoko ^[1]; Oishi, Takayuki ^[2]; Fujita, Hidetoshi ^[1]; Nakazawa, Minako ^[1]; Fujii, Ryouji ^[1]; Imamoto, Naoko ^[3]; Yoneda, Yoshihiro ^[4]; Fukamizu, Akiyoshi ^[2]; Nakajima, Toshihiro ^[1]

---

1. Department of Genome Science, Institute of Medical Science, St. Marianna University School of Medicine, 2-16-1 Sugao, Kawasaki, Kanagawa 216-8512 (Japan)
2. Center for Tsukuba Advanced Research Alliance, Graduate School of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennoudai, Tsukuba, Ibaraki 305-8572 (Japan)
3. Cellular Dynamics Laboratory, Discovery Research Institute, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198 (Japan)
4. Department of Frontier Biosciences, Graduate School of Frontier Biosciences, Osaka University, 2-2 Yamada-oka, Suita, Osaka 565-0871 (Japan)

RNA helicase A (RHA), an ATPase/helicase, regulates the gene expression at various steps including transcriptional activation and RNA processing. RHA is known to shuttle between the nucleus and cytoplasm. We identified the nuclear localization signal (NLS) of RHA and analyzed the nuclear import mechanisms. The NLS of RHA (RHA-NLS) consisting of 19 amino acid residues is highly conserved through species and does not have the consensus classical NLS. In vitro nuclear import assays revealed that the nuclear import of RHA was Ran-dependent and mediated with the classical importin-{alpha}/{beta}-dependent pathway. The binding assay indicated that the basic residues in RHA-NLS were used for interaction with importin-{alpha}. Furthermore, the nuclear import of RHA-NLS was supported by importin-{alpha}1 and preferentially importin-{alpha}3. Our results indicate that the nuclear import of RHA is mediated by the importin-{alpha}3/importin-{beta}-dependent pathway and suggest that the specificity for importin may regulate the functions of cargo proteins.

• OSTI ID: 20798777
• Journal Information: Biochemical and Biophysical Research Communications, Vol. 340, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2005.11.161; PII: S0006-291X(05)02709-9; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
AMINO ACIDS
CELL NUCLEI
CYTOPLASM
GENES
IN VITRO
PROTEINS
RABBIT TUBES
RNA
RNA PROCESSING
SPECIFICITY