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DrosophilaGTPase Nucleostemin 2 Changes Cellular Distribution during Larval Development and the GTP-Binding Motif Is Essential to Nucleoplasmic Localization
Author(s) -
Eriko Matsuo,
Toshihiro Nagamine,
Shogo Matsumoto,
Kazuhide Tsuneizumi
Publication year - 2011
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.110212
Subject(s) - nucleoplasm , nucleolus , biology , ribosome biogenesis , microbiology and biotechnology , gtpase , ran , cytoplasm , nuclear protein , gtp' , nuclear localization sequence , subcellular localization , cell nucleus , nuclear transport , genetics , rna , transcription factor , ribosome , gene , biochemistry , enzyme
Nucleostemin (NS), a nucleolar guanosine triphosphate (GTP)-binding protein, plays significant roles in cell cycle progression and ribosomal biogenesis. Drosophila Nucleostemin 2 (NS2), a member of the Drosophila NS family, regulates early eye development and is essential to cell survival in vivo, but the underlying mechanisms have yet to be clarified. Biochemical analysis using the recombinant NS2 protein indicated that NS2 has GTPase activity. Immunohistochemistry revealed that NS2 changes in subcellular locus from the nucleolus to the nucleoplasm during larval development, and that a mutation in the ATP/GTP-binding site motif A (p-loop) prevents nuclear localization of NS2 and results in cytoplasmic distribution. Furthermore, downregulation of NS2 altered the rRNA proportions between the nucleus and the cytoplasm. These results suggest that NS2 at least requires GTP to import into the nucleoplasm.

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