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Two short protein domains are responsible for the nuclear localization of the mouse spermine oxidase µ isoform
Author(s) -
Bianchi Marzia,
Amendola Roberto,
Federico Rodolfo,
Polticelli Fabio,
Mariottini Paolo
Publication year - 2005
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2005.04718.x
Subject(s) - nuclear localization sequence , gene isoform , flavin group , nuclear transport , alternative splicing , biochemistry , nuclear protein , biology , exon , microbiology and biotechnology , cytosol , spermine , enzyme , cytoplasm , cell nucleus , gene , transcription factor
In mouse, at least two catalytically active splice variants (mSMOα and mSMOµ) of the flavin‐containing spermine oxidase enzyme are present. We have demonstrated previously that the cytosolic mSMOα is the major isoform, while the mSMOµ enzyme is present in both nuclear and cytoplasmic compartments and has an extra protein domain corresponding to the additional exon VIa. By amino acid sequence comparison and molecular modeling of mSMO proteins, we identified a second domain that is necessary for nuclear localization of the mSMOµ splice variant. A deletion mutant enzyme of this region was constructed to demonstrate its role in protein nuclear targeting by means of transient expression in the murine neuroblastoma cell line, N18TG2.