In mouse, at least two catalytically active splice variants (mSMOalfa and mSMOmu) of the flavin-containing spermine oxidase enzyme are present. We have demonstrated previously that the cytosolic mSMOalfa is the major isoform, while the mSMOmu 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 mSMOmu 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.

Bianchi, M., Amendola, R., Federico, R., Polticelli, F., Mariottini, P. (2005). Two short domains are responsible for the nuclear localization of the mouse spermine oxidase mu isoform. THE FEBS JOURNAL, 272, 3052-3059 [10.1111/j.1742-4658.2005.04718.x].

Two short domains are responsible for the nuclear localization of the mouse spermine oxidase mu isoform

POLTICELLI, Fabio;MARIOTTINI, Paolo
2005-01-01

Abstract

In mouse, at least two catalytically active splice variants (mSMOalfa and mSMOmu) of the flavin-containing spermine oxidase enzyme are present. We have demonstrated previously that the cytosolic mSMOalfa is the major isoform, while the mSMOmu 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 mSMOmu 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.
Bianchi, M., Amendola, R., Federico, R., Polticelli, F., Mariottini, P. (2005). Two short domains are responsible for the nuclear localization of the mouse spermine oxidase mu isoform. THE FEBS JOURNAL, 272, 3052-3059 [10.1111/j.1742-4658.2005.04718.x].
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11590/142384
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 17
  • ???jsp.display-item.citation.isi??? 16
social impact