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MBC in Press, published online ahead of print June 4, 2004
Mol. Biol. Cell 10.1091/mbc.E04-02-0152

A more recent version of this article appeared on August 1, 2004
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Submitted on February 25, 2004
Revised on May 17, 2004
Accepted on May 21, 2004

Splicing Factor hSlu7 Contains a Unique Functional Domain Required to Retain the Protein within the Nucleus

Noam Shomron, Mika Reznik, and Gil Ast*

Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel

Monitoring Editor: Joseph Gall

Precursor-mRNA splicing removes the introns and ligates the exons to form a mature mRNA. This process is carried out in a spliceosomal complex containing more than 150 proteins and five small nuclear ribonucleoproteins. Splicing protein hSlu7 is required for correct selection of the 3' splice site. Here we identify by bioinformatics and mutational analyses three functional domains of the hSlu7 protein that have distinct roles in its subcellular localization - a Nuclear Localization Signal, a zinc-knuckle motif, and a lysine-rich region. The zinc-knuckle motif is embedded within the Nuclear Localization Signal in a unique functional structure which is not required for hSlu7’s entrance into the nucleus but rather to maintain hSlu7 inside it, preventing its shuttle back to the cytoplasm via the CRM1 pathway. Thus, the zinc-knuckle motif of hSlu7 determines the cellular localization of the protein through a nucleo-cytoplasmic sensitive shuttling balance. Altogether this indicates that zinc-dependant nucleo-cytoplasmic shuttling might be the possible molecular basis by which hSlu7 protein levels are regulated within the nucleus.

*Corresponding author. E-mail: gilast{at}post.tau.ac.il






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