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Molecular Biology of the Cell Vol. 15, 37823795, August 2004

Summary: Molecular Biology of the Cell
Vol. 15, 37823795, August 2004
Splicing Factor hSlu7 Contains a Unique Functional
Domain Required to Retain the Protein within the
Noam Shomron, Mika Reznik, and Gil Ast*
Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel Aviv
University, Tel Aviv, Israel 69978
Submitted February 25, 2004; Revised May 17, 2004; Accepted May 21, 2004
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 >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 that 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 chromosomal region maintenance 1 pathway. Thus,
the zinc-knuckle motif of hSlu7 determines the cellular localization of the protein through a nucleocytoplasmic-sensitive
shuttling balance. Altogether, this indicates that zinc-dependent nucleocytoplasmic shuttling might be the possible
molecular basis by which hSlu7 protein levels are regulated within the nucleus.


Source: Ast, Gil - Department of Molecular Genetics and Biochemistry, Tel Aviv University


Collections: Biology and Medicine