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J Biol Chem, Vol. 273, Issue 19, 11643-11649, May 8, 1998
From the Centro de Biología Molecular "Severo Ochoa,"
Departamento de Biología Molecular, Facultad de Ciencias,
Universidad Autónoma de Madrid, E-28049 Madrid, Spain
Multiple protein 4.1 isoforms are originated by
alternative pre-mRNA splicing, differential use of two translation
initiation sites, and posttranslational modifications. The complexity
of alternative splicing events suffered by the 4.1 pre-mRNA makes necessary the direct cloning of 4.1 full-coding cDNA sequences to
ensure that the encoded 4.1 proteins are naturally occurring isoforms.
We have approached this point by reverse transcription-polymerase chain
reaction techniques using RNA from the nucleated human Molt-4 T-cell
line as a starting template. Molecular cloning of 4.1 cDNAs using
the second translation initiation codon has allowed us to identify two
4.1 isoforms, designated 4.1H and 4.1I, which are differentially
targeted to the nucleus (4.1H) and the cytoplasm (4.1I). These two
isoforms differ only in the inclusion (4.1H) or exclusion (4.1I) of 21 amino acids encoded by exon 16. A cluster of basic amino acids, KKKR,
generated by joining of the sequences encoded by the constitutive exon
13 and the alternative exon 16, is necessary for the nuclear targeting
of 4.1H, as demonstrated by site-directed mutagenesis analysis.
Immunofluorescence microscopy and biochemical studies indicate that
4.1H belongs to the group of nuclear 4.1 proteins that are distributed
diffusely throughout the nucleoplasm and that are extractable in 0.5%
Triton X-100. This is the first demonstration of differential nuclear
targeting by the presence of an alternative domain, among naturally
occurring protein 4.1 isoforms.
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