Fig. 4. The Tonalli proteins. (A) The two alternatively spliced forms predicted by the BDGP, release 2, are shown. In the upper part is a scale that indicates the aminoacid residues. In the TnaA protein the exons are indicated as E. E1 to E4 are exons shared between the TnaA and the TnaB forms. The glutamine rich domains are indicated by lightly shaded boxes. The bipartite nuclear location signal is indicated by the hatched box. The SP-RING finger is indicated by a black box. The TnaB carboxyl termini is indicated by the grey box and is different from the one in TnaA. The XSPRING domain, which is present in the human KIAA proteins and in proteins in other organisms, is indicated by the box above the proteins. (B) Multiple alignment of the SP-RING finger region in different proteins. KIAA1224 and KIAA1886 human proteins (accession numbers in Results); Su(var), D. melanogaster Su(var)2-10/ZimpA/B (gb/AAD29287.1); Miz1, (Msx-interacting-zinc finger) from mouse (gb/AAB96678.1); PIAS1 from mouse (gb/AAC36702.1); KCh, K⁺ channel-associated protein from rat (gb/AAC40114.1); PIAS3 from mouse (dbj/BAA78533.1); PIASy from human (gb/AAC36703.1); CEW10D5 predicted protein from C. elegans (pir/T26331); VICIA, Vicia faba transcription factor (pir/T12184); SER-INT, a Schizosaccharomyces pombe homologue (pir/T37748) of Saccharomyces cerevisiae Siz proteins; NFI1/SIZ2, CDC12 and septin-interacting protein in S. cerevisiae (gb/AAA86121.1); SIZ1, septin-interacting protein from S. cerevisiae (pir/S69691). The bottom line is the identical (in uppercase letters) and most common (lowercase) residues in all sequences. (C) Multiple alignment of Drosophila TnaA, human KIAA1224, and human KIAA1886 XSPRING domains (495-798). The glutamine 566 that changes for a stop codon in tna¹ is indicated by the residue number. The bipartite nuclear location signal residues are underlined. The SP-RING finger residues are indicated with asterisks. Consensus sequence of the same amino acid present in the three proteins is indicated.

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