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doi: 10.1242/10.1242/dev.00222

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The Drosophila trithorax group gene tonalli(tna) interacts genetically with the Brahma remodeling complex and encodes an SP-RING finger protein

Luis Gutiérrez1, Mario Zurita1, James A. Kennison2 and Martha Vázquez1,*

1 Departamento de Fisiología Molecular y Genética del Desarrollo, Instituto de Biotecnología, UNAM, Cuernavaca, Morelos 62250, México
2 Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA



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  		Fig. 1. tna mutant phenotypes mimic homeotic loss-of-function phenotypes. In all panels wild type is on the left and the mutant is on the right (A) The held-out wings phenotype of a tna1/brm2 double heterozygote indicative of loss of Antp P2 function. (B) The partial transformation of haltere to wing in a tna1/tna4 mutant fly indicative of loss of Ubx function. (C) The reduction in the number of sex comb teeth on the first leg of a tna2/tna4 mutant male indicative of loss of Scr function.

 


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  		Fig. 3. Molecular organization and developmental expression of the tna locus. (A) The tna genomic region is represented at the bottom of the panel. The tna- P-element insertion sites are indicated by gray circles. The arrows by the insertions represent the orientation of the respective P-element with respect to the tna transcription direction. The tna+ EP0374 insertion site is shown as a white circle. The restriction sites are: B, BamHI; X, XbaI; E, EcoRI; H, HindIII. CG6418 is an RNA helicase transcribed towards the 3' end of the tna locus. The transcripts (mRNAs) are depicted in the middle of the panel. The BDGP, release 2-predicted transcripts containing the translated exons (black rectangles for shared, grey rectangles for the non-shared exons between tnaA and tnaB) are shown. We have added the 5' untranslated exon and the 3' poly(A)+ regions (white rectangles) deduced from our analysis of the locus. The 5' UTR exon is open on the left to indicate that the tna transcription initiation start site has not been determined. The indicated sizes of both transcripts are in agreement with the northern analysis shown in B. The upper part A (cDNAs) shows representative cDNAs isolated from the tna locus. AT07790 is one of several ESTs identified in adult testis. RE42750 is an EST from adult heads. The ZAP1 embryo cDNA clone was isolated from the UNI-ZAP library from 0-12-hour embryos (see Material and Methods) and was the probe for the northern blot shown in B. The PCR1 embryo cDNA clone was RT-PCR amplified with 5' and 3' primers sequences from the reported LD16921 embryonic clone (see Material and Methods). (B) RNA poly(A)+ was prepared from 0-3-hour and 3-21-hour embryos (0-3 and 3-21), first, second and third instar larvae (L1, L2, L3), pupae (P) and adults (A). Samples were blotted and run under standard conditions. The blot was probed with the ZAP1 cDNA (A). The blot was washed and rehybridized using a probe for rp49 as a loading control. The sizes of the detected bands are indicated.

 


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  		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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  		Fig. 2. Phenotypes from maternal loss of tna function. Prepupa (A) and young pupa (B) that lack both maternal and zygotic tna functions. These individuals are tna1/Df(3L)lxd6 [tna-] and very few individuals reach the pharate adult stage without paternal rescue. One of the males that reached the pharate adult stage is shown in C. The first leg has a smaller sex comb with fewer sex comb teeth (inset in C) suggesting a reduction in Scr function. (D) A tna1/+ male that lacked maternal Tna function but was rescued by the paternally-inherited wild-type allele. The paternally rescued males have sex combs with normal numbers of sex comb teeth (inset in D).

 

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