Cloning and Characterization of UXT, a Novel Gene in Human Xp11, which Is Widely and Abundantly Expressed in Tumor Tissue

Schröer, Andreas; Schneider, Sebastian; Ropers, Hans‐Hilger; Nothwang, Hans Gerd

doi:10.1006/geno.1998.5712

Cited by 55 publications

(60 citation statements)

References 15 publications

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“…The C19ORF5 gene displayed a major transcript of about 3 kb in all twelve tissues tested with additional less abundant transcripts apparent in some tissues. Consistent with its name and a previous report [17], the UXT gene was expressed as a single transcript of about 0.75 kb at near equal levels in all 12 tissues. The C6ORF34 gene exhibited an mRNA at about 1 kb, which was most abundant in heart, skeletal muscle, kidney and liver, and least abundant in thymus and spleen.…”

Section: Lrpprc Interaction Partnerssupporting

confidence: 88%

“…The two-hybrid screen yielded a cDNA encoding the full-length 157-residue UXT (Ubiquitously Expressed Transcript) gene product from Xp11 that is widely expressed, most abundantly in heart and tumor tissues [17]. A 3D-PSSM analysis showed that UXT is characterized by a three α-helix bundle with similarities to the spectrin repeat [26], which was confirmed by MAXHOM multiple sequence alignment (Fig.…”

Section: Uxt (Xp_033860)-mentioning

confidence: 74%

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Sequence Analysis of LRPPRC and Its SEC1 Domain Interaction Partners Suggests Roles in Cytoskeletal Organization, Vesicular Trafficking, Nucleocytosolic Shuttling, and Chromosome Activity

2002

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LRPPRC (originally called LRP130) is an intracellular 130-kDa leucine-rich protein that copurifies with the FGF receptor from liver cell extracts and has been detected in diverse multiprotein complexes from the cell membrane, cytoskeleton and nucleus. Here we report results of a sequence homology analysis of LRPPRC and its SEC1 domain interactive partners. Twenty-three copies of tandem repeats that are similar to PPR, TPR and HEAT repeats characterize the LRPPRC sequence. The N-terminus exhibits multiple copies of leucine-rich nuclear transport signals followed by ENTH, DUF28 and SEC1 homology domains. We used the SEC1 domain to trap interactive partners expressed from a human liver cDNA library. Interactive C19ORF5 (XP_038600) exhibited a strong homology to microtubule-associated proteins (MAP) and a potential arginine-rich mRNA binding motif. UXT (XP_033860) exhibited α-helical properties homologous to the actin-associated spectrin repeat and L/I heptad repeats in mobile transcription factors. C6ORF34 (XP_004305) was homologous to the non-DNA binding C-terminus of the E. coli Rob transcription factor. CECR2 (AAK15343) exhibited a transcription factor AT-hook motif next to two bromodomains and a homology to guanylate-binding protein 1. Taken together these features suggest a regulatory role of LRPPRC and its SEC1 domain-interactive partners in integration of cytoskeletal networks with vesicular trafficking, nucleocytosolic shuttling, chromosome remodeling and transcription.

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Section: Lrpprc Interaction Partnerssupporting

confidence: 88%

Section: Uxt (Xp_033860)-mentioning

confidence: 74%

Sequence Analysis of LRPPRC and Its SEC1 Domain Interaction Partners Suggests Roles in Cytoskeletal Organization, Vesicular Trafficking, Nucleocytosolic Shuttling, and Chromosome Activity

2002

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“…UXT/ART-27 was mapped to the Xp11 locus, a region responsible of a number of genetic disorders, including Renpenning, Prieto, and Sutherland-Haan syndromes, but does not appear to be involved in their onset (Schroer et al 1999).…”

Section: Uxt (Art-27/stap1)mentioning

confidence: 99%

“…In a separate study, UXT was also shown to bind the transcriptional repressor Evi1 and inhibit its cell transformation property in Rat1 cells (McGilvray et al 2007). Conversely, UXT was found to be overexpressed in many other tumor cell lines (Schroer et al 1999;Zhao et al 2005a).…”

Section: Uxt (Art-27/stap1)mentioning

confidence: 99%

New insights into the biogenesis of nuclear RNA polymerases?This paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

Cloutier

Coulombe

2010

Biochem. Cell Biol.

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More than 30 years of research on nuclear RNA polymerases (RNAP I, II, and III) has uncovered numerous factors that regulate the activity of these enzymes during the transcription reaction. However, very little is known about the machinery that regulates the fate of RNAPs before or after transcription. In particular, the mechanisms of biogenesis of the 3 nuclear RNAPs, which comprise both common and specific subunits, remains mostly uncharacterized and the proteins involved are yet to be discovered. Using protein affinity purification coupled to mass spectrometry (AP-MS), we recently unraveled a high-density interaction network formed by nuclear RNAP subunits from the soluble fraction of human cell extracts. Validation of the dataset using a machine learning approach trained to minimize the rate of false positives and false negatives yielded a highconfidence dataset and uncovered novel interactors that regulate the RNAP II transcription machinery, including a set of proteins we named the RNAP II-associated proteins (RPAPs). One of the RPAPs, RPAP3, is part of an 11-subunit complex we termed the RPAP3/R2TP/prefoldin-like complex. Here, we review the literature on the subunits of this complex, which points to a role in nuclear RNAP biogenesis.

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“…1b,c) Figure 4 Expression patterns of genes located on the H locus. Expression levels of genes in female hindwings at stages P1-P2 (n = 4 for mimetic; n = 3 for non-mimetic), P4-P5 (n = 6 for mimetic; n = 3 for non-mimetic) and P10.5 (n = 3 for mimetic; n = 3 for non-mimetic), as analyzed Gene annotation for both the h-and H-type chromosomes identified three independent transcripts near the left breakpoints, ubiquitously expressed transcript (UXT; transcriptional regulator) 8 , unknown-3-exons (U3X; long noncoding RNA emerging in the H locus) and unknown transcripts downstream of prospero (Supplementary Figs. 3 and 4), that had higher expression in the wings of mimetic females (HH or Hh) than in those of non-mimetic females (hh) (Fig.…”

mentioning

confidence: 99%

A genetic mechanism for female-limited Batesian mimicry in Papilio butterfly

et al. 2015

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0 5In Batesian mimicry, animals avoid predation by resembling distasteful models. In the swallowtail butterfly Papilio polytes, only mimetic-form females resemble the unpalatable butterfly Pachliopta aristolochiae. A recent report showed that a single gene, doublesex (dsx), controls this mimicry 1 ; however, the detailed molecular mechanisms remain unclear. Here we determined two whole-genome sequences of P. polytes and a related species, Papilio xuthus, identifying a single ~130-kb autosomal inversion, including dsx, between mimetic (H-type) and non-mimetic (h-type) chromosomes in P. polytes. This inversion is associated with the mimicry-related locus H, as identified by linkage mapping. Knockdown experiments demonstrated that female-specific dsx isoforms expressed from the inverted H allele (dsx(H)) induce mimetic coloration patterns and simultaneously repress non-mimetic patterns. In contrast, dsx(h) does not alter mimetic patterns. We propose that dsx(H) switches the coloration of predetermined wing patterns and that female-limited polymorphism is tightly maintained by chromosomal inversion.

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Cloning and Characterization of UXT, a Novel Gene in Human Xp11, which Is Widely and Abundantly Expressed in Tumor Tissue

Cited by 55 publications

References 15 publications

Sequence Analysis of LRPPRC and Its SEC1 Domain Interaction Partners Suggests Roles in Cytoskeletal Organization, Vesicular Trafficking, Nucleocytosolic Shuttling, and Chromosome Activity

Sequence Analysis of LRPPRC and Its SEC1 Domain Interaction Partners Suggests Roles in Cytoskeletal Organization, Vesicular Trafficking, Nucleocytosolic Shuttling, and Chromosome Activity

A genetic mechanism for female-limited Batesian mimicry in Papilio butterfly

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