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J Biol Chem, Vol. 273, Issue 26, 16005-16010, June 26, 1998

Cotranscription and Intergenic Splicing of Human Galactose-1-phosphate Uridylyltransferase and Interleukin-11 Receptor -Chain Genes Generate a Fusion mRNA in Normal Cells
IMPLICATION FOR THE PRODUCTION OF MULTIDOMAIN PROTEINS DURING EVOLUTION

Florence Magrangeas, Gilles Pitiot^¶, Sigrid Dubois, Elisabeth Bragado-Nilsson^¶, Michel Chérel, Séverin Jobert^¶, Benoit Lebeau, Olivier Boisteau, Bernard Lethé, Jacques Mallet^¶, Yannick Jacques, and Stéphane Minvielle

From  INSERM U463, 44035 Nantes, France, the ^¶ Laboratoire de Génétique Moléculaire de la Neurotransmission et des Processus Neurodégénératifs, CNRS UMR9923, 75013 Paris, France, and the  Cellular Genetics Unit, Université Catholique de Louvain and the Ludwig Institute for Cancer Research, B-1200 Brussels, Belgium

In the past 10 years, much attention has been focused on transcription preinitiation complex formation as a target for regulating gene expression, and other targets such as transcription termination complex assemblage have been less intensively investigated. We established the existence of poly(A) site choice and fusion splicing of two adjacent genes, galactose-1-phosphate uridylyltransferase (GALT) and interleukin-11 receptor -chain (IL-11R), in normal human cells. This 16-kilobase (kb) transcription unit contains two promoters (the first one is constitutive, and the second one, 8 kb downstream, is highly regulated) and two cleavage/polyadenylation signals separated by 12 kb. The promoter from the GALT gene yields two mRNAs, a 1.4-kb mRNA encoding GALT and a 3-kb fusion mRNA when the first poly(A) site is spliced out and the second poly(A) is used. The 3-kb mRNA codes for a fusion protein of unknown function, containing part of the GALT protein and the entire IL-11R protein. The GALT promoter/IL-11R poly(A) transcript results from leaky termination and alternative splicing. This feature of RNA polymerase (pol) II transcription, which contrasts with efficient RNA pol I and pol III termination, may be involved, together with chromosome rearrangements, in the generation of fusion proteins with multiple domains and would have major evolutionary implications in terms of natural processes to generate novel proteins with common motifs. Our results, together with accumulation of genomic informations, will stimulate new considerations and experiments in gene expression studies.

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