Identification of the cellular targets of the transcription factor TCERG1 reveals a prevalent role in mrna processing
| Autor: | Pearson, J.L., Robinson, T.J., Muñoz, M.J., Kornblihtt, A.R., Garcia-Blanco, M.A. |
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| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
RNA splicing
Transcription Genetic Polymers Short interfering rnas Biochemistry Computational approaches Hela cells High confidences genetics RNA Small Interfering transcription factor cell strain HEK293 target cell Pcr analysis Oligonucleotide Array Sequence Analysis Targets microRNA messenger RNA Reverse Transcriptase Polymerase Chain Reaction article cell line protein function unclassified drug Nucleic acids female priority journal transcription regulation Untranslated regions Transcription HeLa cell Rna polymerase ii drug antagonism Binding sites embryo Binding energy Transcriptional regulations knockout gene reverse transcription polymerase chain reaction Gene expression analysis Reverse transcriptions Transcription factors gene expression profiling Humans controlled study human RNA Messenger Analysis of datums binding site human cell TCERG1 protein human DNA microarray genetic transcription Proteins nucleotide sequence 3' untranslated region small interfering RNA Cellular targets unindexed sequence MicroRNAs RNA processing transcription factor tcerg1 physiology Spliceosomes gene expression Trans-Activators RNA microarray analysis Microarray datums spliceosome metabolism transactivator protein |
| Zdroj: | J. Biol. Chem. 2008;283(12):7949-7961 Biblioteca Digital (UBA-FCEN) Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales instacron:UBA-FCEN |
| Popis: | The transcription factor TCERG1 (also known as CA150) associates with RNA polymerase II holoenzyme and alters the elongation efficiency of reporter transcripts. TCERG1 is also found as a component of highly purified spliceosomes and has been implicated in splicing. To elucidate the function of TCERG1, we used short interfering RNA-mediated knockdown followed by en masse gene expression analysis to identify its cellular targets. Analysis of data from HEK293 and HeLa cells identified high confidence targets of TCERG1. We found that targets of TCERG1 were enriched in microRNA-binding sites, suggesting the possibility of post-transcriptional regulation. Consistently, reverse transcription-PCR analysis revealed that many of the changes observed upon TCERG1 knockdown were because of differences in alternative mRNA processing of the 3′-untranslated regions. Furthermore, a novel computational approach, which can identify alternatively processed events from conventional microarray data, showed that TCERG1 led to widespread alterations in mRNA processing. These findings provide the strongest support to date for a role of TCERG1 in mRNA processing and are consistent with proposals that TCERG1 couples transcription and processing. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc. Fil:Muñoz, M.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Kornblihtt, A.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. |
| Databáze: | OpenAIRE |
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