| http://purl.uniprot.org/citations/9792439 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9792439 | http://www.w3.org/2000/01/rdf-schema#comment | "The apolipoprotein (apo) B mRNA can be modified by a posttranscriptional base change from cytidine to uridine at nucleotide position 6666. This editing of apo B mRNA is mediated by a specific enzyme-complex of which only the catalytic subunit APOBEC-1 (apo B mRNA editing enzyme component 1) has been cloned and extensively characterized. In this study, two-hybrid selection in yeast identified hnRNP C1 protein to interact with APOBEC-1. Recombinant hnRNP C1 protein inhibited partially purified apo B mRNA editing activity from rat small intestine and bound specifically to apo B sense RNA around the editing site. The inhibition of apo B mRNA editing by hnRNP C1 protein was not due to masking of the RNA substrate as the mutant protein M104 spanning the RNA-binding domain of hnRNP C1 protein bound strongly to the apo B RNA, but did not inhibit the editing reaction. The apo B mRNA editing enzyme-complex of rat liver nuclear extracts sedimented in sucrose density gradients around 22-27S, but did not contain hnRNP C1 protein that was found exclusively within 40S hnRNP complexes. The removal of 40S hnRNP complexes increased the activity of the 22-27S editing enzyme-complex. Adding back 40S hnRNP complexes with hnRNP C1 protein resulted in an inhibition of the 22-27S apo B mRNA editing enzyme-complex, while addition of 18S fractions had no effect. In conclusion, hnRNP C1 protein identified by two-hybrid selection in yeast is a potent inhibitor of the apo B mRNA editing enzyme-complex. The abundant hnRNP C1 protein, which is contiguously deposited on nascent pre-mRNA during transcription and is involved in spliceosome assembly and mRNA splicing, is a likely regulator of the editing of apo B mRNA which restricts the activity of APOBEC-1 to limited and specific editing events."xsd:string |
| http://purl.uniprot.org/citations/9792439 | http://purl.org/dc/terms/identifier | "doi:10.1515/bchm.1998.379.8-9.1063"xsd:string |
| http://purl.uniprot.org/citations/9792439 | http://purl.uniprot.org/core/author | "Greeve J."xsd:string |
| http://purl.uniprot.org/citations/9792439 | http://purl.uniprot.org/core/author | "Lellek H."xsd:string |
| http://purl.uniprot.org/citations/9792439 | http://purl.uniprot.org/core/author | "Greten H."xsd:string |
| http://purl.uniprot.org/citations/9792439 | http://purl.uniprot.org/core/author | "Rautenberg P."xsd:string |
| http://purl.uniprot.org/citations/9792439 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9792439 | http://purl.uniprot.org/core/name | "Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/9792439 | http://purl.uniprot.org/core/pages | "1063-1073"xsd:string |
| http://purl.uniprot.org/citations/9792439 | http://purl.uniprot.org/core/title | "Inhibition of the apolipoprotein B mRNA editing enzyme-complex by hnRNP C1 protein and 40S hnRNP complexes."xsd:string |
| http://purl.uniprot.org/citations/9792439 | http://purl.uniprot.org/core/volume | "379"xsd:string |
| http://purl.uniprot.org/citations/9792439 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9792439 |
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