A comparison of mammalian and yeast pre-mRNA 3'-end processing.
Many components of the mammalian and yeast pre-mRNA 3'-end-processing machinery have recently been purified and cDNAs or genes coding for these factors have been cloned. Most of the factors consist of multiple subunits, some of which serve to bind the RNA substrate, others of which are involved in forming a complex network of protein-protein interactions. Most of the mammalian 3'-end-processing factors are similar in their amino acid sequence to the yeast factors, indicating that they have a common evolutionary history.
Keller
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Department of Cell Biology, Biozentrum University of Basel, Klingelbergstrasse 70, CH-4056, Basel, Switzerland. Keller2@ubaclu.unibas.ch
Minvielle-Sebastia
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D000818:Animals; D046911:Macromolecular Substances; D008322:Mammals / Q000235:genetics*; D011061:Poly A / Q000378:metabolism*; D039102:Poly(A)-Binding Proteins; D011062:Polynucleotide Adenylyltransferase / Q000378:metabolism; D012322:RNA Precursors / Q000235:genetics*; D012323:RNA Processing, Post-Transcriptional; D012333:RNA, Messenger / Q000235:genetics*; D016601:RNA-Binding Proteins / Q000378:metabolism / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D013728:Terminator Regions, Genetic; D039221:mRNA Cleavage and Polyadenylation Factors
D046911:Macromolecular Substances; D039102:Poly(A)-Binding Proteins; D012322:RNA Precursors; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D039221:mRNA Cleavage and Polyadenylation Factors; D011061:Poly A; D011062:Polynucleotide Adenylyltransferase