In all eukaryotic genomes the genetic information is stored in a discontinous fashion. Exons and introns are fundamental units for the generation of a great diversity of RNA transcripts. The junction of exons and elimination of introns is achieved by a process known as splicing. This process is catalyzed by a huge macromolecular machinery that harbors more than 200 different proteins, called the spliceosome, that assembles in a stepwise manner. In an early step of assembly, the U2AF small subunit (U2AF35) binds the conserved AG dinucleotide just preceding the 3′ splice site. The U2AF large subunit (U2AF65) binds the polypyrimidine tract (PPT) through its tandem RNA recognition motifs (RRM). U2AF65 also possesses a C-terminal atypical RRM motif called “U2AF Homology Motif” (UHM). This atypical RRM has lost its RNA-binding ability, but it interacts with an N-terminal “UHM Ligand Motif” (ULM) of SF1. U2AF65 defects have been associated with a variety of human diseases. Acquired U2AF65 mutations recur among certain cancers, however their functional consequences are still not fully characterized. Here you can see a very recent structure of the human intact U2AF65 RRM-region bound to a synthetic oligonucleotide to illustrate its substrate specificity and function (PDB code: 7S3B)
#molecularart ... #immolecular ... #splicing ... #U2AF ... #U2AF65 ... #RNA ... #xtal
Structure of the U2AF65 splicing factor rendered with @proteinimaging and depicted with @corelphotopaint
#molecularart ... #immolecular ... #splicing ... #U2AF ... #U2AF65 ... #RNA ... #xtal
Structure of the U2AF65 splicing factor rendered with @proteinimaging and depicted with @corelphotopaint
