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A critical step in the pre-mRNA splicing reaction is the stable binding of U2 snRNP to the branchpoint sequence (BPS) to form the A complex.
The self-catalytic protein splicing reaction is mediated by the intein plus the first carboxy-extein amino acid (aa), which are capable of splicing in heterologous exteins.
We have isolated and determined the protein composition of the spliceosomal complex C. The pre-mRNA in this complex has undergone catalytic step I, but not step II, of the splicing reaction.
U2, U6 and U5 snRNAs remain at the catalytic core throughout the splicing reaction.
These splicing factors function at early steps of the splicing reaction, during the initial recognition and specification of splicing signals.
Thus, 99.4% of hnRNA corresponds to intervening sequences that have to be removed during the splicing reaction.
Similar(19)
This trans-splicing reaction can be exploited by pre-trans-splicing molecules (PTMs), which are incapable of cis-splicing.
Presumably the oligonucleotide is added by a trans-splicing reaction since the gene donating the trans-spliced leader has been sequenced.
Split inteins are fractured proteins that catalyze the splicing of two flanking polypeptides together through a trans-splicing reaction.
Zettler, J., Schütz, V. & Mootz, H. D. The naturally split Npu DnaE intein exhibits an extraordinarily high rate in the protein trans-splicing reaction.
Split inteins have separate pieces (N-intein and C-intein) that reassemble non-covalently to catalyze a protein trans-splicing reaction joining two polypeptides.
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