Prp19: Difference between revisions

Research has shown that different PRP proteins are involved in splicing in very different ways. For instance, some PRP proteins are directly associated with snRNPs (snurps) such as PRP8 and PRP18's with the [http://en.wikipedia.org/wiki/U5_snRNA <i>U5</i>] snRNP. Others interact with with snRNA at different times, such as PRP17 and PRP18 with U5, which are thought to play a functional role. Certain PRP proteins are involved in specific steps, such as PRP2's involvement in the first cleavage / ligation reaction. Furthermore, some PRPs play roles in snRNP binding. That is, PRP9, PRP11 and PRP21 are thought to help promote U2 binding early on in the spliceosomal assembly process. <ref name ="functional"/> Another important role of PRP proteins is helping to anneal the snRPS themselves. An example of this is [http://proteopedia.com/wiki/index.php/Sandbox_Reserved_340 <i>PRP24</i>] aiding in the association of U4 and U6, which form the disnRNP<ref name ="guthriescience">PMID 9452384</ref>.

Studies have found that PRP19 associates with the spliceosome around the time that the U4 snRNP disassociates from the complex. This is thought to be evidence towards PRP19's involvement in the conformational rearrangement that occurs at this stage of the splicing process.<ref name ="functional"/> Other evidence suggests that PRP19 acts to stabilize the association of U5 and U6 with the active spliceosome. Researchers have also suggested that PRP19 is part of a heteromeric complex which is comprised of at least eight different proteins,coined the nineteen complex or NTC.<ref name ="2004EMBO">PMID:15175653</ref> There is also evidence that PRP19 may be part of an even larger complex consisting of the U2, U5 and U6 snRNA as well as many other proteins.<ref name="ohi">PMID:12088152</ref>