Prp24: Difference between revisions

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===U6 and U4 snRNPs===
===U6 and U4 snRNPs===


U6 is considered to be one of the most catalytically important snRNAs in the spliceosome, as it interacts directly with the 5' splice site through base pairing <ref name="Fortner">PMID:8299941</ref>.  It is thought to undergoe three conformational changes throughout the entire process of splicing and splicesome assembly; it exists as one conformation as free U6 snRNP, another conformation as part of the U4/U6 di-snRNP and a third conformation associated with U2 and the pre-mRNA <ref name="Jandrositz">PMID:7882985</ref>.  In addition to Prp24, U6 is associated with seven other proteins, Lsm 2-8, which form a ring around the 3' portion of the U6 snRNA <ref name="Karaduman2008">PMID:18971323</ref>.
U6 is considered to be one of the most catalytically important snRNAs in the spliceosome, as it interacts directly with the 5' splice site through base pairing <ref name="Fortner">PMID:8299941</ref>.  It is thought to undergo three conformational changes throughout the entire process of splicing and splicesome assembly; it exists as one conformation as free U6 snRNP, another as part of the U4/U6 di-snRNP and as a third when associated with U2 and the pre-mRNA <ref name="Jandrositz">PMID:7882985</ref>.  In addition to Prp24, U6 is associated with seven other proteins, Lsm 2-8, which form a ring around the 3' portion of the U6 snRNA <ref name="Karaduman2008">PMID:18971323</ref>.


The U4 snRNA is though to be non-catalytic because it leaves the spliceosome before the transesterification reactions occur <ref name="Staley"/>.  Its function is instead thought to be aiding U6 in maintaining a conformation that will enable it to interact with U2 and the 5' splice site <ref name="Madhani">PMID:2149118</ref>.  The U4 snRNP contains the U4 snRNA, a ring complex of the Sm proteins B-G, and the proteins Prp3, Prp4, and Snu13 <ref name="Brow review"/>.
The U4 snRNA is thought to be non-catalytic because it leaves the spliceosome before the transesterification reactions occur <ref name="Staley"/>.  Its function is instead thought to be aiding U6 in maintaining a conformation that will enable it to interact with U2 and the 5' splice site <ref name="Madhani">PMID:2149118</ref>.  The U4 snRNP contains the U4 snRNA, a ring complex of the Sm proteins B-G, and the proteins Prp3, Prp4, and Snu13 <ref name="Brow review"/>.


The annealing of the U4 and U6 snRNAs to form the U4/U6 di-snRNP complex, which contains the additional proteins Prp6 and Prp31, is an essential process in the formation of the spliceosome <ref name="Brow review"/>.  It enables interaction with the U5 snRNP to form the U4/U6.U5 complex which serves to deliver the U5 and U6 snRNPs to the appropriate sites in the pre-spliceosome complex to form a catalytically active spliceosome upon departure of U1 and U4 <ref name="Brow review"/>.
The annealing of the U4 and U6 snRNAs to form the U4/U6 di-snRNP complex, which contains the additional proteins Prp6 and Prp31, is an essential process in the formation of the spliceosome <ref name="Brow review"/>.  It enables interaction with the U5 snRNP to form the U4/U6.U5 complex which serves to deliver the U5 and U6 snRNPs to the appropriate sites in the pre-spliceosome complex, forming a catalytically active spliceosome upon departure of U1 and U4 <ref name="Brow review"/>.


===Role of Prp24 in Splicing===   
===Role of Prp24 in Splicing===