Prp24: Difference between revisions

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OCA, Kara Perdue, Michal Harel, Alexander Berchansky

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 ===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.  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.  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 (reference Brow 2002).
+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>.
 The U4 snRNA is though to be non-catalytic because it leaves the spliceosome before the transesterification reactions occur.  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.  The U4 snRNP contains the U4 snRNA, a ring complex of the Sm proteins B-G, and the proteins Prp3, Prp4, and Snu13 (reference Brow 2002).