Prp24: Difference between revisions

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Evidence for a direct interaction of Prp24 and the Lsm proteins comes from a study in which the conserved residues in the C-terminal domain of Prp24 were deleted, resulting in lowered levels of U4/U6 and very literal interaction with the Lsm proteins as compared to wild-type Prp24, indicating that Prp24 interacts directly with the Lsm proteins and the C-terminal domain is necessary for this interaction <ref name="Rader"/>. Another indication of interaction between Prp24 and the Lsm proteins stems from a study showing that Lsm6 and Lsm7 are necessary in cells that require the recycling of the U4/U6 complex for splicing and that the presence of these two proteins increases the efficiency of annealing of U4 and U6 <ref name="Verdone">PMID:15324666</ref>. This suggests that Lsm6 and 7 are involved in a necessary interaction with Prp24 in the formation of U4/U6 di-snRNP.

More recently, a study has suggested that Prp24 interacts specifically with all the Lsm proteins involved in the U6 snRNP, and that the proteins act together as molecular chaperones to restructure and stabilize the 3' stem of U6 for base-pairing with U4 in stem II of U4/U6<ref name="Karaduman2006">PMID:16410014</ref>. Further support for specific interactions of Prp24 with the Lsm proteins comes from an electron microscopy study that showed Prp24 at specific differences from the subunits of the Lsm ring, suggesting that it interacts from a specified position within the U6 snRNP <ref name="Karaduman2006/>.

More recently, a study has suggested that Prp24 interacts specifically with all the Lsm proteins involved in the U6 snRNP, and that the proteins act together as molecular chaperones to restructure and stabilize the 3' stem of U6 for base-pairing with U4 in stem II of U4/U6<ref name="Karaduman2006">PMID:16410014</ref>. Further support for specific interactions of Prp24 with the Lsm proteins comes from an electron microscopy study that showed Prp24 at specific differences from the subunits of the Lsm ring, suggesting that it interacts from a specified position within the U6 snRNP <ref name="Karaduman2006"/>.

===Additional Interactions===

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@@ Line 64: / Line 64: @@
 Evidence for a direct interaction of Prp24 and the Lsm proteins comes from a study in which the conserved residues in the C-terminal domain of Prp24 were deleted, resulting in lowered levels of U4/U6 and very literal interaction with the Lsm proteins as compared to wild-type Prp24, indicating that Prp24 interacts directly with the Lsm proteins and the C-terminal domain is necessary for this interaction <ref name="Rader"/>.  Another indication of interaction between Prp24 and the Lsm proteins stems from a study showing that Lsm6 and Lsm7 are necessary in cells that require the recycling of the U4/U6 complex for splicing and that the presence of these two proteins increases the efficiency of annealing of U4 and U6 <ref name="Verdone">PMID:15324666</ref>.  This suggests that Lsm6 and 7 are involved in a necessary interaction with Prp24 in the formation of U4/U6 di-snRNP.
-More recently, a study has suggested that Prp24 interacts specifically with all the Lsm proteins involved in the U6 snRNP, and that the proteins act together as molecular chaperones to restructure and stabilize the 3' stem of U6 for base-pairing with U4 in stem II of U4/U6<ref name="Karaduman2006">PMID:16410014</ref>.  Further support for specific interactions of Prp24 with the Lsm proteins comes from an electron microscopy study that showed Prp24 at specific differences from the subunits of the Lsm ring, suggesting that it interacts from a specified position within the U6 snRNP <ref name="Karaduman2006/>.
+More recently, a study has suggested that Prp24 interacts specifically with all the Lsm proteins involved in the U6 snRNP, and that the proteins act together as molecular chaperones to restructure and stabilize the 3' stem of U6 for base-pairing with U4 in stem II of U4/U6<ref name="Karaduman2006">PMID:16410014</ref>.  Further support for specific interactions of Prp24 with the Lsm proteins comes from an electron microscopy study that showed Prp24 at specific differences from the subunits of the Lsm ring, suggesting that it interacts from a specified position within the U6 snRNP <ref name="Karaduman2006"/>.
 ===Additional Interactions===