Prp24: Difference between revisions

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The key structural elements of Prp24 are the conserved RNA recognition motifs (RRMs). These motifs are found in many proteins with RNA binding properties and contain conserved RNP elements that are recognizable by their primary sequence <ref name="Shannon"/>. For several years, Prp24 was thought to contain three RRMs, termed RRM 1, RRM 2, and RRM 3 ~~(green link)~~<ref name="Shannon"/>. However, analysis of homologs of Prp24 from several different species allowed the identification of a fourth RRM in Prp24 of ''S. cerevisiae'', albeit one that was much less highly conserved and not easily recognizable by its RNP-consensus domain <ref name="Rader"/>.

The key structural elements of Prp24 are the conserved RNA recognition motifs (RRMs). These motifs are found in many proteins with RNA binding properties and contain conserved RNP elements that are recognizable by their primary sequence <ref name="Shannon"/>. For several years, Prp24 was thought to contain three RRMs, termed RRM 1, RRM 2, and RRM 3 <ref name="Shannon"/>. However, analysis of homologs of Prp24 from several different species allowed the identification of a fourth RRM in Prp24 of ''S. cerevisiae'', albeit one that was much less highly conserved and not easily recognizable by its RNP-consensus domain <ref name="Rader"/>.

===RNA Recognition Motifs===

Prp24 contains four RRMs, RRM 1, RRM 2, RRM 3, and RRM 4. These motifs have a canonical structure of a platform of four β-strands with two α-helices on one side of the β-sheet plane ~~(green link)~~. These RRMs are present in many proteins that bind to to single stranded regions of RNA <ref name="RRM"/> and their presence in Prp24 supports a role for the annealing of U4 and U6 snRNAs into the U4/U6 structure.

Prp24 contains four RRMs, RRM 1, RRM 2, RRM 3, and RRM 4. These motifs have a <scene name='Sandbox_Reserved_340/2ghp/6'>canonical structure of a platform of four β-strands with two α-helices on one side of the β-sheet plane</scene>. These RRMs are present in many proteins that bind to to single stranded regions of RNA <ref name="RRM"/> and their presence in Prp24 supports a role for the annealing of U4 and U6 snRNAs into the U4/U6 structure.

Within each RRM, there are RNP consensus domains <ref name="RRM">PMID:15853797</ref>. These are the regions in the β-strands that are thought to actually interact with the RNA <ref name="RRM"/>. These regions seem to be very important in Prp24 and its interaction with U4 and U6. The study that first identified a probable link between the Prp24 protein and U4/U6 found that mutations in RNP 1 and RNP 2 of the carboxy terminal RRM (green link) rescued a cold-sensitive phenotype caused by a U4 mutation in stem II of U4/U6 <ref name="Shannon"/>. Two further studies <ref name="Vidaver"/> <ref name="Kwan">PMID:15811912</ref> showed that the mutation of three highly conserved residues in the RNP domains of any of the four RRMs (green link) conferred either temperature-sensitive growth or lethality to yeast cells.

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 <Structure load='2ghp' size='300' frame='true' align='right' caption='X-ray crystallographic structure of the first three RRMs of Prp24, shown here as the octameric protein observed in the crystal structure' scene='Sandbox_Reserved_340/2ghp/3'/>
-The key structural elements of Prp24 are the conserved RNA recognition motifs (RRMs).  These motifs are found in many proteins with RNA binding properties and contain conserved RNP elements that are recognizable by their primary sequence <ref name="Shannon"/>.  For several years, Prp24 was thought to contain three RRMs, termed RRM 1, RRM 2, and RRM 3 (green link)<ref name="Shannon"/>.  However, analysis of homologs of Prp24 from several different species allowed the identification of a fourth RRM in Prp24 of ''S. cerevisiae'', albeit one that was much less highly conserved and not easily recognizable by its RNP-consensus domain <ref name="Rader"/>.
+The key structural elements of Prp24 are the conserved RNA recognition motifs (RRMs).  These motifs are found in many proteins with RNA binding properties and contain conserved RNP elements that are recognizable by their primary sequence <ref name="Shannon"/>.  For several years, Prp24 was thought to contain three RRMs, termed RRM 1, RRM 2, and RRM 3 <ref name="Shannon"/>.  However, analysis of homologs of Prp24 from several different species allowed the identification of a fourth RRM in Prp24 of ''S. cerevisiae'', albeit one that was much less highly conserved and not easily recognizable by its RNP-consensus domain <ref name="Rader"/>.
 ===RNA Recognition Motifs===
-Prp24 contains four RRMs, RRM 1, RRM 2, RRM 3, and RRM 4.  These motifs have a canonical structure of a platform of four β-strands with two α-helices on one side of the β-sheet plane (green link).  These RRMs are present in many proteins that bind to to single stranded regions of RNA <ref name="RRM"/> and their presence in Prp24 supports a role for the annealing of U4 and U6 snRNAs into the U4/U6 structure.
+Prp24 contains four RRMs, RRM 1, RRM 2, RRM 3, and RRM 4.  These motifs have a <scene name='Sandbox_Reserved_340/2ghp/6'>canonical structure of a platform of four β-strands with two α-helices on one side of the β-sheet plane</scene>.  These RRMs are present in many proteins that bind to to single stranded regions of RNA <ref name="RRM"/> and their presence in Prp24 supports a role for the annealing of U4 and U6 snRNAs into the U4/U6 structure.
 Within each RRM, there are RNP consensus domains <ref name="RRM">PMID:15853797</ref>.  These are the regions in the β-strands that are thought to actually interact with the RNA <ref name="RRM"/>.  These regions seem to be very important in Prp24 and its interaction with U4 and U6.  The study that first identified a probable link between the Prp24 protein and U4/U6 found that mutations in RNP 1 and RNP 2 of the carboxy terminal RRM (green link) rescued a cold-sensitive phenotype caused by a U4 mutation in stem II of U4/U6 <ref name="Shannon"/>.  Two further studies <ref name="Vidaver"/> <ref name="Kwan">PMID:15811912</ref> showed that the mutation of three highly conserved residues in the RNP domains of any of the four RRMs (green link) conferred either temperature-sensitive growth or lethality to yeast cells.