Prp8: Difference between revisions

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==Prp8 Background==

Prp8's name originates from the discovery that it is intricately involved with ''[[p]]''re-m ''[[R]]''NA ''[[p]]''rocessing within Eukaryotic organisms, and extensive research on the protein has revealed it is indispensable for the catalytic activity of the spliceosome earning it the nickname of 'Master Regulator of the Spliceosome' <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. UV crosslinking experiments have shown that Prp8 has contact with the 5' splice site, 3' splice site, [http://en.wikipedia.org/wiki/Polypyrimidine_tract polypyrimidine tract], and branch point of pre-mRNA transcripts, as well as associating with all five of the snRNAs and their associated proteins <ref name='Functional interactions of prp8 with both splice sites at the spliceosome catalytic center'>PMID:10444596</ref>. Thus, Prp8 is the only protein to date involved with [http://en.wikipedia.org/wiki/RNA_splicing pre-mRNA splicing] that actually contacts all catalytic elements of the spliceosome, indicating that it indeed has a very crucial role in pre-mRNA splicing catalysis, and resides in the catalytic heart of the splicing complex. Two other unique properties of Prp8 are its size and evolutionary conservation. Prp8 is the largest of all the spliceosomal proteins at approximately 250 kDa and is 2317 - 2416 amino acid residues in length (depending on the orthologue) <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. In all organisms in which Prp8 has been identified Prp8, it is always been found as a U5 snRNP component and is highly conserved across species, with >60% identity between fungi, mammals, and plants <ref name='Prp8, the pivotal protein of the spliceosomal catalytic center, evolved from a retroelement-encoded reverse transcriptase'>PMID:21441348 </ref>. Although Prp8 is highly conserved between species, its origin is shrouded in mystery because it contains no sequence homology to ''one'' family of proteins, but instead exhibits structural properties and domains from a range of conserved protein families while adding a twist to each that is Prp8 specific <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. Even though Prp8 has been under extensive investigation for over a decade, its specific molecular mechanisms and functions are still unknown, but in light of all the information available, a hypothesis on Prp8's function can be postulated; Prp8 definitely acts as a large scaffold to coordinate the spliceosome's activity because the protein interacts with every part of the complex, however it is unclear whether Prp8 plays a direct role in splicing catalysis or only acts as a guide allowing for correct orientation and dynamic movements <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>.

'''Prp8's''' name originates from the discovery that it is intricately involved with ''[[p]]''re-m ''[[R]]''NA ''[[p]]''rocessing within Eukaryotic organisms, and extensive research on the protein has revealed it is indispensable for the catalytic activity of the spliceosome earning it the nickname of 'Master Regulator of the Spliceosome' <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. UV crosslinking experiments have shown that Prp8 has contact with the 5' splice site, 3' splice site, [http://en.wikipedia.org/wiki/Polypyrimidine_tract polypyrimidine tract], and branch point of pre-mRNA transcripts, as well as associating with all five of the snRNAs and their associated proteins <ref name='Functional interactions of prp8 with both splice sites at the spliceosome catalytic center'>PMID:10444596</ref>. Thus, Prp8 is the only protein to date involved with [http://en.wikipedia.org/wiki/RNA_splicing pre-mRNA splicing] that actually contacts all catalytic elements of the spliceosome, indicating that it indeed has a very crucial role in pre-mRNA splicing catalysis, and resides in the catalytic heart of the splicing complex. Two other unique properties of Prp8 are its size and evolutionary conservation. Prp8 is the largest of all the spliceosomal proteins at approximately 250 kDa and is 2317 - 2416 amino acid residues in length (depending on the orthologue) <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. In all organisms in which Prp8 has been identified Prp8, it is always been found as a U5 snRNP component and is highly conserved across species, with >60% identity between fungi, mammals, and plants <ref name='Prp8, the pivotal protein of the spliceosomal catalytic center, evolved from a retroelement-encoded reverse transcriptase'>PMID:21441348 </ref>. Although Prp8 is highly conserved between species, its origin is shrouded in mystery because it contains no sequence homology to ''one'' family of proteins, but instead exhibits structural properties and domains from a range of conserved protein families while adding a twist to each that is Prp8 specific <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. Even though Prp8 has been under extensive investigation for over a decade, its specific molecular mechanisms and functions are still unknown, but in light of all the information available, a hypothesis on Prp8's function can be postulated; Prp8 definitely acts as a large scaffold to coordinate the spliceosome's activity because the protein interacts with every part of the complex, however it is unclear whether Prp8 plays a direct role in splicing catalysis or only acts as a guide allowing for correct orientation and dynamic movements <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>.

==Pre-mRNA Splicing==

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 ==Prp8 Background==
-Prp8's name originates from the discovery that it is intricately involved with ''[[p]]''re-m ''[[R]]''NA ''[[p]]''rocessing  within Eukaryotic organisms, and extensive research on the protein has revealed it is indispensable for the catalytic activity of the spliceosome earning it the nickname of 'Master Regulator of the Spliceosome' <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. UV crosslinking experiments have shown that Prp8 has contact with the 5' splice site, 3' splice site, [http://en.wikipedia.org/wiki/Polypyrimidine_tract polypyrimidine tract], and branch point of pre-mRNA transcripts, as well as associating with all five of the snRNAs and their associated proteins <ref name='Functional interactions of prp8 with both splice sites at the spliceosome catalytic center'>PMID:10444596</ref>. Thus, Prp8 is the only protein to date involved with [http://en.wikipedia.org/wiki/RNA_splicing pre-mRNA splicing] that actually contacts all catalytic elements of the spliceosome, indicating that it indeed has a very crucial role in pre-mRNA splicing catalysis, and resides in the catalytic heart of the splicing complex. Two other unique properties of Prp8 are its size and evolutionary conservation. Prp8 is the largest of all the spliceosomal proteins at approximately 250 kDa and is 2317 - 2416 amino acid residues in length (depending on the orthologue) <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. In all organisms in which Prp8 has been identified Prp8, it is always been found as a U5 snRNP component and is highly conserved across species, with >60% identity between fungi, mammals, and plants <ref name='Prp8, the pivotal protein of the spliceosomal catalytic center, evolved from a retroelement-encoded reverse transcriptase'>PMID:21441348 </ref>. Although Prp8 is highly conserved between species, its origin is shrouded in mystery because it contains no sequence homology to ''one'' family of proteins, but instead exhibits structural properties and domains from a range of conserved protein families while adding a twist to each that is Prp8 specific <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. Even though Prp8 has been under extensive investigation for over a decade, its specific molecular mechanisms and functions are still unknown, but in light of all the information available, a hypothesis on Prp8's function can be postulated; Prp8 definitely acts as a large scaffold to coordinate the spliceosome's activity because the protein interacts with every part of the complex, however it is unclear whether Prp8 plays a direct role in splicing catalysis or only acts as a guide allowing for correct orientation and dynamic movements <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>.
+'''Prp8's''' name originates from the discovery that it is intricately involved with ''[[p]]''re-m ''[[R]]''NA ''[[p]]''rocessing  within Eukaryotic organisms, and extensive research on the protein has revealed it is indispensable for the catalytic activity of the spliceosome earning it the nickname of 'Master Regulator of the Spliceosome' <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. UV crosslinking experiments have shown that Prp8 has contact with the 5' splice site, 3' splice site, [http://en.wikipedia.org/wiki/Polypyrimidine_tract polypyrimidine tract], and branch point of pre-mRNA transcripts, as well as associating with all five of the snRNAs and their associated proteins <ref name='Functional interactions of prp8 with both splice sites at the spliceosome catalytic center'>PMID:10444596</ref>. Thus, Prp8 is the only protein to date involved with [http://en.wikipedia.org/wiki/RNA_splicing pre-mRNA splicing] that actually contacts all catalytic elements of the spliceosome, indicating that it indeed has a very crucial role in pre-mRNA splicing catalysis, and resides in the catalytic heart of the splicing complex. Two other unique properties of Prp8 are its size and evolutionary conservation. Prp8 is the largest of all the spliceosomal proteins at approximately 250 kDa and is 2317 - 2416 amino acid residues in length (depending on the orthologue) <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. In all organisms in which Prp8 has been identified Prp8, it is always been found as a U5 snRNP component and is highly conserved across species, with >60% identity between fungi, mammals, and plants <ref name='Prp8, the pivotal protein of the spliceosomal catalytic center, evolved from a retroelement-encoded reverse transcriptase'>PMID:21441348 </ref>. Although Prp8 is highly conserved between species, its origin is shrouded in mystery because it contains no sequence homology to ''one'' family of proteins, but instead exhibits structural properties and domains from a range of conserved protein families while adding a twist to each that is Prp8 specific <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>. Even though Prp8 has been under extensive investigation for over a decade, its specific molecular mechanisms and functions are still unknown, but in light of all the information available, a hypothesis on Prp8's function can be postulated; Prp8 definitely acts as a large scaffold to coordinate the spliceosome's activity because the protein interacts with every part of the complex, however it is unclear whether Prp8 plays a direct role in splicing catalysis or only acts as a guide allowing for correct orientation and dynamic movements <ref name='Prp8: At the heart of the spliceosome'>DOI:10.1261/rna.2220705</ref>.
 ==Pre-mRNA Splicing==