Sandbox reserved 981: Difference between revisions

Line 12:

The Prp8 protein has multiple domains: the RNaseH-like, Jab1/MPN, Aar2, and a large domain further divided into a type II endonuclease and large polymerase-like domains<ref name="Galej5" />. Most of these domains received their names because of significant sequence similarities with domains of other proteins.

The type II endonuclease domain <scene name='69/699898/Endonuclease_domain/4'>(residues 1650-1810)</scene> is made up of 5 β-sheets surrounded by 3 α-helices that interact with the polymerase domain through a small linker domain<ref name="Galej2013">Galej, Wojciech P., Andrew J. Newman, Chris Oubridge, and Kiyoshi Nagai. "Crystal Structure of Prp8 Reveals Active Site Cavity of the Spliceosome." Nature 493.7434 (2013): 638-643. Academic Search Complete. Web. 13 Apr. 2015.</ref>. The large polymerase domain <scene name='69/699898/Polymerase_domain/1'>(residues 885-1375)</scene> is subdivided into ~~the~~ palm, finger, thumb ~~and endonuclease~~ domains<ref name="Galej2013">Galej, Wojciech P., Andrew J. Newman, Chris Oubridge, and Kiyoshi Nagai. "Crystal Structure of Prp8 Reveals Active Site Cavity of the Spliceosome." Nature 493.7434 (2013): 638-643. Academic Search Complete. Web. 13 Apr. 2015.</ref>. The palm domain <scene name='69/699898/Reverse_transcriptase_domain/1'>(residues 1048-1182)</scene> is similar in sequence to that of bacterial reverse transcriptase, so it is often referred to as the reverse transcriptase domain<ref name="Galej2013" />. The thumb domain <scene name='69/699898/Thumb_domain/1'>(residues 1257-1375)</scene>, is characterized by an antiparallel β-sheet and three helix bundles<ref name="Galej2013" />.

The type II endonuclease domain <scene name='69/699898/Endonuclease_domain/4'>(residues 1650-1810)</scene> is made up of 5 β-sheets surrounded by 3 α-helices that interact with the polymerase domain through a small linker domain<ref name="Galej2013">Galej, Wojciech P., Andrew J. Newman, Chris Oubridge, and Kiyoshi Nagai. "Crystal Structure of Prp8 Reveals Active Site Cavity of the Spliceosome." Nature 493.7434 (2013): 638-643. Academic Search Complete. Web. 13 Apr. 2015.</ref>. The large polymerase domain <scene name='69/699898/Polymerase_domain/1'>(residues 885-1375)</scene> is subdivided into palm, finger, and thumb domains<ref name="Galej2013">Galej, Wojciech P., Andrew J. Newman, Chris Oubridge, and Kiyoshi Nagai. "Crystal Structure of Prp8 Reveals Active Site Cavity of the Spliceosome." Nature 493.7434 (2013): 638-643. Academic Search Complete. Web. 13 Apr. 2015.</ref>. The palm domain <scene name='69/699898/Reverse_transcriptase_domain/1'>(residues 1048-1182)</scene> is similar in sequence to that of bacterial reverse transcriptase, so it is often referred to as the reverse transcriptase domain<ref name="Galej2013" />. The thumb domain <scene name='69/699898/Thumb_domain/1'>(residues 1257-1375)</scene>, is characterized by an antiparallel β-sheet and three helix bundles<ref name="Galej2013" />.

The RNaseH-like <scene name='69/699898/Rnaseh-like_domain/1'>(1840-2090)</scene> and Jab1/MPN <scene name='69/699898/Jab1-mnp/1'>(2150-2396)</scene> domains are connected by disordered linkers, and stabilized by Aar2, a U5 snRNP assembly factor<ref name="Galej5" />. The C-terminal tail of Aar domain reaches out from its main body in order to interact with the junction between RNaseH and Jab1/MPN. Through this contact Aar2 binds together a β-barrel of Jab1/MPN and β-hairpin from RNaseH domain using a parallel β-sheet. Also, through the Aar2 domain, RNaseH and Jab1/MPN domains are able to interact with the large polymerase domain<ref name="Galej2013" />. Once the Prp8 protein is imported into the nucleus the Aar domain is replaced by a Brr2 domain, an integral U5 snRNP component that is responsible for unwinding the U4/U6 snRNP duplex. This exchange may alter the position of the domains with respect to each other <ref name="Galej2013" />. The active site of Prp8 has been mapped to the RNaseH-like and Large domains. Mutations to this region have revealed <scene name='69/699898/Active_site/1'>splice site repressor points</scene><ref name="Galej2013" />.

Sandbox reserved 981: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 12: / Line 12: @@
 The Prp8 protein has multiple domains: the RNaseH-like, Jab1/MPN, Aar2, and a large domain further divided into a type II endonuclease and large polymerase-like domains<ref name="Galej5" />. Most of these domains received their names because of significant sequence similarities with domains of other proteins.
 <Structure load='4I43' size='300' color='white' frame='true' align='right' caption='Prp8:Aar2 Complex' />
-The type II endonuclease domain <scene name='69/699898/Endonuclease_domain/4'>(residues 1650-1810)</scene> is made up of 5 β-sheets surrounded by 3 α-helices that interact with the polymerase domain through a small linker domain<ref name="Galej2013">Galej, Wojciech P., Andrew J. Newman, Chris Oubridge, and Kiyoshi Nagai. "Crystal Structure of Prp8 Reveals Active Site Cavity of the Spliceosome." Nature 493.7434 (2013): 638-643. Academic Search Complete. Web. 13 Apr. 2015.</ref>. The large polymerase domain <scene name='69/699898/Polymerase_domain/1'>(residues 885-1375)</scene> is subdivided into the palm, finger, thumb and endonuclease domains<ref name="Galej2013">Galej, Wojciech P., Andrew J. Newman, Chris Oubridge, and Kiyoshi Nagai. "Crystal Structure of Prp8 Reveals Active Site Cavity of the Spliceosome." Nature 493.7434 (2013): 638-643. Academic Search Complete. Web. 13 Apr. 2015.</ref>. The palm domain <scene name='69/699898/Reverse_transcriptase_domain/1'>(residues 1048-1182)</scene> is similar in sequence to that of bacterial reverse transcriptase, so it is often referred to as the reverse transcriptase domain<ref name="Galej2013" />. The thumb domain <scene name='69/699898/Thumb_domain/1'>(residues 1257-1375)</scene>, is characterized by an antiparallel β-sheet and three helix bundles<ref name="Galej2013" />.
+The type II endonuclease domain <scene name='69/699898/Endonuclease_domain/4'>(residues 1650-1810)</scene> is made up of 5 β-sheets surrounded by 3 α-helices that interact with the polymerase domain through a small linker domain<ref name="Galej2013">Galej, Wojciech P., Andrew J. Newman, Chris Oubridge, and Kiyoshi Nagai. "Crystal Structure of Prp8 Reveals Active Site Cavity of the Spliceosome." Nature 493.7434 (2013): 638-643. Academic Search Complete. Web. 13 Apr. 2015.</ref>. The large polymerase domain <scene name='69/699898/Polymerase_domain/1'>(residues 885-1375)</scene> is subdivided into palm, finger, and thumb domains<ref name="Galej2013">Galej, Wojciech P., Andrew J. Newman, Chris Oubridge, and Kiyoshi Nagai. "Crystal Structure of Prp8 Reveals Active Site Cavity of the Spliceosome." Nature 493.7434 (2013): 638-643. Academic Search Complete. Web. 13 Apr. 2015.</ref>. The palm domain <scene name='69/699898/Reverse_transcriptase_domain/1'>(residues 1048-1182)</scene> is similar in sequence to that of bacterial reverse transcriptase, so it is often referred to as the reverse transcriptase domain<ref name="Galej2013" />. The thumb domain <scene name='69/699898/Thumb_domain/1'>(residues 1257-1375)</scene>, is characterized by an antiparallel β-sheet and three helix bundles<ref name="Galej2013" />.
 The RNaseH-like <scene name='69/699898/Rnaseh-like_domain/1'>(1840-2090)</scene> and Jab1/MPN <scene name='69/699898/Jab1-mnp/1'>(2150-2396)</scene> domains are connected by disordered linkers, and stabilized by Aar2, a U5 snRNP assembly factor<ref name="Galej5" />. The C-terminal tail of Aar domain reaches out from its main body in order to interact with the junction between RNaseH and Jab1/MPN. Through this contact Aar2 binds together a β-barrel of Jab1/MPN and β-hairpin from RNaseH domain using a parallel β-sheet. Also, through the Aar2 domain, RNaseH and Jab1/MPN domains are able to interact with the large polymerase domain<ref name="Galej2013" />. Once the Prp8 protein is imported into the nucleus the Aar domain is replaced by a Brr2 domain, an integral U5 snRNP component that is responsible for unwinding the U4/U6 snRNP duplex. This exchange may alter the position of the domains with respect to each other <ref name="Galej2013" />. The active site of Prp8 has been mapped to the RNaseH-like and Large domains. Mutations to this region have revealed <scene name='69/699898/Active_site/1'>splice site repressor points</scene><ref name="Galej2013" />.