Phosphatase Family RTR1 - Revision history

Gerard at 21:04, 17 October 2016

2016-10-17T21:04:02Z

Gerard: /* Function */

2016-05-14T22:36:41Z

‎Function

Gerard at 22:22, 14 May 2016

2016-05-14T22:22:00Z

Mark: /* Function */

2015-04-03T21:41:21Z

‎Function

Mark: /* Function */

2015-04-02T19:07:56Z

‎Function

Gerard at 23:05, 24 March 2015

2015-03-24T23:05:11Z

Gerard at 00:13, 23 March 2015

2015-03-23T00:13:42Z

Mark at 16:59, 1 January 2015

2015-01-01T16:59:18Z

Mark at 16:58, 1 January 2015

2015-01-01T16:58:55Z

Mark at 16:56, 1 January 2015

2015-01-01T16:56:00Z

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 __NOTOC__
-[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_RTR1|Fold RTR1]]: [[Phosphatase_Superfamily_RTR1|Superfamily RTR1]]: [[Phosphatase_Family_RTR1|Family RTR1]]
+[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_RTR1|Fold RTR1]]: [[Phosphatase_Superfamily_RTR1|Superfamily RTR1]]
-RTR1 is a phosphatase conserved in eukaryotes that regulates phosphorylation of the  [[CTD_Phosphorylation| C-terminal domain (CTD) of RNA polymerase II]].
+RTR1 is a phosphatase conserved in eukaryotes that regulates the [[CTD_Phosphorylation|phosphorylation states of C-terminal domain (CTD) of RNA polymerase II]].
 === Evolution ===
-RTR1 is found in most eukaryotes. It is absent from the sponge genome, possibly due to incomplete genome assembly. It is single copy in most species including human (RPAP2). However, two copies are found in yeast (RTR1 and RTR2).
+RTR1 is found in most eukaryotes. It is absent from the sponge genome, though it is perhaps due to the quality of genome assembly. It is single copy in human, sea urchin, fruit fly, ''C elegans''. However, two copies are found in yeast (RTR1, RTR2).
-=== Domain ===
+=== Domain Structure===
-RTR1 proteins share a conserved catalytic domain. Yeast RTR1 has a C-terminal region that auto-inhibits the catalytic domain <cite>hsu14</cite>. Human RPAP2 has a far longer tail of unknown function, though it is well conserved in most animals, and weakly conserved in plants. Nematode and Drosophila members lack this extended tail.
+RTR1 has a conserved phosphatase domain with a unique mechanism of action <cite>Irani</cite>. Yeast RTR1 has a C-terminal region (CTR) that auto-inhibits the catalytic domain <cite>hsu14</cite>. The human homolog, RPAP2, has a longer tail with limited sequence similarity to CTR, and is known to bind RNA pol II subunit Rpb6 and to be involved in pre-mRNA 3'-end formation <cite>Wani</cite>.
 === Function ===
-RTR1 was shown to dephosphorylate serine-5 of CTD repeats of RNA pol II in yeast <cite>Mosley09 kim09</cite>, and human <cite>Egloff12</cite>. A study in ''K. lactis'' <cite>xiang12</cite> that challenged these findings was since criticized for using possibly inactive protein <cite>hsu14</cite>.
+Yeast RTR1 dephosphorylates serine-5 of CTD repeats of RNA pol II <cite>Mosley09 kim09</cite>. These findings were challenged by later studies <cite>xiang12</cite>, but more recent study supports its activity towards serine-5 <cite>hsu14</cite> and also the anti-termination tyrosine-1 on CTD repeats <cite>hsu14</cite>.
 === References ===
 <biblio>
 #Mosley09 pmid=19394294
 #Kim09 pmid=19679665
 #xiang12 pmid=22781759
 #hsu14 pmid=24951832
 </biblio>

@@ Line 11: / Line 11: @@
 === Function ===
-Yeast RTR1 was shown to dephosphorylate serine-5 of CTD repeats of RNA pol II <cite>Mosley09 kim09</cite>, and similar activity was reported for human RPAP2 <cite>Egloff12</cite>. These findings were challenged by a later study of RTR1 from K. lactis <cite>xiang12</cite>. But, more recent reports supports RTR1 dephosphorylates serine-5 as well as the newly described anti-termination tyrosine 1 residue of CTD repeats, and the lack of phosphatase activity shown in <cite>xiang12</cite> is due to  the absence of an identifiable step in the purification protocol, - the step removing inhibitory metal -, which resulted in an inactive protein <cite>hsu14</cite>.
+RTR1 was shown to dephosphorylate serine-5 of CTD repeats of RNA pol II in yeast <cite>Mosley09 kim09</cite>, and human <cite>Egloff12</cite>. A study in ''K. lactis'' <cite>xiang12</cite> that challenged these findings was since criticized for using possibly inactive protein <cite>hsu14</cite>.
 === References ===

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_RTR1|Fold RTR1]]: [[Phosphatase_Superfamily_RTR1|Superfamily RTR1]]: [[Phosphatase_Family_RTR1|Family RTR1]]
-RTR1 is a phosphatase conserved in eukaryotes that regulates the [[CTD_Phosphorylation|phosphorylation state of C-terminal domain (CTD) of RNA polymerase II]].
+RTR1 is a phosphatase conserved in eukaryotes that regulates phosphorylation of the  [[CTD_Phosphorylation| C-terminal domain (CTD) of RNA polymerase II]].
 === Evolution ===

@@ Line 11: / Line 11: @@
 === Function ===
-Yeast RTR1 was shown to dephosphorylate serine-5 of CTD repeats of RNA pol II <cite>Mosley09 kim09</cite>, and similar activity was reported for human RPAP2 <cite>Egloff12</cite>. These findings were challenged by a later study of RTR1 from K. lactis <cite>xiang12</cite>. But, more recent reports supports RTR1 dephosphorylates serine-5 as well as the newly described anti-termination tyrosine 1 residue of CTD repeats, and the lack of phosphatase activity shown in <cite>xiang12</cite> is due to  the absence of an identifiable step in the purification protocol which resulted in an inactive protein <cite>hsu14</cite>.
+Yeast RTR1 was shown to dephosphorylate serine-5 of CTD repeats of RNA pol II <cite>Mosley09 kim09</cite>, and similar activity was reported for human RPAP2 <cite>Egloff12</cite>. These findings were challenged by a later study of RTR1 from K. lactis <cite>xiang12</cite>. But, more recent reports supports RTR1 dephosphorylates serine-5 as well as the newly described anti-termination tyrosine 1 residue of CTD repeats, and the lack of phosphatase activity shown in <cite>xiang12</cite> is due to  the absence of an identifiable step in the purification protocol, - the step removing inhibitory metal -, which resulted in an inactive protein <cite>hsu14</cite>.
 === References ===

@@ Line 11: / Line 11: @@
 === Function ===
-Yeast RTR1 was shown to dephosphorylate serine-5 of CTD repeats of RNA pol II <cite>Mosley09 kim09</cite>, and similar activity was reported for human RPAP2 <cite>Egloff12</cite>. These findings were challenged by a later study <cite>xiang12</cite> of RTR1 from K. lactis, but more recent reports supports its activity towards serine-5 <cite>hsu14</cite>, as well as the newly described anti-termination tyrosine 1 residue of CTD repeats <cite>hsu14</cite>.
+Yeast RTR1 was shown to dephosphorylate serine-5 of CTD repeats of RNA pol II <cite>Mosley09 kim09</cite>, and similar activity was reported for human RPAP2 <cite>Egloff12</cite>. These findings were challenged by a later study of RTR1 from K. lactis <cite>xiang12</cite>. But, more recent reports supports RTR1 dephosphorylates serine-5 as well as the newly described anti-termination tyrosine 1 residue of CTD repeats, and the lack of phosphatase activity shown in <cite>xiang12</cite> is due to  the absence of an identifiable step in the purification protocol which resulted in an inactive protein <cite>hsu14</cite>.
 === References ===

@@ Line 5: / Line 5: @@
 === Evolution ===
-RTR1 is found in most of eukaryotes. It is absent from Monosiga and sponge genome, though it is perhaps due to the quality of genome assembly. It is single copy in human, sea urchin, fruit fly, ''C elegans''. However, two copies are found in yeast.
+RTR1 is found in most eukaryotes. It is absent from the sponge genome, possibly due to incomplete genome assembly. It is single copy in most species including human (RPAP2). However, two copies are found in yeast (RTR1 and RTR2).
 === Domain ===
-RTR1 has a conserved domain that carries out the phosphatase activity. Yeast RTR1 has a C-terminal region (CTR) that auto-inhibits the catalytic domain <cite>hsu14</cite>. Human RTR1 encoded by gene RPAP2 has a longer tail, but whether its function is unclear given the limited sequence similarity with CTR in yeast RTR1.
+RTR1 proteins share a conserved catalytic domain. Yeast RTR1 has a C-terminal region that auto-inhibits the catalytic domain <cite>hsu14</cite>. Human RPAP2 has a far longer tail of unknown function.
 === Function ===
-Yeast RTR1 encodes the phosphatase that dephosphorylates serine-5 of CTD repeats of RNA pol II <cite>Mosley09 kim09</cite>. These findings were challenged by later studies <cite>xiang12</cite>, but more recent study supports its activity towards serine-5 <cite>hsu14</cite>. Moreover, it has been shown that Rtr1 dephosphorylates not only serine-5 but also the newly described anti-termination tyrosine 1 marker on CTD repeats <cite>hsu14</cite>.
+Yeast RTR1 was shown to dephosphorylate serine-5 of CTD repeats of RNA pol II <cite>Mosley09 kim09</cite>. These findings were challenged by later studies <cite>xiang12</cite>, but more recent study supports its activity towards serine-5 <cite>hsu14</cite>, which also indicates that RTR1 also dephosphorylates  the newly described anti-termination tyrosine 1 residue of CTD repeats <cite>hsu14</cite>.
 === References ===