Difference between revisions of "Phosphatase Family RTR1"

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__NOTOC__
 
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_RTR1|Fold RTR1]]: [[Phosphatase_Superfamily_RTR1|Superfamily RTR1]]: [[Phosphatase_Family_RTR1|Family RTR1]]
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_RTR1|Fold RTR1]]: [[Phosphatase_Superfamily_RTR1|Superfamily RTR1]]
  
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RTR1 is a phosphatase conserved in eukaryotes that regulates the [[CTD_Phosphorylation|phosphorylation state of C-terminal domain (CTD) of RNA polymerase II]].  
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RTR1 is a phosphatase conserved in eukaryotes that regulates the [[CTD_Phosphorylation|phosphorylation states of C-terminal domain (CTD) of RNA polymerase II]].  
  
 
=== Evolution ===
 
=== Evolution ===
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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).
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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).
  
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=== Domain ===
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=== Domain Structure===
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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.
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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 ===
 
=== Function ===
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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>.
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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 ===
 
=== References ===
 
<biblio>
 
<biblio>
 
#Mosley09 pmid=19394294
 
#Mosley09 pmid=19394294
 +
#Wani pmid= 25639305
 +
#Irani pmid=26933063
 
#Kim09 pmid=19679665
 
#Kim09 pmid=19679665
 
#xiang12 pmid=22781759
 
#xiang12 pmid=22781759
 
#hsu14 pmid=24951832
 
#hsu14 pmid=24951832
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#Egloff12 pmid=22137580
 
 
</biblio>
 
</biblio>

Latest revision as of 21:04, 17 October 2016

Phosphatase Classification: Fold RTR1: Superfamily RTR1

RTR1 is a phosphatase conserved in eukaryotes that regulates the 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, 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 Structure

RTR1 has a conserved phosphatase domain with a unique mechanism of action [1]. Yeast RTR1 has a C-terminal region (CTR) that auto-inhibits the catalytic domain [2]. 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 [3].

Function

Yeast RTR1 dephosphorylates serine-5 of CTD repeats of RNA pol II [4, 5]. These findings were challenged by later studies [6], but more recent study supports its activity towards serine-5 [2] and also the anti-termination tyrosine-1 on CTD repeats [2].

References

  1. Irani S, Yogesha SD, Mayfield J, Zhang M, Zhang Y, Matthews WL, Nie G, Prescott NA, and Zhang YJ. Structure of Saccharomyces cerevisiae Rtr1 reveals an active site for an atypical phosphatase. Sci Signal. 2016 Mar 1;9(417):ra24. DOI:10.1126/scisignal.aad4805 | PubMed ID:26933063 | HubMed [Irani]
  2. Hsu PL, Yang F, Smith-Kinnaman W, Yang W, Song JE, Mosley AL, and Varani G. Rtr1 is a dual specificity phosphatase that dephosphorylates Tyr1 and Ser5 on the RNA polymerase II CTD. J Mol Biol. 2014 Aug 12;426(16):2970-81. DOI:10.1016/j.jmb.2014.06.010 | PubMed ID:24951832 | HubMed [hsu14]
  3. pmid= 25639305 [Wani]
  4. Mosley AL, Pattenden SG, Carey M, Venkatesh S, Gilmore JM, Florens L, Workman JL, and Washburn MP. Rtr1 is a CTD phosphatase that regulates RNA polymerase II during the transition from serine 5 to serine 2 phosphorylation. Mol Cell. 2009 Apr 24;34(2):168-78. DOI:10.1016/j.molcel.2009.02.025 | PubMed ID:19394294 | HubMed [Mosley09]
  5. Xiang K, Manley JL, and Tong L. The yeast regulator of transcription protein Rtr1 lacks an active site and phosphatase activity. Nat Commun. 2012 Jul 10;3:946. DOI:10.1038/ncomms1947 | PubMed ID:22781759 | HubMed [xiang12]
  6. Kim M, Suh H, Cho EJ, and Buratowski S. Phosphorylation of the yeast Rpb1 C-terminal domain at serines 2, 5, and 7. J Biol Chem. 2009 Sep 25;284(39):26421-6. DOI:10.1074/jbc.M109.028993 | PubMed ID:19679665 | HubMed [Kim09]
All Medline abstracts: PubMed | HubMed
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