Difference between revisions of "Phosphatase Family SSU72"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC2|Superfamily CC2]]: [[Phosphatase_Family_SSU72|Family SSU72]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC2|Superfamily CC2]]: [[Phosphatase_Family_SSU72|Family SSU72]] | ||
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| + | SSU72 is a nearly pan-eukaryotic phosphatase of the RNA polymerase C-terminal domain. | ||
===Evolution=== | ===Evolution=== | ||
| − | + | SSU72 is found in most eukaryotes, but is lost in most excavates and some chromalveolates. It is usually present in one copy, but humans also have 8 SSU72 retrogenes of unknown function. | |
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| + | ===Domain Architecture=== | ||
| + | SSU72 consist of just a phosphatase domain, with no N- or C-terminal extensions. | ||
===Function=== | ===Function=== | ||
Latest revision as of 18:20, 12 November 2016
Phosphatase Classification: Superfamily CC2: Family SSU72
SSU72 is a nearly pan-eukaryotic phosphatase of the RNA polymerase C-terminal domain.
Evolution
SSU72 is found in most eukaryotes, but is lost in most excavates and some chromalveolates. It is usually present in one copy, but humans also have 8 SSU72 retrogenes of unknown function.
Domain Architecture
SSU72 consist of just a phosphatase domain, with no N- or C-terminal extensions.
Function
The phosphatase activity of Ssu72 is important for Pol II transcription and termination and for gene looping. It catalyzes CTD Serine-5 dephosphorylation in association with the Pta1 component of the CPF complex. In yeast, Ssu72 is required for pre-mRNA 3’-end cleavage, but so far no evidence exists implicating mammalian Ssu72 in that processing [1] [2].
Reference
- Krishnamurthy S, He X, Reyes-Reyes M, Moore C, and Hampsey M. Ssu72 Is an RNA polymerase II CTD phosphatase. Mol Cell. 2004 May 7;14(3):387-94. DOI:10.1016/s1097-2765(04)00235-7 |
- Xiang K, Nagaike T, Xiang S, Kilic T, Beh MM, Manley JL, and Tong L. Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex. Nature. 2010 Oct 7;467(7316):729-33. DOI:10.1038/nature09391 |
