Ssu72 Abstract: Difference between revisions

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Based on similarity with human Ssu72, the Ssu72 RNA polymerase II CTD phosphatase homolog from Drosophila Melanogaster was inferred to have a tyrosine and serine phosphatase function. It was suggested that the aspartate loop is involved in allowing Ssu72 to phosphorylate serine as well as tyrosine. Sequence and structure comparisons confirmed the similarity between Ssu72 proteins and the tyrosine phosphatases, particularly at the catalytic site. Differences between the two families were also examined, and the nature of the aspartate loop was found to be the most likely to have an effect on function. However, further experimental research is needed to confirm that the Drosophila Ssu72 homolog protein does function as a serine phosphatase.
Based on similarity with human Ssu72, the Ssu72 RNA polymerase II CTD phosphatase homolog from Drosophila Melanogaster was inferred to have a tyrosine and serine phosphatase function. It was suggested that the aspartate loop is involved in allowing Ssu72 to dephosphorylate serine as well as tyrosine. Sequence and structure comparisons confirmed the similarity between Ssu72 proteins and the tyrosine phosphatases, particularly at the catalytic site. Differences between the two families were also examined, and the nature of the aspartate loop was found to be the most likely to have an effect on function. However, further experimental research is needed to confirm that the Drosophila Ssu72 homolog protein does function as a serine phosphatase.


[[Ssu72 Abstract | Abstract]] |
[[Ssu72 Abstract | Abstract]] |

Latest revision as of 01:42, 16 June 2009

Based on similarity with human Ssu72, the Ssu72 RNA polymerase II CTD phosphatase homolog from Drosophila Melanogaster was inferred to have a tyrosine and serine phosphatase function. It was suggested that the aspartate loop is involved in allowing Ssu72 to dephosphorylate serine as well as tyrosine. Sequence and structure comparisons confirmed the similarity between Ssu72 proteins and the tyrosine phosphatases, particularly at the catalytic site. Differences between the two families were also examined, and the nature of the aspartate loop was found to be the most likely to have an effect on function. However, further experimental research is needed to confirm that the Drosophila Ssu72 homolog protein does function as a serine phosphatase.

Abstract | Introduction | Results | Discussion | Method | References