Glycobiology Advance Access originally published online on October 23, 2008
Glycobiology 2009 19(4):331-336; doi:10.1093/glycob/cwn107
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Communication |
Molecular characterization of nucleocytosolic O-GlcNAc transferases of Giardia lamblia and Cryptosporidium parvum
3 Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, MA 02118, USA
1 To whom correspondence should be addressed: Tel: +1-617-414-1054; e-mail: jsamuels{at}bu.edu
Received on August 7, 2008; revised on September 16, 2008; accepted on October 6, 2008
O-Linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of a single GlcNAc to the Ser or Thr of nucleocytoplasmic proteins. OGT activity, which may compete with that of kinases, is involved in signaling in animals and plants, and abnormalities in OGT activities have been associated with type 2 diabetes. Here, we show that ogt genes that predict enzymes with characteristic tetratricopeptide repeats and a spindly domain are present in some protists (Giardia, Cryptosporidium, Toxoplasma, and Dictyostelium) but are absent from the majority of protists examined (e.g., Plasmodium, Trypanosoma, Entamoeba, and Trichomonas). Similarly, ogt genes are present in some fungi but are absent from numerous other fungi, suggesting that secondary loss is an important contributor to the evolution of ogt genes. Nucleocytosolic extracts of Giardia and Cryptosporidium show OGT activity, and recombinant Giardia and Cryptosporidium OGTs are active in yeast and bacteria, respectively. These results suggest the possibility that O-GlcNAc modification of nucleocytosolic proteins also has function(s) in simple eukaryotes.
Key words: Cryptosporidium / evolution / Giardia / O-GlcNAc transferase / recombinant expression
2 Present address: Life Sciences Division, AU-KBC Research Centre, MIT Campus, Chromepet, Chennai 600044, Tamilnadu, India.
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