Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 331-336 |
| Number of pages | 6 |
| Journal | Glycobiology |
| Volume | 19 |
| Issue number | 4 |
| DOIs | |
| State | Published - Mar 20 2009 |
| Externally published | Yes |
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Keywords
- Cryptosporidium
- Evolution
- Giardia
- O-GlcNAc transferase
- Recombinant expression
ASJC Scopus subject areas
- Biochemistry
Cite this
Molecular characterization of nucleocytosolic O-GlcNAc transferases of Giardia lamblia and Cryptosporidium parvum. / Banerjee, Sulagna; Robbins, Phillips W.; Samuelson, John.
In: Glycobiology, Vol. 19, No. 4, 20.03.2009, p. 331-336.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molecular characterization of nucleocytosolic O-GlcNAc transferases of Giardia lamblia and Cryptosporidium parvum
AU - Banerjee, Sulagna
AU - Robbins, Phillips W.
AU - Samuelson, John
PY - 2009/3/20
Y1 - 2009/3/20
N2 - 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.
AB - 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.
KW - Cryptosporidium
KW - Evolution
KW - Giardia
KW - O-GlcNAc transferase
KW - Recombinant expression
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UR - http://www.scopus.com/inward/citedby.url?scp=62349091636&partnerID=8YFLogxK
U2 - 10.1093/glycob/cwn107
DO - 10.1093/glycob/cwn107
M3 - Article
C2 - 18948359
AN - SCOPUS:62349091636
VL - 19
SP - 331
EP - 336
JO - Glycobiology
JF - Glycobiology
SN - 0959-6658
IS - 4
ER -