Giardia intestinalis Glucosamine 6-Phosphate Isomerase: the Key Enzyme to Encystment Appears to be Controlled by Ubiquitin Attachment

The cyst wall of the parasitic protozoan, Giardia intestinalis, is composed of a polymer of N-acetylgalactosamine, the precursor of which is synthesized by an inducible enzyme pathway. The first enzyme in this pathway, glucosamine 6-phosphate isomerase, is transcriptionally regulated. During encystm...

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Bibliographic Details
Published in:The Journal of eukaryotic microbiology 2002-03, Vol.49 (2), p.134-136
Main Authors: LOPEZ, ALEX B, HOSSAIN, MOHAMMED T, VAN KEULEN, HARRY
Format: Article
Language:English
Subjects:
Aldose-Ketose Isomerases - genetics
Aldose-Ketose Isomerases - metabolism
Animals
Biological and medical sciences
Cell Differentiation
Cloning, Molecular
Competition inhibition
cyst wall
DNA, Protozoan
encystment
Enzyme Induction
excystation
Fundamental and applied biological sciences. Psychology
fusion protein
Gene Expression Regulation
Genes, Protozoan
Giardia lamblia - enzymology
Giardia lamblia - genetics
Giardia lamblia - metabolism
glutathione transferase
Life cycle. Host-agent relationship. Pathogenesis
Protozoa
Recombinant Proteins - metabolism
ubiquitin
Ubiquitin - metabolism
ubiquitination
Western blot
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Summary:The cyst wall of the parasitic protozoan, Giardia intestinalis, is composed of a polymer of N-acetylgalactosamine, the precursor of which is synthesized by an inducible enzyme pathway. The first enzyme in this pathway, glucosamine 6-phosphate isomerase, is transcriptionally regulated. During encystment and in mature cysts this isomerase appears to be modified by ubiquitin attachment. Thus, it might be targeted for destruction by an ubiquitin-mediated pathway, suggesting that glucosamine 6-phosphate isomerase expression is tightly regulated.
ISSN:1066-5234
1550-7408
DOI:10.1111/j.1550-7408.2002.tb00356.x