Identification and characterization of a FYVE domain from the early diverging eukaryote Giardia lamblia.
Curr Microbiol
; 62(4): 1179-84, 2011 Apr.
Article
em En
| MEDLINE
| ID: mdl-21165741
ABSTRACT
The morphology of the endomembrane system of Giardia lamblia appears to be significantly different from higher eukaryotes. Therefore, the molecular mechanisms controlling vesicular trafficking are also likely to be altered. Since FYVE domain is a known regulator of endosomal trafficking, the authors used BLAST search to identify FYVE domain(s) in G. lamblia. A 990 amino acid long putative FYVE domain-containing ORF was identified, which contains all the conserved sequence elements in the ligand binding pocket. Phylogenetic analysis reveals that this domain is significantly diverged. The authors have shown that the corresponding gene is expressed in G. lamblia trophozoites and cysts. In spite of this phylogenetic divergence, in vitro biochemical assay indicates that this domain preferentially binds to phosphatidylinositol 3-phosphate {PtdIns(3)P}and in vivo expression of the GFP-tagged G. lamblia FYVE domain in S. cerevisiae, displays its selective localization to PtdIns(3)P-enriched endosomes. This is the first study to characterize a PtdIns(3)P effector protein in this early-diverged eukaryote.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Giardia lamblia
/
Evolução Molecular
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Revista:
Curr Microbiol
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Índia