Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming) gene from the amitochondriate protist, Giardia lamblia.
A Giardia lamblia gene, Glacs, was cloned, sequenced and expressed in Escheria Coli. This gene codes for a 726 residue long acetyl-CoA synthetase (ADP-forming). This enzyme is responsible for the formation of acetate, a metabolic endproduct of G. lamblia. It is known from only two Type I amitochondriate eukaryotes, G. lamblia and Entamoeba histolytica and from the archaebacterium, Pyrococcus furiosus. With Glacs as query, homologous unidentified open reading frames were detected in the complete genomes of only a few archaebacteria and eubacteria. These form a new protein family present in all three domains of life, which probably plays a central role in the acyl-CoA metabolism but is of restricted taxonomic distribution.
Sánchez
L B
LB
The Rockefeller University, New York, NY 10021, USA. sanchel@rockvax.rockfeller.edu
Morrison
H G
HG
Sogin
M L
ML
Müller
M
M
D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D003001:Cloning, Molecular; D003066:Coenzyme A Ligases / Q000235:genetics*; D017931:DNA Primers; D016829:Giardia lamblia / Q000201:enzymology / Q000235:genetics*; D016366:Open Reading Frames
D017931:DNA Primers; D003066:Coenzyme A Ligases; C101958:acetate-CoA ligase (ADP-forming)