Molecular cloning of a rho family gene of Entamoeba histolytica.
An Entamoeba histolytica gene (Eh rho1) was cloned that encodes a putative low-molecular-mass GTP-binding protein, most similar to the ras homologue rho. The Eh rho1 open reading frame was 208 amino acids long and encoded a 23-kDa protein similar to Saccharomyces cerevisiae RHO1-RHO4 and CDC42 and human rhoA, rac1, and G25K gene products. This similarity was greatest at the NH2 terminus of Eh rho1 where two GTP-binding sites and a possible effector site were conserved. A cysteine residue at the COOH terminus of Eh rho1 was followed by eight hydrophobic amino acids rather than the three hydrophobic amino acids present in other ras family proteins.
Lohia
A
A
Department of Tropical Public Health, Harvard School of Public Health, Boston, MA 02115.
Samuelson
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004748:Entamoeba histolytica / Q000235:genetics*; D005656:Fungal Proteins / Q000235:genetics*; D019204:GTP-Binding Proteins / Q000235:genetics*; D017125:Genes, Protozoan / Q000235:genetics*; D011905:Genes, ras / Q000235:genetics; D008969:Molecular Sequence Data; D005810:Multigene Family / Q000235:genetics; D016366:Open Reading Frames; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D020741:rho GTP-Binding Proteins
D005656:Fungal Proteins; D019204:GTP-Binding Proteins; D020741:rho GTP-Binding Proteins