Abstract
We have isolated cDNA clones from a human placental library that code for a low molecular weight GTP-binding protein originally designated Gp (also called G25K). This identification is based on comparisons with the available peptide sequences for the purified human Gp protein and the use of two highly specific anti-peptide antibodies. The predicted amino acid sequence of the protein is very similar to those of various members of the ras superfamily of low molecular weight GTP-binding proteins, including the N-, Ki-, and Ha-ras proteins (30-35% identical), the rho proteins (approximately 50% identical), and the rac proteins (approximately 70% identical). The highest degree of sequence identity (80%) is found with the Saccharomyces cerevisiae cell-division-cycle protein CDC42. The human placental gene, which we designate CDC42Hs, complements the cdc42-1 mutation in S. cerevisiae, which suggests that this GTP-binding protein is the human homolog of the yeast protein.
MeSH Terms
Amino Acid Sequence
Base Sequence
Cell Cycle
Cell Division
Cloning, Molecular
Escherichia coli/genetics
Fungal Proteins/genetics
GTP-Binding Proteins/genetics,metabolism
Genes
Genetic Complementation Test
Guanosine 5'-O-(3-Thiotriphosphate)/metabolism
Humans
Kinetics
Molecular Sequence Data
Mutation
Placenta/metabolism
Pregnancy Proteins/genetics
Restriction Mapping
Saccharomyces cerevisiae/cytology,genetics
Sequence Homology, Nucleic Acid
cdc42 GTP-Binding Protein
cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
Chemicals
Fungal Proteins
Pregnancy Proteins
Guanosine 5'-O-(3-Thiotriphosphate)
GTP-Binding Proteins
cdc42 GTP-Binding Protein
cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Shinjo K
Department of Pharmacology, Cornell University, Ithaca, NY 14850.
Koland J G
Hart M J
Narasimhan V
Johnson D I
Evans T
Cerione R A
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