Molecular cloning and characterization of an isoprenylated 67 kDa protein

• Published in: Biochimica et biophysica acta Vol. 1217; no. 3; pp. 257 - 265
• Main Authors: Asundi, Vinod K., Stahl, Richard C., Showalter, LoriJo, Conner, Kimberly J., Carey, David J.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 06.04.1994; Elsevier
• Subjects: 67 kDa protein; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Base Sequence; Biological and medical sciences; Carrier Proteins - genetics; cDNA sequence; Cloning, Molecular; DNA, Complementary - isolation & purification; Fundamental and applied biological sciences. Psychology; Gene expression; GTP-Binding Proteins - genetics; Isoprenylation; Miscellaneous; Molecular Sequence Data; Protein Prenylation; Proteins; Rats; Rats, Sprague-Dawley; Schwann Cells - metabolism; Sequence Homology, Amino Acid; cDNA sequence; HSPG; 67 kDa protein; VSMC; Gene expression; Isoprenylation; PI-PLC; PCR; Rat; Nucleotide sequence; Rodentia; Isoprenoid; Posttranslational modification; Proteins; Tissue; Vertebrata; Mammalia; Complementary DNA; Aminoacid sequence; Structural analysis
• ISSN: 0167-4781; 0006-3002; 1879-2634
• DOI: 10.1016/0167-4781(94)90284-4

The cDNA coding for a 67 kDa protein (p67) was isolated from a rat Schwann cell library. A recombinant form of p67 expressed in bacteria was used to produce polyclonal anti-p67 antibodies. By immunoblot analysis p67 was found to be expressed in most tissues and cell lines examined. Inspection of the deduced amino acid sequence revealed a COOH-terminal consensus sequence for isoprenylation. Consistent with this finding, p67 was a substrate for isoprenylation in vitro by geranylgeranylpyrophosphate. p67 was associated predominantly with the particulate fraction of rat smooth muscle cells. The rat p67 sequence was highly homologous to a family of recently described human and mouse λ-interferon inducible, guanine nucleotide binding proteins.