Structure of bovine adrenal dopamine beta-monooxygenase, as deduced from cDNA and protein sequencing: evidence that the membrane-bound form of the enzyme is anchored by an uncleaved signal peptide.
A full-length cDNA for dopamine beta-monooxygenase (D beta M) from bovine adrenal glands has been cloned and sequenced. The soluble and membrane-derived forms of D beta M have also been sequenced from their N-termini. While the observed sequences for the soluble protein correspond to those previously reported [Joh, T.H., & Hwang, O. (1986) Ann. N.Y. Acad. Sci. 493, 343-350], the heavy subunit of membrane-derived enzyme is found to contain a unique N-terminus. Alignment of this N-terminus with that deduced from cDNA cloning indicates identity at 22 (and possibly 26) out of 27 residues. This comparison leads us to conclude that the membranous form of bovine D beta M retains an uncleaved N-terminal signal peptide as the source of membrane anchoring.
Taljanidisz
J
J
Department of Chemistry, University of California, Berkeley 94720.
Stewart
L
L
Smith
A J
AJ
Klinman
J P
JP
D000311:Adrenal Glands / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D004299:Dopamine beta-Hydroxylase / Q000235:genetics*; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D015394:Molecular Structure; D021382:Protein Sorting Signals
D008565:Membrane Proteins; D021382:Protein Sorting Signals; D004247:DNA; D004299:Dopamine beta-Hydroxylase