title: Expression and myristoylation of NAP-22 using a baculovirus transfer vector system.
abstract: NAP-22 is a brain enriched acidic protein localized in the membrane fraction. The peptide sequence of NAP-22 elucidated from the cDNA sequencing, however, showed that NAP-22 is a very hydrophilic protein having no transmembrane regions. The peptide sequence analysis also showed that NAP-22 has a consensus sequence of N-myristoylation and the presence of polybasic domain in its N-terminal region. These sites could be the anchoring sites to localize to the membrane. In this study, we showed the myristoylation of NAP-22 using a Baculovirus expression system and also showed a liposome binding ability of the expressed protein in Escherichia coli.
authors.affiliation: Graduate School, Division of Science, University of Tokyo, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Maekawa
authors.forename: Y
authors.initials: Y
authors.lastname: Matsuura
authors.forename: S
authors.initials: S
authors.lastname: Nakamura
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D016367:Baculoviridae / Q000235:genetics*; D002148:Calmodulin-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D005814:Genes, Viral; D005822:Genetic Vectors; D008081:Liposomes; D008969:Molecular Sequence Data; D009036:Moths; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000235:genetics* / Q000378:metabolism; D011499:Protein Processing, Post-Translational
chemical_list: D002148:Calmodulin-Binding Proteins; D008081:Liposomes; D009227:Myristic Acids; D009419:Nerve Tissue Proteins; D019814:Myristic Acid