Molecular cloning and sequence of a novel ommochrome-binding protein cDNA from an insect, Manduca sexta

• Published in: The Journal of biological chemistry 1993-02, Vol.268 (4), p.2337-2340
• Main Authors: Yepiz-Plascencia, G.M, Ho, C, Martel, R.R, Law, J.H
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; ARN MENSAJERO; ARN MESSAGER; Base Sequence; Binding and carrier proteins; Biological and medical sciences; Carrier Proteins - genetics; cDNA; Cloning, Molecular; DNA - genetics; EXPRESION GENICA; EXPRESSION DES GENES; Fundamental and applied biological sciences. Psychology; Gene Expression; genes; Genes, Insect; Hemolymph - chemistry; Insect Hormones - genetics; Insect Proteins; MANDUCA SEXTA; Molecular Sequence Data; Moths - genetics; nucleotide sequence; ommochrome-binding protein; Phenothiazines - metabolism; PIGMENT; PIGMENTOS; predictions; PROTEINAS; PROTEINE; Proteins; Restriction Mapping; RNA, Messenger - genetics; SECUENCIA NUCLEICA; SEQUENCE NUCLEIQUE
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)53780-7

An ommochrome-binding protein (OBP) from the hemolymph of Manduca sexta has recently been purified and characterized. A cDNA clone was isolated from a fifth instar larval cDNA expression library utilizing antiserum against OBP. Northern blot analysis of total fat body RNA detected a transcript of approximately 1.2 kilobases in fifth instar wandering larvae RNA. The complete nucleotide sequence of the 905-base pair cDNA insert was determined by the dideoxy chain termination method. The OBP cDNA encodes a polypeptide of 274 residues with a predicted molecular weight of 30,580 and with one consensus N-linked glycosylation site. Comparison of the NH2-terminal sequence of the mature protein and the cDNA sequence revealed a typical signal peptide of 18 amino acids. In wandering stage larvae, the OBP transcript appeared to be at least 250-fold less abundant than ribosomal RNA