Maize polyamine oxidase: primary structure from protein and cDNA sequencing

FEBS Letters

Rea, Giuseppina²  Schininà, M.Eugenia¹  Tavladoraki, Paraskevi²  Mariottini, Paolo²  Angelini, Riccardo²  Federico, Rodolfo²  Manera, Francesco¹  Di Agostino, Silvia²  Cecconi, Francesco² 

[1] Dipartimento di Scienze Biochimiche `A. Rossi Fanelli' and Centro di Biologia Molecolare del Consiglio Nazionale delle Ricerche, Università `La Sapienza', Piazzale Aldo Moro 5, 00185 Rome, Italy;Dipartimento di Biologia, Università `Roma Tre', Viale Guglielmo Marconi 446, 00146 Rome, Italy

关键词: Flavin oxidase;    Hydrogen peroxide;    Polyamine oxidase;    Primary structure;    Zea mays L.;    dNTP;    deoxynucleoside triphosphate;    MAO;    monoamine oxidase;    MPAO;    maize polyamine oxidase;    RACE;    rapid amplification of cDNA ends;    RT-PCR;    reverse transcription-polymerase chain reaction;    SDS-PAGE;    sodium dodecylsulfate polyacrylamide gel electrophoresis;    UTR;    untranslated region;   

DOI  :  10.1016/S0014-5793(98)00311-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The first complete amino acid sequence of a flavin-containing polyamine oxidase was solved by a combined approach of nucleotide and peptide sequence analysis. A cDNA of 1737 bp, isolated from maize seedlings by reverse transcription-polymerase chain reaction and rapid amplification of cDNA ends strategies, was cloned and its sequence determined. This cDNA contains information for a polypeptide chain of 500 amino acids. Its amino-terminal sequence shows the typical features of secretion signal peptides. The primary structure of the mature protein was independently confirmed by extensive amino acid sequencing. Structural relationships with flavin-containing monoamine oxidases are also discussed.

【 授权许可】

Unknown