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Nucleic Acids Research, 1985, Vol. 13, No. 5 1493-1504
© 1985

Articles

Nucleic acid (cDNA) and amino acid sequences of the maize endosperm protein glutelin-2

Salomé Prat, Jordi Cortadas, Pere Puigdomènech and Jaume Palau

Institut de Biología de Barcelona, Unitat de Biofísica i Biología Molecular, Jorge Girona Salgado 18–26, 08034 Barcelona, Spain

Received December 31, 1984. Revised February 12, 1985. Accepted February 12, 1985.

The cDNA coding for a glutelin-2 protein from maize endosperm has been cloned and the complete amino acid sequence of the protein derived for the first time. An immature maize endosperm cDNA bank was screened for the expression of a ß-lactamase:glutelin-2 (G2) fusion polypeptide by using antibodies against the purified 28 kd G2 protein. A clone corresponding to the 28 kd G2 protein was sequenced and the primary structure of this protein was derived. Five regions can be defined in the protein sequence: an 11 residue N-terminal part, a repeated region formed by eight units of the sequence Pro-Pro-Pro-Val-His-Leu, an alternating Pro-X stretch 21 residues long, a Cys rich domain and a C-terminal part rich in Gln. The protein sequence is preceded by 19 resídues which have the characteristics of the signal peptide found in secreted proteins. Unlike zeins, the main maize storage proteins, 28 kd glutelin-2 has several homologous sequences in common with other cereal storage proteins.


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