ISSN:
1617-4623
Keywords:
Key words Differential display
;
Heterosis
;
RNA-binding protein
;
Wheat
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract A hybrid-specific expressed cDNA fragment, designated as AG5, has been identified in wheat seedling leaves using differential mRNA display. AG5 contains an open reading frame (ORF) encoding 183 amino acid residues. Comparison with amino acid sequences in GenBank revealed that the AG5 protein is homologous to a group of Gly-rich proteins with consensus sequence-type RNA-binding domains (CS-RBD). Structural analysis showed that AG5 protein contains five motifs, including a consensus sequence-type RNA-binding domain near its N-terminus, arginine/aspartic acid repeats and a Gly-rich region in its center, a Cys-X2-Cys-X4-His-X4-Cys (CCHC) zinc finger motif in the Gly-rich region, and TrySer2ArgAsp2Arg repeats towards its C-terminus. Of all previously described RNA-binding proteins, only RZ-1 from tobacco has a similar structure to the AG5 protein, but RZ-1 lacks a TrySer2ArgAsp2Arg repeat motif, indicating that the two proteins may belong to a family of closely related proteins in plants. The possible role of AG5 and its relation to wheat heterosis are discussed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/PL00008693
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