Abstract
cDNA clones were isolated from tissue specific cDNA libraries of barley and maize using as a probe the cDNA of the maize gene C1, a regulator of anthocyanin gene expression. C1-related homology for all of the four cDNAs characterized by sequence analysis is restricted to the N-terminal 120 amino acids of the putative proteins. This region shows striking homology to the N-proximal domain of the myb oncoproteins from vertebrates and invertebrates. Within the myb proto-oncogene family this part of the respective gene products functions as a DNA binding domain. Acidic domains are present in the C-proximal protein segments. Conservation of these sequences, together with the genetically defined regulator function of the C1 gene product, suggest that myb-related plant genes code for trans-acting factors which regulate gene expression in a given biosynthetic pathway. © 1989 Springer-Verlag.
Lingua originale | English |
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pagine (da-a) | 183-187 |
Numero di pagine | 5 |
Rivista | Molecular and General Genetics |
Volume | 216 |
DOI | |
Stato di pubblicazione | Pubblicato - 1989 |
Keywords
- Amino Acid Sequence
- Cloning, Molecular
- DNA
- DNA-Binding Proteins
- Hordeum
- Molecular Sequence Data
- Plant Proteins
- Plant genes
- Plants
- Proto-Oncogene Proteins
- Proto-Oncogene Proteins c-myb
- Zea mays
- myb proto-oncogene homoloy