Molecular analysis of the ADH1-Cm allele of maize.
The Adh1-Cm allele and each gene in the Adh1-FCm duplication have been cloned and restriction-mapped. Of the Cm allele 6 kb was sequenced. A single amino acid substitution of aspartate for tyrosine at residue 52 accounts for the altered enzymatic properties of the Cm protein. Comparison of the nucleotide sequence to that of Adh1-1F and Adh1-1S shows structural and restriction site polymorphisms in the 3' flanking DNA. Cm lacks the insertion sequence present in 1F and 1S and contains a complex sequence composed of two direct repeats and an inverted repeat. The two genes of the duplication allele have similar restriction maps to Cm and each other.
Osterman
J C
JC
School of Biological Sciences, University of Nebraska-Lincoln 68588.
Dennis
E S
ES
D000426:Alcohol Dehydrogenase / Q000235:genetics*; D000483:Alleles; D001483:Base Sequence; D004247:DNA / Q000235:genetics; D004251:DNA Transposable Elements; D007438:Introns; D008969:Molecular Sequence Data; D005810:Multigene Family; D010944:Plants / Q000201:enzymology / Q000235:genetics*; D012150:Polymorphism, Restriction Fragment Length; D012091:Repetitive Sequences, Nucleic Acid; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D003313:Zea mays / Q000201:enzymology / Q000235:genetics
D004251:DNA Transposable Elements; D004247:DNA; D000426:Alcohol Dehydrogenase