Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1995-3-23
pubmed:databankReference
pubmed:abstractText
Two novel tandemly-oriented open reading frames (ORFs) with homology to alcohol dehydrogenase (ADH) were isolated from tomato. The predicted amino acid composition for each of the two tandem adh genes indicates the presence of 22 and 21, respectively, of 22 amino acids conserved in ADH proteins from plants and animals. However, comparison to known plant adh genes reveals a significantly lower similarity indicating that they belong to a novel class of ADHs. According to mapping data, the adh-homologous ORFs do not represent either of the previously studied adh1 or adh2 genes of tomato. The tandem genes, termed adh3a and adh3b, mapped to a distal region of the long arm of chromosome 4, unlike adh1, which maps closer to the centromere. Adh3a and adh3b have over 90% similarity to each other at the nucleotide and putative peptide levels. The adh3a gene has ten exons and nine introns with the transcription initiation site 57 bp upstream of the translation start. A putative TATA box and polyadenylation site have been identified. Adh3a is transcribed and, according to cDNA sequence analysis, fully processed in the late stages of anther development. According to transformation analysis, tissue-specific regulatory elements reside within the -448 to +724 region. The termination codon of adh3a is separated from the putative adh3b translation start site by 789 bp of intervening sequence. The 5' untranscribed sequences of each gene contain a stretch of 68 bp with 78% similarity. Within this stretch are sequences which are homologous to sequences found in anaerobically-induced or pollen-expressed genes from various plant species.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0167-4412
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:geneSymbol
adh3a, adh3b
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1875-91
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:7858224-Alcohol Dehydrogenase, pubmed-meshheading:7858224-Amino Acid Sequence, pubmed-meshheading:7858224-Base Sequence, pubmed-meshheading:7858224-Chromosome Mapping, pubmed-meshheading:7858224-Crosses, Genetic, pubmed-meshheading:7858224-DNA, Complementary, pubmed-meshheading:7858224-Genes, Reporter, pubmed-meshheading:7858224-Lycopersicon esculentum, pubmed-meshheading:7858224-Molecular Sequence Data, pubmed-meshheading:7858224-Phylogeny, pubmed-meshheading:7858224-Plant Proteins, pubmed-meshheading:7858224-Plants, Genetically Modified, pubmed-meshheading:7858224-Plasmids, pubmed-meshheading:7858224-Promoter Regions, Genetic, pubmed-meshheading:7858224-RNA, Plant, pubmed-meshheading:7858224-Regeneration, pubmed-meshheading:7858224-Sequence Analysis, DNA, pubmed-meshheading:7858224-Sequence Homology, Amino Acid, pubmed-meshheading:7858224-Sequence Homology, Nucleic Acid, pubmed-meshheading:7858224-Species Specificity, pubmed-meshheading:7858224-Tissue Distribution, pubmed-meshheading:7858224-Transformation, Genetic
pubmed:year
1994
pubmed:articleTitle
A novel anther-expressed adh-homologous gene in Lycopersicon esculentum.
pubmed:affiliation
Department of Plant Breeding, Cornell University, Ithaca, NY 14853.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't