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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Facchini, P. J. Chappell, J. |
| Description | Author Affiliation: Facchini PJ ( Agronomy Department, University of Kentucky, Lexington 40546-0091.); |
| Abstract | The initial step in the conversion of the isoprenoid intermediate farnesyl diphosphate to the sesquiterpenoid phytoalexin capsidiol in elicitor-treated tobacco tissues is catalyzed by an inducible sesquiterpene cyclase [5-epi-aristolochene synthase (EAS)]. Two independent cDNA clones (cEAS1 and cEAS2) encoding EAS were isolated from an elicitor-induced tobacco cDNA library by differential hybridization and subsequently were characterized by hybrid selection--in vitro translation. Insertion of cEAS1, a partial cDNA clone encoding 175 C-terminal amino acids, into an Escherichia coli expression vector resulted in accumulation of a fusion protein immunodetectable with EAS-specific polyclonal antibodies. The cDNA clones were used to isolate two full-length EAS genes that mapped 5 kilobases (kb) apart on one 15-kb genomic clone. The nucleotide sequences of the structural gene components were identical from 388 base pairs (bp) upstream of the transcription initiation site to 40 bp downstream of the translation termination codon, suggesting a relatively recent duplication event. The genes consist of 1479-bp open reading frames, each containing five introns and specifying 56,828-Da proteins. The N-terminal amino acid sequence deduced from the genomic clones was identical to the first 16 amino acids of the EAS protein identifiable by Edman degradation. RNA blot hybridization with cEAS1 demonstrated a mRNA induction time course consistent with the induction of the EAS mRNA translational activity with maximum levels 4-6 h after elicitation. EAS mRNA was not detected in control cells. DNA blot-hybridization analysis of genomic DNA revealed a copy number of approximately 12-15 for EAS-like genes in the tetraploid tobacco genome. The conservation of a putative allelic prenyl diphosphate binding motif is also discussed. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 22 |
| Volume Number | 89 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1992-12-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Alkyl And Aryl Transferases Cellulase Pharmacology Genes, Plant Multigene Family Plants, Toxic Tobacco Enzymology Genetics Transferases Amino Acid Sequence Cloning, Molecular Codon DNA Isolation & Purification Enzyme Induction Introns Molecular Sequence Data Oligodeoxyribonucleotides Polymerase Chain Reaction RNA, Messenger Biosynthesis Sequence Homology, Amino Acid TATA Box Drug Effects Transcription, Genetic Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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