| A semi-dominant allele, niv-525, acts in trans to inhibit expression of its wild-type homologue in Antirrhinum majus. | |
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MedLine Citation:
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PMID: 3402437 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Niv-525 is a semi-dominant allele of the nivea locus, which encodes the enzyme chalcone synthase required for flower pigment biosynthesis in Antirrhinum majus. Plants heterozygous for niv-525 and wild-type (Niv+) allele, have flowers with a reduced intensity and novel spatial pattern of pigmentation compared with Niv+ homozygotes. In heterozygotes, niv-525 acts in trans to reduce the steady-state level of nivea transcript produced by its Niv+ homologue and hence the quantity of chalcone synthase protein. Niv-525 carries an inverted duplication of 207 bp in its promoter region which has arisen following excision of the transposable element Tam 3. This structure can be explained by a model of plant transposable element excision that involves resolution of two hairpin DNA molecules. Possible mechanisms for the trans-acting effect of niv-525 and its relationship to other examples of allelic interactions, such as transvection in Drosophila melanogaster, are discussed. |
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Authors:
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E S Coen; R Carpenter |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: The EMBO journal Volume: 7 ISSN: 0261-4189 ISO Abbreviation: EMBO J. Publication Date: 1988 Apr |
Date Detail:
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Created Date: 1988-09-16 Completed Date: 1988-09-16 Revised Date: 2010-09-10 |
Medline Journal Info:
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Nlm Unique ID: 8208664 Medline TA: EMBO J Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 877-83 Citation Subset: IM |
Affiliation:
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AFRC, Institute of Plant Science Research, John Innes Institute, Norwich, UK. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Acyltransferases
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genetics Alleles* Base Sequence Gene Expression Regulation* Genes* Genes, Dominant* Molecular Sequence Data Nucleic Acid Conformation Plants / enzymology, genetics* Transcription, Genetic |
| Chemical | |
Reg. No./Substance:
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EC 2.3.-/Acyltransferases; EC 2.3.1.74/flavanone synthetase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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