Source:http://linkedlifedata.com/resource/pubmed/id/11673632
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2001-10-23
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pubmed:abstractText |
Lily MADS box gene 1 (LMADS1), with sequence homology to the AP3 family of genes, was cloned and characterized from lily (Lilium longiflorum). LMADS1 protein contains almost complete consensus sequence of the PISTILLATA (PI)-derived motif (YEFRVQPSQPNLH) found in the AP3 family of genes and paleoAP3 motif (YGSHDLRLA) found in the AP3 family of genes from the low eudicot, magnolid dicot and monocot species. LMADS1 mRNA was expressed in all four whorls of the flower and absent in the vegetative leaves. The LMADS1 protein was only detected in the petals and stamens, indicating that LMADS1 is possibly post-transcriptionally regulated in lily. Arabidopsis plants transformed with 35S::LMADS1 produced flowers with short petals and stamens, however, no floral organ conversion was observed. Ectopic expression of LMADS1 cDNA truncated with the MADS box domain in Arabidopsis generated the ap3-like dominant negative mutation in which the petals were converted into sepal-like structures and the stamens were converted into carpel-like structures. Yeast two-hybrid analysis indicated that LMADS1 truncated with the MADS box domain is able to sufficiently interact with the Arabidopsis PI protein. This result supports that LMADS1 is the functional counterpart of the AP3 gene in lily. Interestingly, in contrast to other B functional genes, LMADS1 truncated with the MADS box domain is able to strongly form homodimers. LMADS1 may represent an ancestral form of the B function gene, which retains the ability to form homodimers in regulating petal and stamen development in lily.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MADS Domain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PISTILLATA protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0032-0781
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1156-68
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11673632-Amino Acid Sequence,
pubmed-meshheading:11673632-Arabidopsis,
pubmed-meshheading:11673632-Arabidopsis Proteins,
pubmed-meshheading:11673632-Base Sequence,
pubmed-meshheading:11673632-DNA Primers,
pubmed-meshheading:11673632-Genes, Dominant,
pubmed-meshheading:11673632-Genes, Plant,
pubmed-meshheading:11673632-Homeodomain Proteins,
pubmed-meshheading:11673632-Lilium,
pubmed-meshheading:11673632-MADS Domain Proteins,
pubmed-meshheading:11673632-Microscopy, Electron, Scanning,
pubmed-meshheading:11673632-Molecular Sequence Data,
pubmed-meshheading:11673632-Mutation,
pubmed-meshheading:11673632-Phylogeny,
pubmed-meshheading:11673632-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11673632-Transcription Factors
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pubmed:year |
2001
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pubmed:articleTitle |
A MADS box gene from lily (Lilium Longiflorum) is sufficient to generate dominant negative mutation by interacting with PISTILLATA (PI) in Arabidopsis thaliana.
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pubmed:affiliation |
Graduate Institute of Agricultural Biotechnology, National Chung Hsing University, Taichung, Taiwan, 40227 R.O.C.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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