ArticleMolecular biology reports2011
Isolation and characterization of three duplicated PISTILLATA genes in Brassica napus.
Article in Molecular biology reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Molecular characterization of oilseed rape accessions collected from multi continents for exploitation of potential heterotic group through SSR markers.Molecular biology reports · 2012Article
- Isolation and characterization of a novel BcMF14 gene from Brassica campestris ssp. chinensis.Molecular biology reports · 2011Article
- Isolation and characterization of gene encoding G protein α subunit protein responsive to plant hormones and abiotic stresses in Brassica napus.Molecular biology reports · 2010Article
- Molecular analysis and expression of a floral organ-specific polygalacturonase gene isolated from rapeseed (Brassica napus L.).Molecular biology reports · 2010Article
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6 authors.
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Abstract
Three coding region cDNAs of duplicated PISTILLATA-like (PI-like) MADS-box genes, BnPI-1, BnPI-2 and BnPI-3, were isolated from B. napus by RT-PCR. The sequence analysis showed that the three PI cDNAs possessed 627, 627 and 625 nucleotides, respectively, and their nucleotide sequences had 96.49-98.72% similarity. Due to a deletion of two nucleotides, the protein sequence in the downstream of the frameshift site was altered in BnPI-3. Therefore, there were only 171 amino acids coded by BnPI-3, while there were 208 ones coded by BnPI-1 or BnPI-2. The deduced amino acid identity between BnPI-1 and BnPI-2 was 97.6% and the amino acid sequence of BnPI-1 and BnPI-2 shared 72.6% identity with BnPI-3. The deduced amino acid sequences of the coded proteins indicated high homology with the members of the PI family of MADS-box proteins. RT-PCR analysis showed that BnPI transcription was only detectable in petals and stamens. The yeast two-hybrid assays results showed that the three BnPI proteins exhibited different dimerization affinities with three BnAP3. BnPI-1 and BnPI-2 could form strong heterodimers with BnAP3. The dimerization affinity of BnPI-1 with BnAP3-4 is the strongest in all the combinations, while the affinity of BnPI-3 with BnAP3-4 is the weakest. The dimerization affinity to BnAP3-4 of BnPI-1 is 3.5 times of that of BnPI-3. The distinguished weak interaction to AP3 of BnPI-3 is probably due to the loss of the PI motif. The divergences of sequence and affinity of protein interaction might reflect some functional divergence of the three PI genes in B. napus.
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