A substitution mutation in OsCCD7 cosegregates with dwarf and increased tillering phenotype in rice |
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Authors: | KRISHNANAND P KULKARNI CHANDRAPAL VISHWAKARMA SARADA P SAHOO JOHN M LIMA MANOJ NATH PRASAD DOKKU RAJESH N GACCHE TRILOCHAN MOHAPATRA S ROBIN N SARLA M SESHASHAYEE ASHOK K SINGH KULDEEP SINGH NAGENDRA K SINGH R P SHARMA |
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Institution: | 1. National Research Centre on Plant Biotechnology, LBS Centre, Indian Agricultural Research Institute, Pusa Campus, New Delhi, 110 012, India 2. School of Life Sciences, Swami Ramanand Teerth Marathwada University, Nanded, 431 606, India 3. Central Rice Research Institute, Cuttack, 753 006, India 4. Tamilnadu Agricultural University, Coimbatore, 641 003, India 5. Directorate of Rice Research, Rajendranagar, Hyderabad, 500 030, India 6. University of Agricultural Sciences, GKVK, Bangalore, 560 065, India 7. Indian Agricultural Research Institute, Pusa Campus, New Delhi, 110 012, India 8. Punjab Agricultural University, Ludhiana, 141 027, India
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Abstract: | Dwarf plant height and tillering ability are two of the most important agronomic traits that determine the plant architecture, and have profound influence on grain yield in rice. To understand the molecular mechanism controlling these two traits, an EMS-induced recessive dwarf and increased tillering1 (dit1) mutant was characterized. The mutant showed proportionate reduction in each internode as compared to wild type revealing that it belonged to the category of dn-type of dwarf mutants. Besides, exogenous application of GA3 and 24-epibrassinolide, did not have any effect on the phenotype of the mutant. The gene was mapped on the long arm of chromosome 4, identified through positional candidate approach and verified by cosegregation analysis. It was found to encode carotenoid cleavage dioxygenase7 (CCD7) and identified as an allele of htd1. The mutant carried substitution of two nucleotides CC to AA in the sixth exon of the gene that resulted in substitution of serine by a stop codon in the mutant, and thus formation of a truncated protein, unlike amino acid substitution event in htd1. The new allele will facilitate further functional characterization of this gene, which may lead to unfolding of newer signalling pathways involving plant development and architecture. |
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