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Carbon and nitrogen remobilization during seed filling in Arabidopsis is strongly impaired in the pyrroline-5-carboxylate dehydrogenase mutant.
- Source :
-
Journal of Experimental Botany . 3/13/2023, Vol. 74 Issue 5, p1489-1500. 12p. - Publication Year :
- 2023
-
Abstract
- Proline is an amino acid that is degraded in the mitochondria by the sequential action of proline dehydrogenase (ProDH) and pyrroline-5-carboxylate dehydrogenase (P5CDH) to form glutamate. We investigated the phenotypes of Arabidopsis wild-type plants, the knockout prodh1 prodh2 double-mutant, and knockout p5cdh allelic mutants grown at low and high nitrate supplies. Surprisingly, only p5cdh presented lower seed yield and produced lighter seeds. Analyses of elements in above-ground organs revealed lower C concentrations in the p5cdh seeds. Determination of C, N, and dry matter partitioning among the above-ground organs revealed a major defect in stem-to-seed resource allocations in this mutant. Again surprisingly, defects in C, N, and biomass allocation to seeds dramatically increased in high-N conditions. 15N-labelling consistently confirmed the defect in N remobilization from the rosette and stem to seeds in p5cdh. Consequently, the p5cdh mutants produced morphologically abnormal, C-depleted seeds that displayed very low germination rates. The most striking result was the strong amplification of the N-remobilization defects in p5cdh under high nitrate supply, and interestingly this phenotype was not observed in the prodh1 prodh 2 double-mutant irrespective of nitrate supply. This study reveals an essential role of P5CDH in carbon and nitrogen remobilization for reserve accumulation during seed development in Arabidopsis. [ABSTRACT FROM AUTHOR]
- Subjects :
- *SEED development
*SEED yield
*SUPPLY & demand
*NITROGEN
*AMINO acids
*GERMINATION
Subjects
Details
- Language :
- English
- ISSN :
- 00220957
- Volume :
- 74
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Journal of Experimental Botany
- Publication Type :
- Academic Journal
- Accession number :
- 162393988
- Full Text :
- https://doi.org/10.1093/jxb/erac499