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A Comparative Study of Proteolytic Mechanisms During Leaf Senescence of Four Genotypes of Winter Oilseed Rape Highlighted Relevant Physiological and Molecular Traits for NRE Improvement

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Journal Plants (Basel)
Date 2016 May 3
PMID 27135221
Citations 4
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Abstract

Winter oilseed rape is characterized by a low N use efficiency related to a weak leaf N remobilization efficiency (NRE) at vegetative stages. By investigating the natural genotypic variability of leaf NRE, our goal was to characterize the relevant physiological traits and the main protease classes associated with an efficient proteolysis and high leaf NRE in response to ample or restricted nitrate supply. The degradation rate of soluble proteins and D1 protein (a thylakoid-bound protein) were correlated to N remobilization, except for the genotype Samouraï which showed a low NRE despite high levels of proteolysis. Under restricted nitrate conditions, high levels of soluble protein degradation were associated with serine, cysteine and aspartic proteases at acidic pH. Low leaf NRE was related to a weak proteolysis of both soluble and thylakoid-bound proteins. The results obtained on the genotype Samouraï suggest that the timing between the onset of proteolysis and abscission could be a determinant. The specific involvement of acidic proteases suggests that autophagy and/or senescence-associated vacuoles are implicated in N remobilization under low N conditions. The data revealed that the rate of D1 degradation could be a relevant indicator of leaf NRE and might be used as a tool for plant breeding.

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References
1.
Noh Y, Amasino R . Identification of a promoter region responsible for the senescence-specific expression of SAG12. Plant Mol Biol. 1999; 41(2):181-94. DOI: 10.1023/a:1006342412688. View

2.
Tilsner J, Kassner N, Struck C, Lohaus G . Amino acid contents and transport in oilseed rape (Brassica napus L.) under different nitrogen conditions. Planta. 2004; 221(3):328-38. DOI: 10.1007/s00425-004-1446-8. View

3.
Huesgen P, Schuhmann H, Adamska I . Deg/HtrA proteases as components of a network for photosystem II quality control in chloroplasts and cyanobacteria. Res Microbiol. 2009; 160(9):726-32. DOI: 10.1016/j.resmic.2009.08.005. View

4.
Otegui M, Noh Y, Martinez D, Vila Petroff M, Staehelin L, Amasino R . Senescence-associated vacuoles with intense proteolytic activity develop in leaves of Arabidopsis and soybean. Plant J. 2005; 41(6):831-44. DOI: 10.1111/j.1365-313X.2005.02346.x. View

5.
Wagner R, Aigner H, Funk C . FtsH proteases located in the plant chloroplast. Physiol Plant. 2011; 145(1):203-14. DOI: 10.1111/j.1399-3054.2011.01548.x. View