, Volume 174, Issue 4, pp 488–494 | Cite as

Rapid variations in the content of the RNA of the small subunit of ribulose-1,5-bisphosphate carboxylase of mature tobacco leaves in response to localized changes in light quantity. Relationships between the activity and quantity of the enzyme

  • Jean-Louis Prioul
  • Agnès Reyss


Mature green leaves from tobacco (Nicotiana tabacum L.) plants were submitted to contrasting light conditions; half of each leaf was shaded (changed from 60 to 25 μmol photons· m-2 ·s-1=LL) and the other half was exposed to higher light (changed from 60 to 360 μmol·m-2· s-1=HL) for 24 h. The activity and quantity of ribulose-1,5-bisphosphate carboxylase (RuBPCase) were measured during the first 24 h in each leaf region and the variation was compared with that of small subunit (SSU)-and large subunit (LSU)-mRNA contents determined by a hybridot technique. Each leaf half responded separately to the actual light received. The activity of RuBPCase increased progressively in the HL zones and decreased in the LL zones. The RuBPCase-protein content was not significantly modified during the first 24 h but SSU-mRNA content responded very rapidly to the treatment. Within 2 h a significant difference in SSU mRNA appeared between LL and HL zones: at the end of the photoperiod the content in LL zones was approx. 25% of the initial value. The increase in the exposed zone, however, was not significant, indicating that there was a dissymmetry of the response to variation in incident white light. The LSU-mRNA contents from the same leaf extracts were totally unaffected by the light treatment. No day-night variations were noted in either SSU or LSU mRNAs in control plants.

Key words

Light and mRNA levels Nicotiana (light, mRNA) Ribulose-1,5-bisphosphate carboxylase (large and small subunit mRNA) 



high-light irradiance


lower-ligh irradiance


large subunit of RuBPCase


ribulose-1,5-bisphosphate carboxylase


small subunit of RuBPCase


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Copyright information

© Springer-Verlag 1988

Authors and Affiliations

  • Jean-Louis Prioul
    • 1
  • Agnès Reyss
    • 1
  1. 1.Structure et Métabolisme des Plantes, associé au CNRS (UA 1128), Bât. 430Université Paris-SudOrsay CédexFrance

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