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Published on April 29, 2009; 10.1104/pp.109.137265

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Received February 17, 2009
Accepted April 23, 2009

Role of Temperature Stress on Chloroplast Biogenesis and Protein Import in Pea (Pisum sativum L)

Siddhartha Dutta , Sasmita Mohanty , and Baishnab C. Tripathy *

School of Life Sciences, Jawaharlal Nehru University, New Delhi 110 067, India

* Corresponding author; email: bctripathy{at}mail.jnu.ac.in.

Modulation of photosynthesis and chloroplast biogenesis, by low and high temperatures, was studied in 12-d-old pea (Pisum sativum L) plants grown at 250C and subsequently exposed to 70C or 400C up to 48h. The decline in variable chlorophyll a fluorescence/maximum chlorophyll a fluorescence and estimated electron transport rate in temperature-stressed plants was substantially restored when they were transferred to room temperature. The ATP-driven import of precursor of small subunit of Rubisco (pRSS) into plastids was down-regulated by 67% and 49% in heat-stressed and chill-stressed plants respectively. Reduction in binding of the pRSS to the chloroplast envelope membranes in heat-stressed plants could be due to the down regulation of Toc159 gene/protein expression. In addition to impaired binding, reduced protein import into chloroplast in heat-stressed plants was likely due to decreased gene/protein expression of certain components of TOC complex (Toc75), TIC complex (Tic20, Tic32, Tic55, Tic62), stromal Hsp93 and stromal processing peptidase. In chill-stressed plants the gene/protein expression of most of the components of protein import apparatus other than Tic110 and Tic40 were not affected suggesting the central role of Tic110 and Tic40 in inhibition of protein import at low temperature. Heating of intact chloroplasts at 350C for 10 min inhibited protein import implying a low thermal stability of the protein import apparatus. Results demonstrate that in addition to decreased gene and protein expression, downregulation of photosynthesis in temperature-stressed plants is caused by reduced post-translational import of plastidic proteins required for the replacement of impaired proteins coded by nuclear genome.






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