Heat-induced disassembly and degradation of chlorophyll-containing protein complexes in vivo
Gradual heating of green leaves up to non-physiological temperatures is often used to estimate thermal stability of photosynthetic apparatus. However, a complete sequence of heat-induced disassembly and denaturation of chlorophyll-containing protein complexes (CPCs) has not been reported yet. In thi...
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Published in | Biochimica et biophysica acta Vol. 1797; no. 1; pp. 63 - 70 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
2010
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Subjects | |
Online Access | Get full text |
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Summary: | Gradual heating of green leaves up to non-physiological temperatures is often used to estimate thermal stability of photosynthetic apparatus. However, a complete sequence of heat-induced disassembly and denaturation of chlorophyll-containing protein complexes (CPCs) has not been reported yet. In this work, we heated (1 °C·min
−
1
) barley leaves to temperatures selected according to the changes in the chlorophyll fluorescence temperature curve (FTC) and we analyzed CPC stability by two-dimensional native Deriphat/SDS–PAGE
. The first distinct change in both structure and function of photosystem II (PSII) appeared at 40–50 °C. PSII core (CCII) dimers began to dissociate monomers, which was accompanied by a decrease in PSII photochemistry and reflected in FTC as the first fluorescence increase. Further changes in CPCs appeared at 57–60 °C, when FTC increases to its second maximum. Photosystem I (PSI) cores (CCI) partially dissociated from light-harvesting complexes of PSI (LHCI) and formed aggregates. The rest of CCI–LHCI complexes, as well as the CCI aggregates, degraded to the PSI-A/B heterodimer in leaves heated to 70 °C. Heating to these temperatures led to a complete degradation of CCII components and corresponding loss of PSII photochemistry. Trimeric light-harvesting complexes of PSII (LHCII) markedly dissociated to monomers and denatured, as evidenced by a release of large amount of free chlorophylls. Between 70 and 80 °C, a complete degradation of LHCII occurred, leaving the PSI-A/B heterodimer as the only detectable CPC in the membrane. This most thermostable CPC disappeared after heating to 90 °C, which corresponded to a loss of PSI photochemistry. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0005-2728 0006-3002 1879-2650 |
DOI: | 10.1016/j.bbabio.2009.08.001 |