Enhanced thermal stability of the thylakoid membranes from spruce. A comparison with selected angiosperms

Photosynth Res. 2016 Dec;130(1-3):357-371. doi: 10.1007/s11120-016-0269-3. Epub 2016 May 6.

Abstract

Recently, we have found that thermal stability of photosystem II (PSII) photochemistry in spruce needles is higher than in other plants (barley, beech) cultivated under the same temperatures. In this work, temperature dependences of various characteristics of PSII organization were studied in order to obtain complex information on the thermal stability of PSII function and organization in spruce. Temperature dependency of circular dichroism spectra revealed by about 6 °C higher thermal stability of macrodomain organization in spruce thylakoid membranes in comparison with Arabidopsis and barley ones; however, thermal disintegration of light-harvesting complex of PSII did not significantly differ among the species studied. These results thus indicate that thermal stability of PSII macro-organization in spruce thylakoid membranes is enhanced to a similar extent as thermal stability of PSII photochemistry. Clear-native polyacrylamide gel electrophoresis of preheated thylakoids demonstrated that among the separated pigment-protein complexes, only PSII supercomplexes (SCs) revealed considerably higher thermal stability in spruce thylakoids as compared to Arabidopsis and barley ones. Hence we suggest that higher thermal stability of PSII macro-organization of spruce is influenced by the maintenance of PSII SCs in the thylakoid membrane. In addition, we discuss possible effects of different PSII organizations and lipid compositions on the thermal stability of spruce thylakoid membranes.

Keywords: Circular dichroism; Norway spruce; Photosystem II organization; Thermal stability; Thylakoid membrane.

Publication types

  • Comparative Study

MeSH terms

  • Arabidopsis / cytology
  • Arabidopsis / physiology
  • Chlorophyll / physiology
  • Chlorophyll A
  • Circular Dichroism
  • Electrophoresis, Polyacrylamide Gel
  • Fluorescence
  • Hordeum / cytology
  • Hordeum / physiology
  • Hot Temperature
  • Photosystem II Protein Complex / physiology
  • Picea / cytology*
  • Picea / physiology
  • Thylakoids / physiology*

Substances

  • Photosystem II Protein Complex
  • Chlorophyll
  • Chlorophyll A