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   <subfield code="a">The short-term response of Arabidopsis thaliana (C3) and Zea mays (C4) chloroplasts to red and far red light</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Maksymilian Zienkiewicz, Anna Drożak, Wioleta Wasilewska, Ilona Bacławska, Ewa Przedpełska-Wąsowicz, Elżbieta Romanowska]</subfield>
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   <subfield code="a">Main conclusion : Light quality has various effects on photochemistry and protein phosphorylation in Zea mays and Arabidopsis thaliana thylakoids due to different degrees of light penetration across leaves and redox status in chloroplasts. The effect of the spectral quality of light (red, R and far red, FR) on the function of thylakoid proteins in Zea mays and Arabidopsis thaliana was investigated. It was concluded that red light stimulates PSII activity in A. thaliana thylakoids and in maize bundle sheath (BS) thylakoids, but not in mesophyll (M) thylakoids. The light quality did not change PSI activity in M thylakoids of maize. FR used after a white light period increased PSI activity significantly in maize BS and only slightly in A. thaliana thylakoids. As shown by blue native (BN)-PAGE followed by SDS-PAGE, proteins were differently phosphorylated in the thylakoids, indicating their different functions. FR light increased dephosphorylation of LHCII proteins in A. thaliana thylakoids, whereas in maize, dephosphorylation did not occur at all. The rate of phosphorylation was higher in maize BS than in M thylakoids. D1 protein phosphorylation increased in maize and decreased in A. thaliana upon irradiation with both R and growth light (white light, W). Light variations did not change the level of proteins in thylakoids. Our data strongly suggest that response to light quality is a species-dependent phenomenon. We concluded that the maize chloroplasts were differently stimulated, probably due to different degrees of light penetration across the leaf and thereby the redox status in the chloroplasts. These acclimation changes induced by light quality are important in the regulation of chloroplast membrane flexibility and thus its function.</subfield>
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   <subfield code="a">Springer-Verlag Berlin Heidelberg, 2015</subfield>
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   <subfield code="a">Acclimation to light quality</subfield>
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   <subfield code="a">Bundle sheath chloroplasts</subfield>
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   <subfield code="a">Mesophyll chloroplasts</subfield>
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   <subfield code="a">PSI</subfield>
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   <subfield code="a">PSII</subfield>
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   <subfield code="a">Protein phosphorylation</subfield>
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   <subfield code="a">Red and far red light</subfield>
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   <subfield code="a">Thylakoids</subfield>
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   <subfield code="a">BS : Bundle sheath</subfield>
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   <subfield code="a">BN-PAGE : Blue native electrophoresis</subfield>
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   <subfield code="a">CET : Cyclic electron transport</subfield>
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   <subfield code="a">FR : Far red light</subfield>
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   <subfield code="a">LHCII : Chlorophyll a/b- binding protein of photosystem II</subfield>
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   <subfield code="a">M : Mesophyll</subfield>
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   <subfield code="a">R : Red light</subfield>
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   <subfield code="a">W : White light</subfield>
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