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Photosynthetic adaptation to Length of Day Is Dependent on S-sulfocysteine synthase activity in the thylakoid

Bermúdez, MA and Galmés, J and Moreno, I and Mullineaux, PM and Gotor, C and Romero, LC (2012) 'Photosynthetic adaptation to Length of Day Is Dependent on S-sulfocysteine synthase activity in the thylakoid.' Plant Physiology, 160 (1). 274 - 288. ISSN 0032-0889

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Abstract

Arabidopsis (Arabidopsis thaliana) chloroplasts contain two O-acetyl-serine(thiol)lyase (OASTL) homologs, OAS-B, which is an authentic OASTL, and CS26, which has S-sulfocysteine synthase activity. In contrast with OAS-B, the loss of CS26 function resulted in dramatic phenotypic changes, which were dependent on the light treatment. We have performed a detailed characterization of the photosynthetic and chlorophyll fluorescence parameters in cs26 plants compared with those of wildtype plants under short-day growth conditions (SD) and long-day growth conditions (LD). Under LD, the photosynthetic characterization, which was based on substomatal CO 2 concentrations and CO 2 concentration in the chloroplast curves, revealed significant reductions in most of the photosynthetic parameters for cs26, which were unchanged under SD. These parameters included net CO 2 assimilation rate, mesophyll conductance, and mitochondrial respiration at darkness. The analysis also showed that cs26 under LD required more absorbed quanta per driven electron flux and fixed CO 2 . The nonphotochemical quenching values suggested that in cs26 plants, the excess electrons that are not used in photochemical rea ctions may form reactive oxygen species. A photoinhibitory effect was confirmed by the background fluorescence signal values under LD and SD, which were higher in young leaves compared with mature ones under SD. To hypothesize the role of CS26 in relation to the photosynthetic machinery, we addressed its location inside of the chloroplast. The activity determination and localization analyses that were performed using immunoblotting indicated the presence of an active CS26 enzyme exclusively in the thylakoid lumen. This finding was reinforced by the observation of marked alterations in many lumenal proteins in the cs26 mutant compared with the wild type. © 2012 American Society of Plant Biologists.

Item Type: Article
Subjects: Q Science > QK Botany
Q Science > QP Physiology
Divisions: Faculty of Science and Health > Biological Sciences, School of
Depositing User: Philip Mullineaux
Date Deposited: 01 Feb 2013 10:39
Last Modified: 17 Aug 2017 18:03
URI: http://repository.essex.ac.uk/id/eprint/5433

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