The extrinsic proteins of Photosystem II

Years of genetic, biochemical, and structural work have provided a number of insights into the oxygen evolving complex (OEC) of Photosystem II (PSII) for a variety of photosynthetic organisms. However, questions still remain about the functions and interactions among the various subunits that make up the OEC. After a brief introduction to the individual subunits Psb27, PsbP, PsbQ, PsbR, PsbU, and PsbV, a current picture of the OEC as a whole in cyanobacteria, red algae, green algae, and higher plants will be presented. Additionally, the role that these proteins play in the dynamic life cycle of PSII will be discussed. © 2006 Springer Science+Business Media B.V

The PsbP domain protein 1 functions in the assembly of lumenal domains in photosystem I

Photosystem I (PS I) is a multisubunit membrane protein complex that functions as a light-driven plastocyanin-ferredoxin oxidoreductase. The PsbP domain protein 1 (PPD1; At4g15510) is located in the thylakoid lumen of plant chloroplasts and is essential for photoautotrophy, functioning as a PS I assembly factor. In this work, RNAi was used to suppress PPD1 expression, yielding mutants displaying a range of phenotypes with respect to PS I accumulation and function. These PPD1 RNAi mutants showed a loss of assembled PS I that was correlated with loss of the PPD1 protein. In the most severely affected PPD1 RNAi lines, the accumulated PS I complexes exhibited defects in electron transfer from plastocyanin to the oxidized reaction center P 700+. The defects in PS I assembly in the PPD1 RNAi mutants also had secondary effects with respect to the association of light-harvesting antenna complexes to PS I. Because of the imbalance in photosystem function in the PPD1 RNAi mutants, light-harvesting complex II associated with and acted as an antenna for the PS I complexes. These results provide new evidence for the role of PPD1 in PS I biogenesis, particularly as a factor essential for proper assembly of the lumenal portion of the complex. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc

N-terminal lipid modification is required for the stable accumulation of CyanoQ in Synechocystis sp. PCC 6803

© 2016 Juneau et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. The CyanoQ protein has been demonstrated to be a component of cyanobacterial Photosystem II (PS II), but there exist a number of outstanding questions concerning its physical association with the complex. CyanoQ is a lipoprotein; upon cleavage of its transit peptide by Signal Peptidase II, which targets delivery of the mature protein to the thylakoid lumenal space, the N-terminal cysteinyl residue is lipid-modified. This modification appears to tether this otherwise soluble component to the thylakoid membrane. To probe the functional significance of the lipid anchor, mutants of the CyanoQ protein have been generated in Synechocystis sp. PCC 6803 to eliminate the N-terminal cysteinyl residue, preventing lipid modification. Substitution of the N-terminal cysteinyl residue with serine (Q-C22S) resulted in a decrease in the amount of detectable CyanoQ protein to 17% that of the wild-type protein. Moreover, the physical properties of the accumulated Q-C22S protein were consistent with altered processing of the CyanoQ precursor. The Q-C22S protein was shifted to a higher apparent molecular mass and partitioned in the hydrophobic phase in TX-114 phase-partitioning experiments. These results suggest that the hydrophobic N-terminal 22 amino acids were not properly cleaved by a signal peptidase. Substitution of the entire CyanoQ transit peptide with the transit peptide of the soluble lumenal protein PsbO yielded the Q-SS mutant and resulted in no detectable accumulation of the modified CyanoQ protein. Finally, the CyanoQ protein was present at normal amounts in the PS II mutant strains ΔpsbB and ΔpsbO, indicating that an association with PS II was not a prerequisite for stable CyanoQ accumulation. Together these results indicate that CyanoQ accumulation in Synechocystis sp. PCC 6803 depends on the presence of the N-terminal lipid anchor, but not on the association of CyanoQ with the PS II complex

The extrinsic proteins of photosystem II: update

© 2016, Springer-Verlag Berlin Heidelberg. Main conclusion: Recent investigations have provided important new insights into the structures and functions of the extrinsic proteins of Photosystem II. This review is an update of the last major review on the extrinsic proteins of Photosystem II (Bricker et al., Biochemistry 31:4623–4628 2012). In this report, we will examine advances in our understanding of the structure and function of these components. These proteins include PsbO, which is uniformly present in all oxygenic organisms, the PsbU, PsbV, CyanoQ, and CyanoP proteins, found in the cyanobacteria, and the PsbP, PsbQ and PsbR proteins, found in the green plant lineage. These proteins serve to stabilize the Mn4CaO5 cluster and optimize oxygen evolution at physiological calcium and chloride concentrations. The mechanisms used to perform these functions, however, remain poorly understood. Recently, important new findings have significantly advanced our understanding of the structures, locations and functions of these important subunits. We will discuss the biochemical, structural and genetic studies that have been used to elucidate the roles played by these proteins within the photosystem and their locations within the photosynthetic complex. Additionally, we will examine open questions needing to be addressed to provide a coherent picture of the role of these components within the photosystem

Action research and democracy

This contribution explores the relationship between research and learning democracy. Action research is seen as being compatible with the orientation of educational and social work research towards social justice and democracy. Nevertheless, the history of action research is characterized by a tension between democracy and social engineering. In the social-engineering approach, action research is conceptualized as a process of innovation aimed at a specific Bildungsideal. In a democratic approach action research is seen as research based on cooperation between research and practice. However, the notion of democratic action research as opposed to social engineering action research needs to be theorized. So called democratic action research involving the implementation by the researcher of democracy as a model and as a preset goal, reduces cooperation and participation into instruments to reach this goal, and becomes a type of social engineering in itself. We argue that the relationship between action research and democracy is in the acknowledgment of the political dimension of participation: ‘a democratic relationship in which both sides exercise power and shared control over decision-making as well as interpretation’. This implies an open research design and methodology able to understand democracy as a learning process and an ongoing experiment

The extrinsic proteins of Photosystem II

In this review we examine the structure and function of the extrinsic proteins of Photosystem II. These proteins include PsbO, present in all oxygenic organisms, the PsbP and PsbQ proteins, which are found in higher plants and eukaryotic algae, and the PsbU, PsbV, CyanoQ, and CyanoP proteins, which are found in the cyanobacteria. These proteins serve to optimize oxygen evolution at physiological calcium and chloride concentrations. They also shield the Mn 4CaO 5 cluster from exogenous reductants. Numerous biochemical, genetic and structural studies have been used to probe the structure and function of these proteins within the photosystem. We will discuss the most recent proposed functional roles for these components, their structures (as deduced from biochemical and X-ray crystallographic studies) and the locations of their proposed binding domains within the Photosystem II complex. This article is part of a Special Issue entitled: Photosystem II. © 2011 Elsevier B.V. All rights reserved

On the stability of periodic orbits in delay equations with large delay

We prove a necessary and sufficient criterion for the exponential stability of periodic solutions of delay differential equations with large delay. We show that for sufficiently large delay the Floquet spectrum near criticality is characterized by a set of curves, which we call asymptotic continuous spectrum, that is independent on the delay.Comment: postprint versio

Bottom-up perspective:The role of roots and rhizosphere in climate change adaptation and mitigation in agroecosystems

Climate change is happening and causing severe impact on the sustainability of agroecosystems. We argue that many of the abiotic stresses associated with climate change will be most acutely perceived by the plant at the root-soil interface and are likely to be mitigated at this globally important interface. In this review we will focus on the direct impacts of climate change, temperature, drought and pCO2, on roots and rhizospheres. We consider which belowground traits will be impacted and discuss the potential for monitoring and quantifying these traits for modelling and breeding programs. We discuss the specific impacts of combined stress and the role of the microbial communities populating the root-soil interface, collectively referred to as the rhizosphere microbiota, in interactions with roots under stress and discuss the plastic responses to stress as a way of adapting plants to climate change. We then go on to discuss the role that modelling has in understanding this complex problem and suggest the best belowground targets for adaptation and mitigation to climate change. We finish by considering where the main uncertainties lie, providing perspective on where research is needed. This review therefore focuses on the potential of roots and rhizosphere to adapt to the climate change effects and to mitigate their negative impacts on plant growth, crop productivity, soil health and ecosystem services

Surface tension, rheology and hydrophobicity of rhizodeposits and seed mucilage influence soil water retention and hysteresis

Aims: Rhizodeposits collected from hydroponic solutions with roots of maize and barley, and seed mucilage washed from chia, were added to soil to measure their impact on water retention and hysteresis in a sandy loam soil at a range of concentrations. We test the hypothesis that the effect of plant exudates and mucilages on hydraulic properties of soils depends on their physicochemical characteristics and origin.Methods: Surface tension and viscosity of the exudate solutions were measured using the Du Noüy ring method and a cone-plate rheometer, respectively. The contact angle of water on exudate treated soil was measured with the sessile drop method. Water retention and hysteresis were measured by equilibrating soil samples, treated with exudates and mucilages at 0.46 and 4.6 mg g−1 concentration, on dialysis tubing filled with polyethylene glycol (PEG) solution of known osmotic potential.Results: Surface tension decreased and viscosity increased with increasing concentration of the exudates and mucilage in solutions. Change in surface tension and viscosity was greatest for chia seed exudate and least for barley root exudate. Contact angle increased with increasing maize root and chia seed exudate concentration in soil, but not barley root. Chia seed mucilage and maize root rhizodeposits enhanced soil water retention and increased hysteresis index, whereas barley root rhizodeposits decreased soil water retention and the hysteresis effect. The impact of exudates and mucilages on soil water retention almost ceased when approaching wilting point at −1500 kPa matric potential.Conclusions: Barley rhizodeposits behaved as surfactants, drying the rhizosphere at smaller suctions. Chia seed mucilage and maize root rhizodeposits behaved as hydrogels that hold more water in the rhizosphere, but with slower rewetting and greater hysteresis