Unveiling the molecular mechanisms of size-dependent effect of polystyrene micro/nano-plastics on Chlamydomonas reinhardtii through proteomic profiling.

Microplastics have become a prevalent environmental pollutant due to widespread release and production. Algae, as primary producers, play a crucial role in maintaining the ecological balance of freshwater environments. Despite reports on the inhibition of microalgae by microplastics, the size-dependent effects on microalgae and associated molecular mechanism remain poorly understood. This study investigates the impacts of three polystyrene micro/nano-plastics (PS-MNPs) with different sizes (100 nm, 350 nm, and 6 µm) and concentrations (25-200 mg/L) on Chlamydomonas reinhardtii (C. reinhardtii) throughout its growth period. Results reveal size- and concentration-dependent growth inhibition and induction of oxidative stress by PS-MNPs, with microalgae exhibiting increased vulnerability to smaller-sized and higher-concentration PS-MNPs. Proteomics analysis elucidates the size-dependent suppression of proteins involved in the photosynthesis process by PS-MNPs. Photosynthetic activity assays demonstrate that smaller PS-MNPs more significantly reduce chlorophyll content and the maximal photochemical efficiency of photosystem II. Finally, electron microscope and Western blot assays collectively confirm the size effect of PS-MNPs on microalgae growth is attributable to suppressed protein expression rather than shading effects. This study contributes to advancing our understanding of the intricate interactions between micro/nano-plastics and algae at the molecular level, emphasizing the efficacy of proteomics in dissecting the mechanistic aspects of microplastics-induced biological effects on environmental indicator organisms.

The plastid-encoded protein Orf2971 is required for protein translocation and chloroplast quality control.

Photosynthesis and the biosynthesis of many important metabolites occur in chloroplasts. In these semi-autonomous organelles, the chloroplast genome encodes approximately 100 proteins. The remaining chloroplast proteins, close to 3,000, are encoded by nuclear genes whose products are translated in the cytosol and imported into chloroplasts. However, there is still no consensus on the composition of the protein import machinery including its motor proteins and on how newly imported chloroplast proteins are refolded. In this study, we have examined the function of orf2971, the largest chloroplast gene of Chlamydomonas reinhardtii. The depletion of Orf2971 causes the accumulation of protein precursors, partial proteolysis and aggregation of proteins, increased expression of chaperones and proteases, and autophagy. Orf2971 interacts with the TIC (translocon at the inner chloroplast envelope) complex, catalyzes ATP (adenosine triphosphate) hydrolysis, and associates with chaperones and chaperonins. We propose that Orf2971 is intimately connected to the protein import machinery and plays an important role in chloroplast protein quality control.

Smart Self-Cleaning Membrane via the Blending of an Upper Critical Solution Temperature Diblock Copolymer with PVDF.

Poly(2,2,2-trifluoroethyl methacrylate)-b-poly(imidazoled glycidyl methacrylate-co-diethylene glycol methyl ether methacrylate) (PTFEMA-b-P(iGMA-co-MEO2MA)) containing an upper critical solution temperature (UCST) polymer chain was prepared and blended with poly(vinylidene fluoride) (PVDF) to produce a thermoresponsive membrane with smart self-cleaning performance. The successful preparation of the membrane was demonstrated by attenuated total reflection-Fourier-transform infrared spectroscopy, X-ray photoelectron spectroscopy, and scanning electron microscopy characterization. The membrane shows UCST performance, and its flux changes with the filtrate temperature as the UCST polymer chain stretches out and contracts in response to various temperatures. In addition, the UCST polymer chain can disrupt the foulant and push it away from the membrane when the temperature is above the UCST and thus enables membranes to exhibit a smart self-cleaning behavior. To the best of our knowledge, this work is the first report of a smart self-cleaning membrane based on the blending of a diblock copolymer containing a UCST polymer chain with PVDF.

Preparation of Multipurpose Polyvinylidene Fluoride Membranes via a Spray-Coating Strategy Using Waterborne Polymers.

As reported herein, the waterborne polymers poly(glycidyl methacrylate-co-poly(ethylene glycol) methyl ether methacrylate) P(GMA-co-mPEGMA) and polyethyleneimine (PEI) were used to prepare multipurpose polyvinylidene fluoride (PVDF) membranes via a direct spray-coating method. P(GMA-co-mPEGMA) and PEI were alternately sprayed onto the PVDF membrane to yield stable cross-linked copolymer coatings. The successful coating of polymers onto the membrane surface was verified by scanning electron microscopy, attenuated total reflectance-Fourier transform infrared spectroscopy, and X-ray photoelectron spectroscopy characterization. The coated membrane exhibited oil rejection rates that exceeded 99.0% for oil water mixture separation and 98.0% for oil/water emulsion separation. The flux recovery ratio reached 96.7% after bovine serum albumin filtration and washing with water. The removal efficiencies of the coated membrane M3 for Congo red, methyl orange, methylene blue, and crystal violet, Pb(II), Cu(II), and Cd(II) were 82.4, 83.9, 6.3, 26.8, 90.6, 91.3, and 86.2%, respectively. Thus, it can be used for the removal of dyes and heavy metal ions from wastewater. The antibacterial activities of the coated membranes were also confirmed by the inhibition zone tests and confocal laser scanning microscopy analysis. In addition, the cross-linking strategy provides the coated membranes with excellent durability and repeatability. More importantly, the use of water as the solvent can ensure that the application of these membrane coatings proceeds via a very safe and environmentally friendly coating process.

In situ growth of well-ordered NiFe-MOF-74 on Ni foam by Fe2+ induction as an efficient and stable electrocatalyst for water oxidation.

Well-ordered NiFe-MOF-74 is in situ grown on Ni foam by the induction of Fe2+ and directly used as an OER electrocatalyst. Benefited from the intrinsic open porous structure of MOF-74, the in situ formed MOF arrays and the synergistic effect of Ni and Fe, outstanding water oxidation activity is obtained in alkaline electrolytes with an overpotential of 223 mV at 10 mA cm-2.

A Ni-P@NiCo LDH core-shell nanorod-decorated nickel foam with enhanced areal specific capacitance for high-performance supercapacitors.

Recently, transition metal-based nanomaterials have played a key role in the applications of supercapacitors. In this study, nickel phosphide (Ni-P) was simply combined with NiCo LDH via facile phosphorization of Ni foam and subsequent electrodeposition to form core-shell nanorod arrays on the Ni foam; the Ni-P@NiCo LDH was then directly used for a pseudocapacitive electrode. Owing to the splendid synergistic effect between Ni-P and NiCo LDH nanosheets as well as the hierarchical structure of 1D nanorods, 2D nanosheets, and 3D Ni foam, the hybrid electrode exhibited significantly enhanced electrochemical performances. The Ni-P@NiCo LDH electrode showed a high specific capacitance of 12.9 F cm-2 at 5 mA cm-2 (3470.5 F g-1 at a current density of 1.3 A g-1) that remained as high as 6.4 F cm-2 at a high current density of 100 mA cm-2 (1700 F g-1 at 27 A g-1) and excellent cycling stability (96% capacity retention after 10 000 cycles at 40 mA cm-2). Furthermore, the asymmetric supercapacitors (ASCs) were assembled using Ni-P@NiCo LDH as a positive electrode and activated carbon (AC) as a negative electrode. The obtained ASCs delivered remarkable energy density and power density as well as good cycling performance. The enhanced electrochemical activities open a new avenue for the development of supercapacitors.

A Light Harvesting Complex-Like Protein in Maintenance of Photosynthetic Components in Chlamydomonas.

Using a genetic approach, we have identified and characterized a novel protein, named Msf1 (Maintenance factor for photosystem I), that is required for the maintenance of specific components of the photosynthetic apparatus in the green alga Chlamydomonas reinhardtii Msf1 belongs to the superfamily of light-harvesting complex proteins with three transmembrane domains and consensus chlorophyll-binding sites. Loss of Msf1 leads to reduced accumulation of photosystem I and chlorophyll-binding proteins/complexes. Msf1is a component of a thylakoid complex containing key enzymes of the tetrapyrrole biosynthetic pathway, thus revealing a possible link between Msf1 and chlorophyll biosynthesis. Protein interaction assays and greening experiments demonstrate that Msf1 interacts with Copper target homolog1 (CHL27B) and accumulates concomitantly with chlorophyll in Chlamydomonas, implying that chlorophyll stabilizes Msf1. Contrary to other light-harvesting complex-like genes, the expression of Msf1 is not stimulated by high-light stress, but its protein level increases significantly under heat shock, iron and copper limitation, as well as in stationary cells. Based on these results, we propose that Msf1 is required for the maintenance of photosystem I and specific protein-chlorophyll complexes especially under certain stress conditions.

Deletion of CGLD1 Impairs PSII and Increases Singlet Oxygen Tolerance of Green Alga Chlamydomonas reinhardtii.

The green alga Chlamydomonas reinhardtii is a key model organism for studying photosynthesis and oxidative stress in unicellular eukaryotes. Using a forward genetics approach, we have identified and characterized a mutant x32, which lacks a predicted protein named CGLD1 (Conserved in Green Lineage and Diatom 1) in GreenCut2, under normal and stress conditions. We show that loss of CGLD1 resulted in minimal photoautotrophic growth and PSII activity in the organism. We observed reduced amount of PSII complex and core subunits in the x32 mutant based on blue-native (BN)/PAGE and immunoblot analysis. Moreover, x32 exhibited increased sensitivity to high-light stress and altered tolerance to different reactive oxygenic species (ROS) stress treatments, i.e., decreased resistance to H2O2/or tert-Butyl hydroperoxide (t-BOOH) and increased tolerance to neutral red (NR) and rose bengal (RB) that induce the formation of singlet oxygen, respectively. Further analysis via quantitative real-time PCR (qRT-PCR) indicated that the increased singlet-oxygen tolerance of x32 was largely correlated with up-regulated gene expression of glutathione-S-transferases (GST). The phenotypical and physiological implications revealed from our experiments highlight the important roles of CGLD1 in maintaining structure and function of PSII as well as in protection of Chlamydomonas under photo-oxidative stress conditions.

Loss of algal Proton Gradient Regulation 5 increases reactive oxygen species scavenging and H2 evolution.

We have identified hpm91, a Chlamydomonas mutant lacking Proton Gradient Regulation5 (PGR5) capable of producing hydrogen (H2 ) for 25 days with more than 30-fold yield increase compared to wild type. Thus, hpm91 displays a higher capacity of H2 production than a previously characterized pgr5 mutant. Physiological and biochemical characterization of hpm91 reveal that the prolonged H2 production is due to enhanced stability of PSII, which correlates with increased reactive oxygen species (ROS) scavenging capacity during sulfur deprivation. This anti-ROS response appears to protect the photosynthetic electron transport chain from photo-oxidative damage and thereby ensures electron supply to the hydrogenase.