Institutional Change in Market-Liberal State Capitalism : An Integrative Perspective on the Development of the Private Business Sector in China

This paper shows that a more accurate depiction of the development of China’s private sector is gained by considering the complex interaction between bottom-up and topdown processes. First, the paper analyzes the general characteristics of Chinese capitalism to help understand and classify the gradual institutional change in the enterprise sector. Second, it draws on insights from comparative political economy and new approaches in political science to introduce the strategy of “wearing a red hat,” an empirical phenomenon that provides a framework for the emergence from the 1980s of China’s private sector. This section also examines the closely interwoven relationships between private companies and the party-state that have taken place since the 1990s. Third, the paper indicates that focusing on state/capital relationships at different administrational levels contributes to a better understanding of China’s private sector. It concludes that the development and success of the new private enterprises, which remained closely linked to the state, enabled the ruling elite to form and consolidate a hegemonic project that provided relative societal coherence on the often bumpy road to reform.Dieser Artikel zeigt auf, dass ein Blick auf die komplexen Interaktionen zwischen „Bottom- up“- und „Top-down“-Prozessen ein präziseres Bild der Entwicklung des Privatsektors in China liefert. Dabei hilft erstens eine Analyse von grundlegenden Merkmalen des chinesischen Kapitalismus, um den graduellen institutionellen Wandel im Unternehmenssektor verstehen beziehungsweise einordnen zu können. Unter Bezugnahme auf die Vergleichende Politische Ökonomie und neuere politikwissenschaftliche Ansätze werden, zweitens, die empirischen Phänomene des „wearing a red hat“ in der Entstehungsphase des Privatsektors ab den 1980ern sowie der seitdem eng verknüpften Beziehungen zwischen Privatunternehmen und dem Parteistaat eingeführt. Drittens wird erörtert, dass ein Fokus auf die engen Beziehungen zwischen Staat und Kapital auf verschiedenen administrativen Ebenen zu einem besseren Verständnis des chinesischen Privatsektors beiträgt. Wie abschließend festgehalten wird, ermöglichte die Entwicklung und der Erfolg der neuen privaten, jedoch weiterhin eng mit dem Staat verbundenen Unternehmen es der Machtelite, ein hegemoniales Projekt zu formieren und aufrechtzuerhalten, das dem holprigen Reformweg eine relative gesellschaftliche Stabilität verlieh

A functional RNase P protein subunit of bacterial origin in some eukaryotes

RNase P catalyzes 5′-maturation of tRNAs. While bacterial RNase P comprises an RNA catalyst and a protein cofactor, the eukaryotic (nuclear) variant contains an RNA and up to ten proteins, all unrelated to the bacterial protein. Unexpectedly, a nuclear-encoded bacterial RNase P protein (RPP) homolog is found in several prasinophyte algae including Ostreococcus tauri. We demonstrate that recombinant O. tauri RPP can functionally reconstitute with bacterial RNase P RNAs (RPRs) but not with O. tauri organellar RPRs, despite the latter’s presumed bacterial origins. We also show that O. tauri PRORP, a homolog of Arabidopsis PRORP-1, displays tRNA 5′-processing activity in vitro. We discuss the implications of the striking diversity of RNase P in O. tauri, the smallest known free-living eukaryote.Ministerio de Ciencia e Innovación European Regional Fund BFU2007-60651Junta de Andalucía P06-CVI-01692National Science Foundation MCB-0238233 MCB-0843543European Union ASSEMBLE 22779

Electron Transfer Pathways and Dynamics of Chloroplast NADPH-dependent Thioredoxin Reductase C (NTRC)

NADPH-dependent thioredoxin reductases (NTRs) contain a flavin cofactor and a disulfide as redox-active groups. The catalytic mechanism of standard NTR involves a large conformational change between two configurations. Oxygenic photosynthetic organisms possess a plastid-localized NTR, called NTRC, with a thioredoxin module fused at the C terminus. NTRC is an efficient reductant of 2-Cys peroxiredoxins (2-Cys Prxs) and thus is involved in the protection against oxidative stress, among other functions. Although the mechanism of electron transfer of canonical NTRs is well established, it is not yet known in NTRC. By employing stopped-flow spectroscopy, we have carried out a comparative kinetic study of the electron transfer reactions involving NTRC, the truncated NTR module of NTRC, and NTRB, a canonical plant NTR. Whereas the three NTRs maintain the conformational change associated with the reductive cycle of catalysis, NTRC intramolecular electron transfer to the thioredoxin module presents two kinetic components (kET of ∼2 and 0.1 s−1), indicating the occurrence of additional dynamic motions. Moreover, the dynamic features associated with the electron transfer to the thioredoxin module are altered in the presence of 2-Cys Prx. NTRC shows structural constraints that may locate the thioredoxin module in positions with different efficiencies for electron transfer, the presence of 2-Cys Prx shifting the conformational equilibrium of the thioredoxin module to a specific position, which is not the most efficien

The heterologous expression of a plastocyanin in the diatom Phaeodactylum tricornutum improves cell growth under iron-deficient conditions

We have investigated if the heterologous expression of a functional green alga plastocyanin in the diatom Phaeodactylum tricornutum can improve photosynthetic activity and cell growth. Previous in vitro assays showed that a single-mutant of the plastocyanin from the green algae Chlamydomonas reinhardtii is effective in reducing P. tricornutum photosystem I. In this study, in vivo assays with P. tricornutum strains expressing this plastocyanin indicate that even the relatively low intracellular concentrations of holo-plastocyanin detected (≈4 μM) are enough to promote an increased growth (up to 60%) under iron-deficient conditions as compared with the WT strain, measured as higher cell densities, content in pigments and active photosystem I, global photosynthetic rates per cell, and even cell volume. In addition, the presence of plastocyanin as an additional photosynthetic electron carrier seems to decrease the over-reduction of the plastoquinone pool. Consequently, it promotes an improvement in the maximum quantum yield of both photosystem II and I, together with a decrease in the acceptor side photoinhibition of photosystem II—also associated to a reduced oxidative stress—a decrease in the peroxidation of membrane lipids in the choroplast, and a lower degree of limitation on the donor side of photosystem I. Thus the heterologous plastocyanin appears to act as a functional electron carrier, alternative to the native cytochrome c6, under iron-limiting conditions.Junta de Andalucía PAIDI BIO-022Ministerio de Economía y Competitividad BIO2015-64169-

The singular properties of photosynthetic cytochrome c 550 from the diatom Phaeodactylum tricornutum suggest new alternative functions

Cytochrome c 550 is an extrinsic component in the luminal side of photosystem II (PSII) in cyanobacteria, as well as in eukaryotic algae from the red photosynthetic lineage including, among others, diatoms. We have established that cytochrome c 550 from the diatom Phaeodactylum tricornutum can be obtained as a complete protein from the membrane fraction of the alga, although a C-terminal truncated form is purified from the soluble fractions of this diatom as well as from other eukaryotic algae. Eukaryotic cytochromes c 550 show distinctive electrostatic features as compared with cyanobacterial cytochrome c 550 . In addition, co-immunoseparation and mass spectrometry experiments, as well as immunoelectron microscopy analyses, indicate that although cytochrome c 550 from P. tricornutum is mainly located in the thylakoid domain of the chloroplast – where it interacts with PSII –, it can also be found in the chloroplast pyrenoid, related with proteins linked to the CO 2 concentrating mechanism and assimilation. These results thus suggest new alternative functions of this heme protein in eukaryotes.Ministerio de Economía, Industria y Competitividad BIO2015-64169-PJunta de Andalucía PAIDI BIO-02

Molecular recognition in the interaction of chloroplast 2-Cys peroxiredoxin with NADPH-thioredoxin reductase C (NTRC) and thioredoxin x

In addition to the standard NADPH thioredoxin reductases (NTRs), plants hold a plastidic NTR (NTRC), with a thioredoxin module fused at the C-terminus. NTRC is an efficient reductant of 2-Cys peroxiredoxins (2-Cys Prxs). The interaction of NTRC and chloroplastic thioredoxin x with 2-Cys Prxs has been confirmed in vivo, by bimolecular fluorescence complementation (BiFC) assays, and in vitro, by isothermal titration calorimetry (ITC) experiments. In comparison with thioredoxin x, NTRC interacts with 2-Cys Prx with higher affinity, both the thioredoxin and NTR domains of NTRC contributing significantly to this interaction, as demonstrated by using the NTR and thioredoxin modules of the enzyme expressed separately. The presence of the thioredoxin domain seems to prevent the interaction of NTRC with thioredoxin x.Junta de Andalucía BIO-022, CVI-4528, BIO-182, CVI-5919Ministerio de Ciencia e Innovación BIO2010-15430, BFU2010-1945

The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum

The photosynthetic cytochrome c550 from the marine diatom Phaeodactylum tricornutum has been purified and characterized. Cytochrome c550 is mostly obtained from the soluble cell extract in relatively large amounts. In addition, the protein appeared to be truncated in the last hydrophobic residues of the C-terminus, both in the soluble cytochrome c550 and in the protein extracted from the membrane fraction, as deduced by mass spectrometry analysis and the comparison with the gene sequence. Interestingly, it has been described that the C-terminus of cytochrome c550 forms a hydrophobic finger involved in the interaction with photosystem II in cyanobacteria. Cytochrome c550 was almost absent in solubilized photosystem II complex samples, in contrast with the PsbO and Psb31 extrinsic subunits, thus suggesting a lower affinity of cytochrome c550 for the photosystem II complex. Under iron-limiting conditions the amount of cytochrome c550 decreases up to about 45% as compared to iron-replete cells, pointing to an iron-regulated synthesis. Oxidized cytochrome c550 has been characterized using continuous wave EPR and pulse techniques, including HYSCORE, and the obtained results have been interpreted in terms of the electrostatic charge distribution in the surroundings of the heme centre.España, MINECO BIO2012-35271, BIO2015-64169-P, MAT2011-23861 and CTQ2015-64486-

Iron Deficiency Induces a Partial Inhibition of the Photosynthetic Electron Transport and a High Sensitivity to Light in the Diatom Phaeodactylum tricornutum

Iron limitation is the major factor controlling phytoplankton growth in vast regions of the contemporary oceans. In this study, a combination of thermoluminescence (TL), chlorophyll fluorescence, and P700 absorbance measurements have been used to elucidate the effects of iron deficiency in the photosynthetic electron transport of the marine diatom P. tricornutum. TL was used to determine the effects of iron deficiency on photosystem II (PSII) activity. Excitation of iron-replete P. tricornutum cells with single turn-over flashes induced the appearance of TL glow curves with two components with different peaks of temperature and contributions to the total signal intensity: the B band (23°C, 63%), and the AG band (40°C, 37%). Iron limitation did not significantly alter these bands, but induced a decrease of the total TL signal. Far red excitation did not increase the amount of the AG band in iron-limited cells, as observed for iron-replete cells. The effect of iron deficiency on the photosystem I (PSI) activity was also examined by measuring the changes in P700 redox state during illumination. The electron donation to PSI was substantially reduced in iron-deficient cells. This could be related with the important decline on cytochrome c6 content observed in these cells. Iron deficiency also induced a marked increase in light sensitivity in P. tricornutum cells. A drastic increase in the level of peroxidation of chloroplast lipids was detected in iron-deficient cells even when grown under standard conditions at low light intensity. Illumination with a light intensity of 300 μE m-2 s-1 during different time periods caused a dramatic disappearance in TL signal in cells grown under low iron concentration, this treatment not affecting to the signal in iron-replete cells. The results of this work suggest that iron deficiency induces partial blocking of the electron transfer between PSII and PSI, due to a lower concentration of the electron donor cytochrome c6. This decreased electron transfer may induce the over-reduction of the plastoquinone pool and consequently the appearance of acceptor side photoinhibition in PSII even at low light intensities. The functionality of chlororespiratory electron transfer pathway under iron restricted conditions is also discussed.España, Ministerio de Economía y Competitividad BIO2012-35271España, Ministerio de Economía y Competitividad BIO2015-64169España, Ministerio de Economía y Competitividad BIO2013-4355

Photosystem I Reduction in Diatoms: As Complex as the Green Lineage Systems but Less Efficient

Diatoms occupy a key branch in the evolutionary tree of oxygen-evolving photosynthetic organisms. Here, the electron transfer reaction mechanism from cytochrome <i>c</i>₆ to photosystem I from the diatom <i>Phaeodactylum tricornutum</i> has been analyzed by laser-flash absorption spectroscopy. Kinetic traces of photosystem I reduction fit to biphasic curves, the analysis of the observed rate constants indicating that electron transfer occurs in a cytochrome <i>c</i>₆/photosystem I transient complex, which undergoes a reorganization process from the initial encounter complex to the optimized final configuration. The mild ionic strength dependence of the rate constants makes evident the relatively weak electrostatically attractive nature of the interaction. Taken together, these results indicate that the “red” <i>Phaeodactylum</i> system is less efficient than “green” systems, both in the formation of the properly arranged (cytochrome <i>c</i>₆/photosystem I) complex and in the electron transfer itself. The results obtained from cross-reactions with cytochrome <i>c</i>₆ and photosystem I from cyanobacteria, green algae, and plants shed light on the different evolutionary pathway of the electron transfer to photosystem I in diatoms with regard to the way that it evolved in higher plants

Interaction of photosystem I from Phaeodactylum tricornutum with plastocyanins as compared with its native cytochrome c6: Reunion with a lost donor

In the Phaeodactylum tricornutum alga, as in most diatoms, cytochrome c6 is the only electron donor to photosystem I, and thus they lack plastocyanin as an alternative electron carrier. We have investigated, by using laser-flash absorption spectroscopy, the electron transfer to Phaeodactylum photosystem I from plastocyanins from cyanobacteria, green algae and plants, as compared with its own cytochrome c6. Diatom photosystem I is able to effectively react with eukaryotic acidic plastocyanins, although with less efficiency than with Phaeodactylum cytochrome c6. This efficiency, however, increases in some green alga plastocyanin mutants mimicking the electrostatics of the interaction site on the diatom cytochrome. In addition, the structure of the transient electron transfer complex between cytochrome c6 and photosystem I from Phaeodactylum has been analyzed by computational docking and compared to that of green lineage and mixed systems. Taking together, the results explain why the Phaeodactylum system shows a lower efficiency than the green systems, both in the formation of the properly arranged [cytochrome c6-photosystem I] complex and in the electron transfer itself.Peer reviewe