Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas. - Test2 - elhamkhani - TriplyDB

Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

http://www.wikidata.org/entity/Q34309055

about

Origins and diversity of eukaryotic CO2-concentrating mechanisms: lessons for the future Systematically programmed adaptive evolution reveals potential role of carbon and nitrogen pathways during lipid accumulation in Chlamydomonas reinhardtii DNA barcoding to map the microbial communities: current advances and future directions.Native architecture of the Chlamydomonas chloroplast revealed by in situ cryo-electron tomography A step forward to building an algal pyrenoid in higher plants.A repeat protein links Rubisco to form the eukaryotic carbon-concentrating organelle Introducing an algal carbon-concentrating mechanism into higher plants: location and incorporation of key components.Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases.The CO2 concentrating mechanism and photosynthetic carbon assimilation in limiting CO2 : how Chlamydomonas works against the gradient.Pyrenoid loss impairs carbon-concentrating mechanism induction and alters primary metabolism in Chlamydomonas reinhardtii.Environmentally driven evolution of Rubisco and improved photosynthesis and growth within the C3 genus Limonium (Plumbaginaceae).Progress and challenges of engineering a biophysical carbon dioxide-concentrating mechanism into higher plants.The mechanisms whereby the green alga Chlorella ohadii, isolated from desert soil crust, exhibits unparalleled photodamage resistance.A newly isolated Chlorella sp. from desert sand crusts exhibits a unique resistance to excess light intensity.A reversible decrease in ribulose 1,5-bisphosphate carboxylase/oxygenase carboxylation activity caused by the aggregation of the enzyme's large subunit is triggered in response to the exposure of moderate irradiance-grown plants to low irradiance.Identification of Reference and Biomarker Proteins in Chlamydomonas reinhardtii Cultured under Different Stress Conditions The Eukaryotic CO2-Concentrating Organelle Is Liquid-like and Exhibits Dynamic Reorganization.Photosystem II photochemistry and phycobiliprotein of the red algae Kappaphycus alvarezii and their implications for light adaptation.Rubisco small subunits from the unicellular green alga Chlamydomonas complement Rubisco-deficient mutants of Arabidopsis Molecular aspects of the biophysical CO2-concentrating mechanism and its regulation in marine diatoms.Engineering photosynthesis: progress and perspectives.The algal pyrenoid: key unanswered questions.The Chlamydomonas CO2 -concentrating mechanism and its potential for engineering photosynthesis in plants.Regulatory components of carbon concentrating mechanisms in aquatic unicellular photosynthetic organisms.Overcoming adversity through diversity: aquatic carbon concentrating mechanisms.Pyrenoid loss in Chlamydomonas reinhardtii causes limitations in CO2 supply, but not thylakoid operating efficiency.Dynamics of carbon-concentrating mechanism induction and protein relocalization during the dark-to-light transition in synchronized Chlamydomonas reinhardtii.The carbon concentrating mechanism in Chlamydomonas reinhardtii: finding the missing pieces.Substitutions at the opening of the Rubisco central solvent channel affect holoenzyme stability and CO2/O 2 specificity but not activation by Rubisco activase.Activation of interspecies-hybrid Rubisco enzymes to assess different models for the Rubisco-Rubisco activase interaction.Pyrenoid functions revealed by proteomics in Chlamydomonas reinhardtii.Absolute Quantification of Major Photosynthetic Protein Complexes in Using Quantification Concatamers (QconCATs)

P2860

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P2860

Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

http://www.wikidata.org/entity/Q34309055

description

2012 nî lūn-bûn

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2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2012年の論文

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name

Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

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Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

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Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

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Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

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Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

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Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

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Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

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Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

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Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas.

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Proceedings of the National Academy of Sciences of the United States of America

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Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas

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Howard Griffiths

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Jeremy N Skepper

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Juliette Jouhet

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Moritz T Meyer

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Robert J Spreitzer

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Todor Genkov

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P2860

The Chlamydomonas genome reveals the evolution of key animal and plant functions.

Primary Production of the Biosphere: Integrating Terrestrial and Oceanic Components

Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized

A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions

First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii

Large structures at high resolution: the 1.6 A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate

Protein-based organelles in bacteria: carboxysomes and related microcompartments

To concentrate or ventilate? Carbon acquisition, isotope discrimination and physiological ecology of early land plant life forms

Bundle sheath leakiness and light limitation during C4 leaf and canopy CO2 uptake

Over-expression of the β-carboxysomal CcmM protein in Synechococcus PCC7942 reveals a tight co-regulation of carboxysomal carbonic anhydrase (CcaA) and M58 content

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Madeline C Mitchell

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