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  • 1
    Online Resource
    Online Resource
    New York, NY :Springer,
    Keywords: Plastids. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (585 pages)
    Edition: 1st ed.
    ISBN: 9781493911363
    Series Statement: Advances in Plant Biology Series ; v.5
    DDC: 571.659
    Language: English
    Note: Intro -- Preface -- Contents -- Contributors -- Part I -- Genetic Material and its Expression -- Chapter 1 -- Chloroplast Gene Expression-RNA Synthesis and Processing -- 1.1 Introduction -- 1.2 RNA Synthesis -- 1.2.1 The Plastid-Encoded Plastid RNA Polymerase (PEP) is a Bacteria-Type Multisubunit RNA Polymerase -- 1.2.2 PEP Promoters -- 1.2.3 The Nuclear-Encoded Plastid RNA Polymerase (NEP) is Represented by Phage-Type RNA Polymerases -- 1.2.4 NEP Promoters -- 1.2.5 Division of Labor among Different Plastid RNA Polymerases -- 1.3 RNA Processing -- 1.3.1 Chloroplast RNA Splicing -- 1.3.1.1 Chloroplast Introns and Factors -- 1.3.1.2 Regulation of Chloroplast RNA Splicing -- 1.3.2 Chloroplast RNA Editing -- 1.3.2.1 Chloroplast RNA Editing Sites and Factors -- 1.3.2.2 Regulation of Chloroplast RNA Editing -- 1.3.3 RNA Cleavage and Degradation -- 1.3.3.1 Chloroplast RNases -- 1.3.3.2 Intercistronic mRNA Processing -- 1.3.3.3 Regulation of RNA Degradation -- 1.3.4 RNA Processing: Outlook -- References -- Chapter 2 -- Chloroplast Gene Expression-Translation -- 2.1 Introduction -- 2.2 Technical Considerations for Measuring Translational Activities in Chloroplasts -- 2.2.1 Genetic Approaches -- 2.2.1.1 Model Organisms -- 2.2.1.2 Chloroplast Reporter Genes -- 2.2.2 Measurement of in vivo Protein Synthesis -- 2.2.2.1 Pulse Labelling of Proteins -- 2.2.2.2 Polysomal Loading -- 2.2.3 Reconstituted Systems -- 2.2.3.1 In Vitro Translation Systems -- 2.2.3.2 RNA Binding Assays -- 2.3 Constituents of the Chloroplast Translational Apparatus -- 2.3.1 Basic Elements and Factors -- 2.3.1.1 Chloroplast tRNAs and Codon Usage -- 2.3.1.2 Chloroplast Ribosomes and General Translation Factors -- 2.3.1.3 Shine-Dalgarno Sequences and Start Codon Recognition -- 2.3.2 Gene Specific Elements and Factors for Translation Initiation. , 2.3.2.1 Cis-acting Signals on Chloroplast RNAs -- 2.3.2.2 Nucleus-Encoded Factors for Chloroplast Translation -- 2.4 Regulatory Principles of Chloroplast Translation -- 2.4.1 Regulation by Light and Redox/Metabolic Status -- 2.4.1.1 psbA mRNA Translation -- 2.4.1.2 psbD mRNA Translation -- 2.4.1.3 rbcL mRNA Translation -- 2.4.1.4 psaB mRNA Translation -- 2.4.2 Regulation of Translation via Interconnected Steps of Gene Expression -- 2.5 Spatial Organization of Chloroplast Translation -- 2.6 Conclusions and Future Perspectives -- References -- Chapter 3 -- The Chloroplast Genome and Nucleo-Cytosolic Crosstalk -- 3.1 Introduction -- 3.2 Nucleus-Encoded Trans-Acting Factors Involved in Chloroplast Gene Expression -- 3.2.1 Chloroplast Transcription Factors -- 3.2.2 Factors Involved in Post-Transcriptional Steps of Chloroplast Gene Expression -- 3.2.3 CES Control -- 3.2.4 Redox Control of Post-Transcriptional Steps of Chloroplast Gene Expression -- 3.3 Retrograde Signaling -- 3.3.1 Role of Tetrapyrroles in Retrograde Signaling -- 3.3.2 Plastid Protein Synthesis and Retrograde Signaling -- 3.3.3 Chloroplast Redox Changes and Retrograde Signaling -- 3.3.4 Reactive Oxygen Species Involved in Retrograde Signaling -- 3.3.5 Additional Metabolites Involved in Retrograde Signaling during Stress Responses -- 3.3.6 Repressible Chloroplast Gene Expression in Chlamydomonas -- 3.4 Conclusions and Perspectives -- References -- Part II -- Plastid Differentiation -- Chapter 4 -- An Overview of Chloroplast Biogenesis and Development -- 4.1 Introduction -- 4.2 Chloroplast Biogenesis -- 4.3 Plastidic and Nuclear Factors Required for Chloroplast Biogenesis -- 4.3.1 Nuclear Transcription -- 4.3.2 Chloroplast Gene Transcription and Translation -- 4.3.3 Protein Import and Processing -- 4.3.4 Pigment Biosynthesis -- 4.3.5 Retrograde Signalling -- 4.3.6 Chloroplast Division. , 4.4 Temporal and Cellular Factors Required for Chloroplast Biogenesis and Development -- 4.5 Future Directions -- References -- Chapter 5 -- Dynamic Architecture of Plant Photosynthetic Membranes -- 5.1 Introduction -- 5.2 Overall Thylakoid Architecture -- 5.2.1 Structural Organization of Grana Thylakoids -- 5.2.1.1 Grana Diameter -- 5.2.1.2 Grana Distribution in Chloroplasts -- 5.2.1.3 Transversal Grana Structure -- 5.2.2 Flexibility of the Grana Architecture -- 5.2.2.1 Classification of Structural Changes in the Grana Architecture -- 5.2.2.2 Lateral Changes in Grana Diameter (Fig. 5.1b) -- 5.2.2.3 Swelling of Thylakoid Lumen (Fig. 5.1c) -- 5.2.2.4 Vertical Destacking of Grana (Fig. 5.1d) -- 5.3 The Supramolecular Level -- 5.3.1 Macromolecular Crowding -- 5.3.2 Disordered Versus Ordered -- 5.3.3 Functional Significance of Protein Ordering -- 5.3.4 Stroma Lamellae -- 5.4 Outlook -- References -- Chapter 6 -- Plastid Division -- 6.1 Introduction -- 6.2 Placement of the Plastid Division Site -- 6.2.1 Many Proteins are Involved in the Choice of the Division Site -- 6.2.2 How Do Proteins Involved in the Choice of the Division Site Work Together? -- 6.3 Assembly and Dynamics of the FtsZ Ring -- 6.3.1 Z-ring Assembly Requires Two Isoforms of FtsZ -- 6.3.2 Opposing Roles of ARC6 and PARC6 on Z-Ring Formation -- 6.3.3 Chaperone-Regulation of Z-Ring Assembly/Maintenance -- 6.4 Assembly of the Plastid Division Machinery -- 6.4.1 The Plastid Dividing Rings -- 6.4.2 PDV1, PDV2 and Dynamin Recruitment to the Division Site -- 6.5 Constriction and Separation of Chloroplasts -- 6.5.1 Force Generation by the Stromal Plastid Division Machinery -- 6.5.2 Force Generation by the Cytosolic Plastid Division Machinery -- 6.6 Regulation of Plastid Division -- 6.6.1 Regulation During Cell Proliferation -- 6.6.2 Plastid Division and Plastid DNA Replication. , 6.6.3 Plastid Division Is Regulated by Cell Differentiation, and Cell Expansion -- 6.6.4 Chloroplast Division Is Regulated by Exogenous Cues -- References -- Chapter 7 -- Stromules -- 7.1 Introduction -- 7.2 Initial Observations of Stromule-Like Structures in Plants -- 7.2.1 Stromules in Different Cells and Tissues -- 7.2.2 Initial Observations of Stromules in Virus Infected Tissue -- 7.2.3 Stromules are Dynamic -- 7.2.4 Extension and Retraction Rates -- 7.3 Visualization of Stromules -- 7.3.1 Differential Interference Contrast (DIC) Imaging of Stromules -- 7.3.2 Fluorescent Protein Markers and Confocal Microscopy -- 7.3.3 Transmission Electron Microscopy (TEM) and Cryo-fixation of Stromules -- 7.4 Origin, Formation and Regulation of Stromule Formation -- 7.4.1 Chloroplast Envelope -- 7.4.2 Actin and Microtubule Requirements -- 7.5 Induction and Regulation of Stromules -- 7.5.1 Abiotic Stress Responses -- 7.5.2 Biotic Stress Defense Response -- 7.5.3 ABA and H2O2-Mediated Induction of Stromules -- 7.6 Putative Functions of Stromules -- 7.6.1 Increased Chloroplast Surface Area -- 7.6.2 Intra- and Inter-organelle Trafficking -- 7.6.3 Signaling -- 7.6.4 Starch Granule Formation -- 7.7 Future Insights -- References -- Chapter 8 -- The Apicoplast: A Parasite's Symbiont -- 8.1 Introduction -- 8.1.1 What are Apicomplexans? -- 8.1.2 Obligate Intracellular Parasites with a Plastid -- 8.2 Apicoplast Origin and Evolution -- 8.2.1 Metamorphosis of an Alga -- 8.2.2 The Origin of the Apicoplast: The Red Versus Green Debate -- 8.2.3 Was the Red Algal Acquisition a Unique Event in the History of Evolution? -- 8.2.4 Chromera velia, a (No Longer) Missing Link -- 8.3 Apicoplast Biogenesis -- 8.3.1 Import of Nuclear-encoded Proteins to various Apicoplast Destinations -- 8.3.2 Targeting Signals -- 8.3.3 Crossing the Borders -- 8.3.3.1 The Two Innermost Membranes. , 8.3.3.2 The Second Outermost Membrane -- 8.3.3.3 The Outermost Membrane -- 8.3.4 Organelle Replication and Division-Drug Targets Beyond Metabolism -- 8.3.4.1 Apicoplast Genome Replication and Gene Translation -- 8.3.4.2 Division of the Apicoplast Organelle -- 8.4 Metabolic Functions of the Apicoplast -- 8.4.1 The Apicoplast's Function is Anabolic Metabolism -- 8.4.2 Type II Fatty Acid Synthesis (FASII) -- 8.4.3 Heme Biosynthesis -- 8.4.4 Iron-sulfur Clusters and Isoprenoids -- 8.4.5 Transport of Metabolites -- 8.5 Conclusion -- References -- Part III -- Biogenesis of Chloroplast Proteins -- Chapter 9 -- Mechanisms of Chloroplast Protein Import in Plants -- 9.1 Introductory Topics -- 9.1.1 Background -- 9.1.2 Transit Peptides -- 9.1.3 Energetics and Stages of Import -- 9.1.4 Identification of Translocon Components -- 9.2 Translocation Across the Outer Membrane -- 9.2.1 Components of the TOC Complex -- 9.2.2 TOC Components in Arabidopsis thaliana -- 9.2.3 TOC Complexes -- 9.2.4 Cytosolic Factors and Regulators of Chloroplast Protein Import -- 9.3 Translocation Across the Inner Membrane -- 9.3.1 Arrival and Conductance -- 9.3.2 Import Propulsion -- 9.3.3 Redox Regulation -- 9.3.4 Transit Peptide Cleavage -- 9.4 Targeting to the Envelope Membranes -- 9.4.1 Sorting to the Outer Membrane -- 9.4.2 Sorting to the Intermembrane Space and Inner Membrane -- 9.5 Alternative Protein Import Pathways -- 9.5.1 Dual-Targeting -- 9.5.2 Non-canonical Protein Transport -- 9.6 Concluding Remarks -- References -- Chapter 10 -- Protein Routing Processes in the Thylakoid -- 10.1 Overview of Conservative Protein Sorting to the Thylakoid Membrane and Lumen -- 10.2 The Sec and SRP Transport Pathways in Chloroplasts -- 10.2.1 cpSec Transport -- 10.2.2 cpSRP Transport -- 10.2.3 A Second Sec System -- 10.3 The Twin Arginine Transport (Tat) Pathway in Chloroplasts. , 10.3.1 Introduction.
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  • 2
    Online Resource
    Online Resource
    San Diego :Elsevier Science & Technology,
    Keywords: Chlamydomonas. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (866 pages)
    Edition: 3rd ed.
    ISBN: 9780323910583
    DDC: 579.832
    Language: English
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 7468-7475 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-5028
    Keywords: Chlamydomonas reinhardtii ; chloroplast gene expression ; insertional mutagenesis ; cytochrome b6f complex ; nuclear-encoded factors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The random integration of transforming DNA into the nuclear genome of Chlamydomonas has been employed as an insertional mutagen to generate a collection of photosynthetic mutants that display abnormal steady-state fluorescence levels and an acetate-requiring phenotype. Electron paramagnetic resonance spectroscopy was then used to identify those mutants that specifically lack a functional cytochrome b6f complex. Our analysis of RNA and protein synthesis in five of these mutants reveals four separate phenotypes. One mutant fails to accumulate transcript for cytochrome f, whilst a second displays a severely reduced accumulation of the cytochrome b6 transcript. Two other mutants appear to be affected in the insertion of the haem co-factor into cytochrome b6. The fifth mutant displays no detectable defect in the synthesis of any of the known subunits of the complex. Genetic analysis of the mutants demonstrates that in three cases, the mutant phenotype co-segregates with the introduced DNA. For the mutant affected in the accumulation of the cytochrome f transcript, we have used the introduced DNA as a tag to isolate the wild-type version of the affected gene.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Planta 183 (1991), S. 423-433 
    ISSN: 1432-2048
    Keywords: Chlamydomonas (light-harvesting complexes) ; Chlorophyll a/b protein (chlamydomonas) ; Light-harvesting complex
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have adapted the procedure for the isolation of PSII membranes from higher plants (D.A. Berthold et al., 1981, FEBS Lett. 134, 231–234) to the green algae Chlamydomonas reinhardtii. The chlorophyll (Chl)-binding proteins from this PSII preparation have been further separated into single Chl-binding polypeptides and characterized spectroscopically. Seven single polypeptides were shown to bind Chl a and Chl b. In particular, we demonstrate that polypeptides p9, p10 and p22, which had not been previously shown to bind Chl a and b, have characteristics similar to those of CP29, CP26 and CP24 from higher plants. We note, however, that p9 and p10 are phosphorylatable in C. reinhardtii, at variance with CP29 and CP26 from higher plants. Our data support the notion that the PSII antenna systems in C. reinhardtii and in higher plants are very similar. Therefore, studies on the organization and regulation of light-harvesting processes in C. reinhardtii may provide information of general relevance for both green algae and higher plants.
    Type of Medium: Electronic Resource
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