Note: Cover -- Title Page -- Copyright -- Contents -- Acknowledgements -- Chapter 1 Glacigenic Diamictons - A Rationale for Study -- Chapter 2 A Brief History of Till Research and Developing Nomenclature -- Chapter 3 Till - When is it an Inappropriate Term? -- Chapter 4 Glacigenic Diamictons: A Strategy for Field Description and Analysis -- 4.1 Diamicton -- 4.2 (Glacigenic) Melange -- 4.3 Physics of Material Behaviour -- 4.4 Typical Structures -- 4.5 Clast Macrofabrics and Microfabrics -- Chapter 5 Subglacial Sedimentary Processes: Origins of Till Matrix and Terminal Grade -- Chapter 6 Subglacial Sedimentary Processes: Modern Observations on Till Evolution -- 6.1 Lodgement, Lee-Side Cavity Filling and Ploughing -- 6.2 Deformation -- 6.3 Soft-Bed Sliding (Ice Keel Ploughing), Meltwater Drainage and Ice-Bed Decoupling -- 6.4 Melt-Out -- 6.5 Glacitectonite Production, Rafting and Cannibalisation -- Chapter 7 Subglacial Sedimentary Processes: Laboratory and Modelling Experiments on Till Evolution -- Chapter 8 Measuring Strain Signatures in Glacial Deposits -- Chapter 9 The Geological Record: Products of Lodgement, Cavity Fill and the Boulder Pavement Problem -- 9.1 Introduction - Repositioning Field Studies and Experimental Reductionism -- 9.2 Lodgement -- 9.3 Clast (Boulder) Pavements -- 9.4 Lee-side Cavity Fills -- Chapter 10 The Geological Record: Deforming Bed Deposits -- Chapter 11 The Geological Record: Sliding Bed Deposits -- Chapter 12 The Geological Record: Impacts of Pressurised Water (Clastic Dykes) -- Chapter 13 The Geological Record: Melt-out Till -- Chapter 14 The Geological Record: Glacitectonite -- Chapter 15 Glacial Diamictons Unrelated to Subglacial Processes -- Chapter 16 Till Spatial Mosaics, Temporal Variability and Architecture -- Chapter 17 Concluding Remarks: The Case for a Simplified Nomenclature -- References -- Index -- EULA.

Note: Intro -- Annual Plant Reviews Volume 46 -- Contents -- List of Contributors -- Preface -- Acknowledgements -- 1 Introduction: Mysteries, Molecules and Mechanisms -- 1.1 Darwin and Margulis revisited -- 1.2 Nuclei-general features -- 1.3 The plant nuclear genome -- 1.3.1 General features -- 1.3.2 Replication of the nuclear genome -- 1.4 DNA inside, ribosomes outside -- 1.5 Concluding comments on the evolution of the nucleus -- References -- 2 The Nuclear Envelope-Structure and Protein Interactions -- 2.1 Introduction -- 2.2 Organization and structure of the plant nuclearenvelope -- 2.3 Proteins of the plant nuclear envelope -- 2.3.1 Proteins involved in signalling -- 2.3.2 Proteins of the nuclear pore complex -- 2.3.3 Proteins of the INM -- 2.3.4 Proteins spanning the periplasm and linking the NE membranes -- 2.3.5 The plant lamina -- 2.4 The plant nuclear envelope and the nucleoskeleton -- attachments at the INM -- 2.5 The plant nuclear envelope and the cytoskeleton -- attachments at the ONM -- 2.6 Targeting of proteins to the plant NE -- 2.7 Nuclear envelope protein dynamics in mitosis -- 2.7.1 The role of NPC in regulating NE dynamics in cell division -- 2.7.2 NE protein dynamics in division -- 2.8 The phragmoplast and cell plate and their relationship to the NE -- 2.9 The plant NE in meiosis -- 2.10 Lipid composition of the plant NE and its homeostasis -- 2.10.1 Nuclear-vacuolar junctions and lipid homeostasis -- 2.10.2 NE phospholipid regulation by lipins -- 2.11 The role of plant NE components in stress responses -- 2.11.1 Nuclei repositioning in response to environmental stimuli -- 2.11.2 Functions of the plant NE during viral infection -- 2.12 Concluding remarks -- Acknowledgements -- References -- 3 The Plant Nuclear Pore Complex - The Nucleocytoplasmic Barrierand Beyond -- 3.1 Nuclear pore complex structure -- 3.1.1 Structure of the NPC. , 3.1.2 Molecular composition of the NPC -- 3.1.3 Nucleocytoplasmic trafficking -- 3.1.3.1 Karyopherins and Ran cycle -- 3.1.3.2 Non-karyopherin transport -- 3.1.3.3 Models explaining 'virtual gating' of the NPC -- 3.2 Physiological and developmental roles of plant nuclear pore components -- 3.2.1 Plant-microbe interactions -- 3.2.2 Hormone responses -- 3.2.2.1 Abscisic acid signalling -- 3.2.2.2 Auxin signalling -- 3.2.3 Abiotic stress responses -- 3.2.3.1 Temperature stress -- 3.2.3.2 Salt and osmotic stress -- 3.2.4 Growth and development -- 3.3 The Dynamics of the Nuclear Pore Complex -- 3.3.1 Types of mitosis -- 3.3.2 NPC disassembly and dynamics of animal NPC components -- 3.3.3 Dynamics of fungal NPC components -- 3.3.4 Dynamics of plant NPC components -- 3.4 Conclusions -- References -- 4 Nucleoskeleton in Plants: The Functional Organization of Filaments in the Nucleus -- 4.1 Introduction -- 4.2 Intermediate filaments and the nucleoskeleton -- 4.3 Plants do not have intermediate filaments but they may have functional equivalents -- 4.4 Plants can evolve different solutions to the same problem -- 4.5 Intermediate filaments first evolved in the nucleus -- 4.6 Plants require a rigid nuclear boundary -- 4.7 Is there a trans-nuclear envelope complex in plants that links the nucleoskeleton to the cytoskeleton? -- 4.8 Role of the nuclear lamina as part of the nucleoskeleton -- 4.9 Structural evidence for the nucleoskeleton -- 4.10 NuMA in plants -- 4.11 Matrix attachment regions (MARs) and the role of the nucleoskeleton in chromatin organization -- 4.12 Chromocentres and the plant nucleoskeleton -- 4.13 Long coiled-coil proteins in plants and their role in nuclear organization: candidates for plamins and nucleoskeletal proteins? -- 4.14 Actin and microtubules in the nucleus -- 4.15 Conclusions -- Acknowledgements -- References. , 5 Genomics and Chromatin Packaging -- 5.1 Chromatin components and structure in highereukaryotes -- 5.2 Histones and nucleosome fibre -- 5.2.1 Histone variants -- 5.2.2 Histone modifications -- 5.2.3 Nucleosome dynamics -- 5.3 Linker histone and the higher order chromatin-order fibre -- 5.3.1 The elusive higher order chromatin fibre -- 5.4 Chromatin loops and chromosome axis -- 5.5 Conclusions and future prospects -- References -- 6 Heterochromatin Positioning and Nuclear Architecture -- 6.1 Heterochromatin structure -- 6.1.1 Heterochromatic sequences -- 6.1.2 Epigenetic marks -- 6.1.2.1 DNA methylation -- 6.1.2.2 Histone code -- 6.1.2.3 Histone-repressive marks -- 6.1.2.4 Histone-activating marks -- 6.1.2.5 Histone variants -- 6.1.2.6 Non-coding RNA -- 6.1.3 Non-histone protein binding -- 6.1.4 Heterochromatin is an epigenetic state -- 6.2 Heterochromatin organization -- 6.2.1 Heterochromatin and nuclear architecture -- 6.2.1.1 Chromosome territories in Arabidopsis -- 6.2.1.2 Chromocentres and the rosette-loop model of chromatin organization -- 6.2.1.3 Chromatin organization in large genome species -- 6.2.2 Recruitment of heterochromatin at the nuclear periphery -- 6.2.2.1 The central role of lamins in animals -- 6.2.2.2 The inner nuclear membrane and heterochromatin -- 6.2.2.3 Heterochromatin positioning in plants -- 6.2.3 Higher order of chromatin organization -- 6.2.3.1 Boundary elements -- 6.2.3.2 Condensin and cohesin -- 6.2.3.3 Matrix Attachment Regions -- 6.2.3.4 Future prospects in plants -- 6.3 Functional significance of heterochromatin positioning -- 6.3.1 Centric heterochromatin directs chromosome segregation -- 6.3.2 Spatial positioning of heterochromatin affects transcriptional activity -- 6.3.3 Heterochromatin positioning protects against genomeinstability -- 6.4 Perspectives -- Acknowledgements -- References. , 7 Telomeres in Plant Meiosis: Their Structure, Dynamics and Function -- 7.1 Introduction -- 7.1.1 The meiotic pathway -- 7.1.2 Arabidopsis thaliana as a model for meiosis -- 7.2 The telomeres and associated proteins -- 7.2.1 Telomere binding proteins -- 7.2.2 Arabidopsis telomere binding proteins -- 7.2.3 DNA repair proteins -- 7.3 The behaviour of the telomeres in meiosis -- 7.3.1 The bouquet -- 7.3.2 A role for the bouquet -- 7.4 Telomere dynamics in Arabidopsis thaliana meiosis -- 7.4.1 Meiosis in A. thaliana telomere-deficient lines -- 7.5 How are the telomeres moved in meiotic prophase I? -- 7.5.1 Colchicine disrupts meiotic progression -- 7.5.2 The role of actin in telomere movement -- 7.6 Components of the nuclear envelope -- 7.7 Components of the plant nuclear envelope -- 7.8 Conclusions and future prospects -- Acknowledgements -- References -- 8 The Nuclear Pore Complex in Symbiosis and Pathogen Defence -- 8.1 Introduction -- 8.2 The nuclear pore and plant-microbe symbiosis -- 8.2.1 Common signalling in arbuscular mycorrhiza and root-nodule symbiosis -- 8.2.2 Symbiotic signalling at the nucleus -- 8.2.3 Symbiotic defects in ljnup85, ljnup133 and nena mutants -- 8.2.4 How do nucleoporins function in plant-microbe symbiosis? -- 8.3 The nuclear pore and plant defence -- 8.3.1 Plant immune responses can be triggered by pathogen-associated molecular patterns and microbial effectors -- 8.3.2 AtNUP88 and AtNUP96 are required for basal and NB-LRR-mediated plant immunity -- 8.3.3 Mechanisms of nucleoporin-mediated plant defence signalling -- 8.4 Specificity, redundancy and general functions of plant nucleoporins -- 8.4.1 The NUP107-160 sub-complex -- 8.4.2 Hormone signalling -- 8.4.3 Development, flowering time, stress tolerance and RNA transport -- 8.5 Challenges and conclusion -- References -- Index -- Supplemental Images.