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Balance of power – dynamic regulation of chromatin in plant development
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Marcel Lafos
Veröffentlicht/Copyright:
13. September 2009
Abstract
Chromatin states profoundly determine and maintain gene activity and gene repression in eukaryotic organisms. Regulation of chromatin involves chromatin remodeling, chromatin modifications and exchange of chromatin components and is linked to DNA methylation in some cases. In plants and other organisms, chromatin proteins control many developmental pathways, integrate changes in the environment and can confer a cellular memory of these cues. Here, we review the molecular mechanisms that provide a dynamic regulation of chromatin in a cell. In addition, we discuss how chromatin needs to be flexibly regulated during plant growth to confer stable expression states that can occasionally be reset, e.g., owing to changes in the environment and progression of development.
Received: 2009-5-2
Accepted: 2009-8-11
Published Online: 2009-09-13
Published in Print: 2009-11-01
©2009 by Walter de Gruyter Berlin New York
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Schlagwörter für diesen Artikel
epigenetics;
flowering;
histone methylation;
plant;
Polycomb;
Trithorax
Artikel in diesem Heft
- Editorial
- Highlight: Molecular and Cellular Mechanisms of Memory
- Highlight: 60th Mosbach Colloquium of the GBM ‘Molecular and Cellular Mechanisms of Memory’
- Protein carboxyl methylation and the biochemistry of memory
- Chemotaxis: how bacteria use memory
- Mechanistic insights in light-induced cAMP production by photoactivated adenylyl cyclase alpha (PACα)
- Balance of power – dynamic regulation of chromatin in plant development
- Ultrafast memory loss and relaxation processes in hydrogen-bonded systems
- Memory and neural networks on the basis of color centers in solids
- Dissection of gene regulatory networks in embryonic stem cells by means of high-throughput sequencing
- The epigenetic bottleneck of neurodegenerative and psychiatric diseases
- Protein Structure and Function
- Mechanism of activation of Saccharomyces cerevisiae calcineurin by Mn2+
- Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation
- Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg257/Lys260, and unmasking of acid-base catalysis
- Genes and Nucleic Acids
- CA/C1 peptidases of the malaria parasites Plasmodium falciparum and P. berghei and their mammalian hosts – a bioinformatical analysis
- Proteolysis
- Placental expression of proteases and their inhibitors in patients with HELLP syndrome
- Irreversible inhibition of human cathepsins B, L, S and K by hypervalent tellurium compounds
