RESUMEN
The moss Physcomitrella patens is an important model organism for studying plant evolution, development, physiology and biotechnology. Here we have generated microarray gene expression data covering the principal developmental stages, culture forms and some environmental/stress conditions. Example analyses of developmental stages and growth conditions as well as abiotic stress treatments demonstrate that (i) growth stage is dominant over culture conditions, (ii) liquid culture is not stressful for the plant, (iii) low pH might aid protoplastation by reduced expression of cell wall structure genes, (iv) largely the same gene pool mediates response to dehydration and rehydration, and (v) AP2/EREBP transcription factors play important roles in stress response reactions. With regard to the AP2 gene family, phylogenetic analysis and comparison with Arabidopsis thaliana shows commonalities as well as uniquely expressed family members under drought, light perturbations and protoplastation. Gene expression profiles for P. patens are available for the scientific community via the easy-to-use tool at https://www.genevestigator.com. By providing large-scale expression profiles, the usability of this model organism is further enhanced, for example by enabling selection of control genes for quantitative real-time PCR. Now, gene expression levels across a broad range of conditions can be accessed online for P. patens.
Asunto(s)
Bryopsida/crecimiento & desarrollo , Bryopsida/genética , Regulación de la Expresión Génica de las Plantas , Estrés Fisiológico/genética , Transcriptoma/genética , Bryopsida/fisiología , Perfilación de la Expresión Génica , Filogenia , Reacción en Cadena en Tiempo Real de la PolimerasaRESUMEN
We demonstrate that the self-assembly in polar media and gelation of an amphiphilic Pd(II) complex with pendant chlorine ligands are governed by cooperative intra- and interstrand CH···O interactions between peripheral triethylene glycol chains leading to slipped π-stacks.
Asunto(s)
Glicoles/química , Compuestos Organometálicos/síntesis química , Paladio/química , Tensoactivos/síntesis química , Ligandos , Modelos Moleculares , Estructura Molecular , Compuestos Organometálicos/química , Tensoactivos/químicaRESUMEN
Chloroplasts and bacterial cells divide by binary fission. The key protein in this constriction division is FtsZ, a self-assembling GTPase similar to eukaryotic tubulin. In prokaryotes, FtsZ is almost always encoded by a single gene, whereas plants harbor several nuclear-encoded FtsZ homologs. In seed plants, these proteins group in two families and all are exclusively imported into plastids. In contrast, the basal land plant Physcomitrella patens, a moss, encodes a third FtsZ family with one member. This protein is dually targeted to the plastids and to the cytosol. Here, we report on the targeted gene disruption of all ftsZ genes in P. patens. Subsequent analysis of single and double knockout mutants revealed a complex interaction of the different FtsZ isoforms not only in plastid division, but also in chloroplast shaping, cell patterning, plant development, and gravity sensing. These results support the concept of a plastoskeleton and its functional integration into the cytoskeleton, at least in the moss P. patens.
Asunto(s)
Bryopsida/genética , Técnicas de Inactivación de Genes/métodos , Secuencia de Bases , Bryopsida/enzimología , Bryopsida/metabolismo , Cloroplastos/genética , Cloroplastos/metabolismo , Cartilla de ADN , GTP Fosfohidrolasas/genética , GTP Fosfohidrolasas/metabolismo , Fenotipo , Filogenia , Proteínas de Plantas/genética , Proteínas de Plantas/metabolismo , Reacción en Cadena de la Polimerasa , Transcripción GenéticaRESUMEN
FtsZ is a filament-forming protein that assembles into a ring at the division site of prokaryotic cells. As FtsZ and tubulin share several biochemical and structural similarities, FtsZ is regarded as the ancestor of tubulin. Chloroplasts--the descendants of endosymbiotic bacteria within plant cells--also harbour FtsZ. In contrast to eubacteria, plants have several different FtsZ isoforms. So far, these isoforms have only been implicated with filamentous structures, rings and networks, inside chloroplasts. Here, we demonstrate that a novel FtsZ isoform in the moss Physcomitrella patens is located not only in chloroplasts but also in the cytoplasm, assembling into rings in both cell compartments. These findings comprise the first report on cytosolic localization of a eukaryotic FtsZ isoform, and indicate that this protein might connect cell and organelle division at least in moss.