azolla caroliniana/cariës

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The pore of the leaf cavity of Azolla species: teat cell differentiation and cell wall projections.

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The differentiation of the specialized secretory teat cells of the leaf cavity pore of Azolla species was investigated at the ultrastructural level with emphasis on their peculiar cell wall projections. The results indicated that the projections are formed as soon as the teat cells complete their

Identification of eubacteria isolated from leaf cavities of four species of the N-fixing azolla fern as arthrobacter conn and dimmick.

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The nutritional and physiological characteristics of 15 isolates from four species of the Azolla fern were determined. Although some minor variation existed in levels of urease activity, ability to utilize xylose, and formation of N(2) gas from NO(3), all 15 isolates were rather similar and believed

Indole-3-acetic acid (IAA) production by Arthrobacter species isolated from Azolla.

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Arthrobacter species, isolated from the leaf cavities and the microsporocarps of the aquatic fern species Azolla pinnata and Azolla filiculoides, produced indole-3-acetic acid (IAA) in culture when the precursor tryptophan was added to the medium. No IAA production was detected in the absence of

Quantitative and qualitative DNA variations in Anabaena azollae Strasb. living in Azolla filiculoides lam.

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Heterocysts and vegetative cells of the filamentous nitrogen-fixing Anabaena azollae isolated from the apex to the basal leaf cavities of Azolla filiculoides were examined by epifluorescent microscope after fluorochrome staining. Acridine orange (AO), DAPI, and chromomycin fluorochromes were used in

Identification of a common cyanobacterial symbiont associated with Azolla spp. through molecular and morphological characterization of free-living and symbiotic cyanobacteria.

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Symbiotically associated cyanobacteria from Azolla mexicana and Azolla pinnata were isolated and cultured in a free-living state. Morphological analyses revealed differences between the free-living isolates and their symbiotic counterparts, as did restriction fragment length polymorphism (RFLP)

Azolla-Anabaena symbionts and microbial mat as nitrogen-fixing biocatalysts for bioregenerative space life support.

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This study was conducted to characterize the responses of selected nitrogen-fixing biocatalysts to various environmental parameters that are likely to be encountered in a scaled-up nitrogen-fixing bioregenerative unit for use in a biologically based life support system (BLSS). The results showed

Effects of lead accumulation on the Azolla caroliniana-Anabaena association.

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The effect of lead accumulation on photopigment production, mineral nutrition, and Anabaena vegetative cell size and heterocyst formation in Azolla caroliniana was investigated. Plants were exposed to 0, 1, 5, 10, and 20 mg L(-1) lead acetate for ten days. Lead accumulation increased when plants

Occurrence and ultrastructural characterization of bacteria in association with and isolated from Azolla caroliniana.

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The occurrence and ultrastructure of bacteria in leaf cavities of symbiotic Azolla caroliniana were examined by transmission electron microscopy. Bacteria were observed in all leaf cavities of Azolla cultures. Five ultrastructurally distinct types of bacteria were observed in each individual leaf

Immunocytochemical localization of nitrogenase in bacteria symbiotically associated with Azolla spp.

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In situ immunogold labeling and transmission electron microscopy were used to detect nitrogenase in bacteria (bactobionts) symbiotically associated with leaf cavities of Azolla caroliniana and Azolla filiculoides. In A. caroliniana, the Fe protein of the nitrogenase complex was detected in a subset

Occurrence of the 32-kDa QB-binding protein of photosystem II in vegetative cells, dheterocysts and akinetes of Azolla carotiniana cyanobionts.

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Transmission electron microscopy and immunocytological labeling were used to localize the 32-kilodalton (kDa) protein (DI polypeptide) of photosystem II in different cell types of the cyanobionts within leaf cavities of Azolla caroliniana Willd. The 32-kDa protein binds the secondary electron

The Azolla, Anabaena azollae Relationship: I. Initial Characterization of the Association.

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Cultures of Azolla caroliniana Willd. free of the symbiotic blue-green alga, Anabaena azollae, were obtained by treatment of Azolla fronds with a regimen of antibiotics. These symbiontfree plants can be maintained only on medium containing a combined nitrogen source.Morphological aspects of the

Proteomic analysis of the cyanobacterium of the Azolla symbiosis: identity, adaptation, and NifH modification.

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Cyanobacteria are able to form stable nitrogen-fixing symbioses with diverse eukaryotes. To extend our understanding of adaptations imposed by plant hosts, two-dimensional gel electrophoresis and mass spectrometry (MS) were used for comparative protein expression profiling of a cyanobacterium

The Azolla-Anabaena azollae Relationship : XII. Nitrogenase Activity and Phycobiliproteins of the Endophyte as a Function of Leaf Age and Cell Type.

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Nitrogenase activity was measured in leaves along the main stem axes of Azolla pinnata R. Br. The activity was negligible in leaves of the apical region, rapidly increased to a maximum as leaves matured, and declined in aging leaves. In situ absorption and fluorescence emission spectra were obtained

Inhibition of nitrogen-fixing activity of the cyanobiont affects the localization of glutamine synthetase in hair cells of Azolla.

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In the Azolla-Anabaena association, the host plant Azolla efficiently incorporates and assimilates ammonium ions that are released from the nitrogen-fixing cyanobiont, probably via glutamine synthetase (GS; EC 6.3.1.2) in hair cells, which are specialized cells protruding into the leaf cavity. In

Differences in mRNA levels in Anabaena living freely or in symbiotic association with Azolla.

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Azolla is a small water fern in whose leaf cavities the filamentous nitrogen-fixing cyanobacterium Anabaena azollae is symbiotically associated. Using cloned genes from Anabaena 7120 for glutamine synthetase (GS), ribulose-1,5-bisphosphate (RuBP) carboxylase, nitrogenase and the 32-kd protein of

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