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PubMed1993

Five Nodulation Mutants of White Sweetclover (Melilotus alba Desr.) Exhibit Distinct Phenotypes Blocked at Root Hair Curling, Infection Thread Development, and Nodule Organogenesis.

In an effort to obtain a developmental sequence of mutations in the Rhizobium-legume interaction within a single legume species, we have characterized the early events of nodule development in 10 nodulation mutants of sweetclover, Melilotus alba Desr. cv U389, representing five genetic loci. Both seed and root exudates from all of the sweetclover mutants induced expression of the nod genes of Rhizobium meliloti. Mutants in three loci were blocked in the early stages of root hair curling. Of these, a mutant in the sym-3 locus exhibited root hair deformations in response to inoculation with R. meliloti but produced no nodules or emerging nodule primordia, suggesting a blockage in the signal transduction events leading to nodule organogenesis. In contrast, mutants in both the sym-1 and sym-5 loci formed ineffective nodules in response to inoculation but differed slightly in the type of root hair response observed. None of these three early mutants formed infection threads. Infection threads were observed in mutant sym-2 as well as in ineffective nodules. Mutant sym-4 also formed infection threads but lacked nodules. The phenotypes observed for mutants from these five loci suggest that a secondary receptor or signal produced by the plant is required for nodule development.

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PubMed1993

Two Sweetclover (Melilotus alba Desr.) Mutants Temperature Sensitive for Chlorophyll Expression.

The nonallelic sweetclover (Melilotus alba Desr.) mutants U371 (ch10/ch10 genotype) and U372 (ch11/ch11 genotype) are derived from the U389 (+/+ genotype) parental strain. Growth of the U389 strain at a temperature of 17 or 26[deg]C results in plants normally green in appearance. The U371 and U372 mutant plants grown at 26[deg]C are slightly to moderately chlorophyll (Chl) deficient and have decreased Chl b/a ratios. Growth of the mutants at 17[deg]C results in plants severely deficient in Chl a, with markedly reduced levels of carotenoids except for violaxanthin, and with negligible amounts of Chl b or apoproteins for the light-harvesting complex of photosystem II. If mutant plants grown at 17[deg]C are transferred to 26[deg]C, during the next 20 d the amount of Chl per fresh weight will increase 5-fold and both the Chl b/a ratio and the expression of the light-harvesting complex apoproteins will progressively increase. Studies of the U371 mutant during the temperature-induced greening demonstrate progressive changes in chloroplast ultra-structure and leaf carbon isotope fractionation that parallel the increases in Chl. Changes observed in the leaf carbon isotope fractionation in the mutant suggest that, in addition to the already known effects of various abiotic factors, structural and metabolic internal factors can also influence whether the limitation in CO2 fixation is at the level of diffusion or carboxylation. Such temperature-initiated progressive greening in these and similar mutants may make them useful tools to elucidate not only the biosynthesis and assembly of the photosynthetic apparatus, but also physiological phenomena such as the influence of light-driven energy production on the overall carbon isotope fractionation during photosynthesis.

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PubMed1966

Relationship of Phenylalanine Ammonia-lyase Activity to o-Hydroxycinnamic Acid Content in Melilotus alba.

Phenylalanine ammonia-lyase activity was investigated in preparations representing various parts of sweetclover (Melilotus alba Desr.) plants of CuCu and cucu genotypes. In contrast to other plant parts, very young leaves and stems of CuCu plants displayed high phenylalanine ammonia-lyase activity. Initial leaf samples from CuCu plants were approximately 3 times as high in enzyme activity as leaves from cucu plants, but stems were only slightly higher in activity. Defoliation of the plants resulted in decreased enzyme activity, increased o-hydroxycinnamic acid content, and essentially no difference in enzyme activity between the genotypes. It appears that phenylalanine ammonia-lyase activity in leaves is not primarily controlled by the Cu/cu alleles and that the reaction catalyzed by this enzyme is not the limiting step in o-hydroxycinnamic acid synthesis.

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PubMed1980

Intracellular Localization of Two Enzymes Involved in Coumarin Biosynthesis in Melilotus alba.

The localization of phenylalanine ammonia-lyase [EC 4.3.1.5] within sweet clover (Melilotus alba) leaves was investigated. Apical buds and axillary leaves contained 15 to 30 times more enzyme activity than did mature leaves. Mesophyll protoplasts were prepared by digesting young leaves with Cellulysin and Macerase and were gently ruptured yielding intact chloroplasts. These chloroplast preparations exhibited neither phenylalanine ammonia-lyase nor o-coumaric acid O-glucosyltransferase activities. The general enzymic properties of sweet clover leaf phenylalanine ammonia-lyase were similar to those described for this enzyme isolated from other plant species. The conversion of l-phenylalanine to trans-cinnamic acid, which occurred at an optimum pH of about 8.7, was strongly inhibited by the metabolites trans-cinnamic and o-coumaric acids. In contrast, o-coumaric acid glucoside, coumarin, p-coumaric acid, and melilotic acid had no significant effect on the reaction rate.

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PubMed1981

Isolation and Characterization of Vacuoles from Melilotus alba Mesophyll.

Methods for the preparation of protoplasts and vacuoles from mesophyll tissues of sweet clover (Melilotus alba Desr.) are described. Vacuoles are obtained using a new procedure which involves lysis of the plasmalemma during a brief centrifugation of protoplasts through a diethylaminoethyl dextran layer. This method combines the release of vacuoles and their purification in one step. The contamination of vacuole preparations was found to be low, as judged by enzymic markers and microscopic inspection. The method described is rapid and gives a good yield of vacuoles without causing changes in osmotic pressure. Several hydrolases were found to be located in vacuoles from sweet clover, which were also examined for their amino acid content.

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PubMed1981

Subcellular Localization of 2-(beta-d-Glucosyloxy)-Cinnamic Acids and the Related beta-glucosidase in Leaves of Melilotus alba Desr.

The distribution of the glucosides of trans- and cis-2-hydroxy cinnamic acid and of the beta-glucosidase which hydrolyzes the latter glucoside was examined in preparations of epidermal and mesophyll tissue obtained from leaves of sweet clover (Melilotus alba Desr.). The concentrations of glucosides in the two tissues were about equal when compared on the basis of fresh or dry weight. Inasmuch as the epidermal layers account for no more than 10% of the leaf volume, the mesophyll tissue contains 90% or more of the glucosides. Vacuoles isolated from mesophyll protoplasts contained all of the glucosides present initially in the protoplasts.The specific activities of the beta-glucosidase in the two tissues were also similar; thus, most of the enzyme is contained in mesophyll tissue. However, the amount of enzyme in mesophyll protoplast extracts amounts to only 1 to 2% of the activity present in leaf homogenates when chlorophyll was the basis for comparison. (This small amount of coumarin-beta-glucosidase present in protoplasts is not associated with chlorophyll-containing fractions.) In contrast, 90% of the uridine diphosphate glucose-o-coumaric acid glucosyl transferase activity present in leaf homogenate was recoverable in protoplasts prepared from intact leaves. Such results indicate that most of the coumarin-beta-glucosidase in M. alba leaves is located in the extracytoplasmic space. Only a small fraction (7%) of this extra cytoplasmic beta-glucosidase was associated with individual cells or cell clusters isolated from clover leaves.

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PubMed1985

Mutants of Sweetclover (Melilotus alba) Lacking Chlorophyll b: Studies on Pigment-Protein Complexes and Thylakoid Protein Phosphorylation.

Mutants of sweetclover (Melilotus alba) with defects in the nuclear ch5 locus were examined. Using thin-layer chromatography and absorption spectroscopy, three of these mutants were found to lack chlorophyll (Chl) b. One of these three mutants, U374, possessed thylakoid membranes lacking the three Chl b-containing pigment-protein complexes (AB-1, AB-2, and AB-3) while still containing A-1 and A-2, Chl a complexes derived from photosystems I and II, respectively. Complete solubilization and denaturation of the thylakoid proteins from this mutant revealed very little apoprotein from the Chl b-containing light-harvesting complexes, the major thylakoid proteins in normal plants. The normal and mutant sweetclover plants had active thylakoid protein kinase activities and numerous polypeptides were labeled following incubation with [gamma-(32)P]ATP. With the U374 mutant, however, there was very little detectable label co-migrating with the light-harvesting complex apoproteins on polyacrylamide gels. The Chl b-deficient chlorina-f2 mutant of barley (Hordeum vulgare) also had an active protein kinase activity capable of phosphorylating numerous polypeptides, including ones migrating with the same mobility as the light-harvesting complex apoproteins. These results indicate that the sweetclover mutants may be useful systems for studies on the function and organization of Chl b in thylakoid membranes of higher plants.

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PubMed1986

A Temperature-Sensitive Chlorophyll b-Deficient Mutant of Sweetclover (Melilotus alba).

The ch4 mutant of sweetclover (Melilotus alba) has previously been demonstrated to be partially deficient in chlorophyll and to have a higher ratio of chlorophyll a to b than normal plants. We were able to substantiate these findings when plants were grown at 23 degrees C and lower (permissive temperatures). However, when grown at 26 degrees C (nonpermissive temperature) the plants produced small yellow leaves which exhibited one-twentieth the chlorophyll content of normal plants. Affected leaves did not increase their chlorophyll content when plants were incubated at permissive temperatures, but leaves which developed at the lower temperature contained increased amounts of chlorophyll. Similarly, only new leaves, not previously grown leaves, exhibited the yellow phenotype when the mutant plant was shifted from the permissive temperature to the nonpermissive temperature. Ribulose 1,5-bisphosphate carboxylase activity was decreased by half, relative to normal plants, in the mutant plants grown at the nonpermissive temperature, indicating that general protein synthesis was not greatly impaired and that the effect of the mutation was perhaps specific for chlorophyll content. HPLC analysis indicated that carotenoid content was not diminished to the same extent as chlorophyll and we have determined that the thylakoid protein kinase is not altered, as is the case for other chlorophyll b-deficient mutants. Experiments suggest that changes in photoperiod may be able to modulate the effect of temperature.

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PubMed1987

Photonastic Control of Leaflet Orientation in Melilotus indicus (Fabaceae).

Leaflet orientation in Melilotus indicus (L.) All. Is under photonastic control during the day and nyctinastic control during the night, but also exhibits a diaphototropic (solar-tracking) response. Detached leaves with the two lateral leaflets excised were used to study the solar-tracking capability of the terminal leaflet. Perception of the photonastic excitation is located in the pulvinule. The lower (abaxial) and upper (adaxial) surfaces perceive photonastic excitation, which results in concomitant contraction of the side exposed to light and/or expansion of the opposite side. Steady state laminar elevation is determined by the fluence rates of the light incident simultaneously on the opposite sides. Light sensitivity of the lower side exceeds that of the upper. Response to photonastic excitation of either side is affected by angle of incidence of the light, but angular dependence is restricted to a limited range of angle of incidence, which differs for the two sides. This may be accounted for by the different topography of the two pulvinar surfaces and the localization in them of the light-sensitive tissues.

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PubMed1988

Chlorophyll Expression Varies with Development State in the Temperature-Sensitive ch4 Mutation of Melilotus alba.

The ch4 mutant of sweetclover (Melilotus alba) has previously been demonstrated to be temperature- and photoperiod-sensitive for the accumulation of chlorophyll. Pigment content of ch4 mutant leaves was examined as a function of trifoliolate mass, an index of leaf development. Inhibition of chlorophyll accumulation caused by increased growth temperature or decreased photoperiod can be attenuated during the earliest leaf development stages but is almost complete after the trifoliolates have reached 10 milligrams in size. Once this size is reached, the total amount of chlorophyll per trifoliolate remains constant, and the amount of chlorophyll per gram of leaf decreases as the leaf expands. We have evidence for several other sweetclover mutants with this general phenotype, all with alterations previously determined to be located in different genes as evidenced by complementation following genetic crosses. This mutant phenotype may represent lesions in the chlorophyll biosynthetic pathway or the assembly of the photosynthetic apparatus.

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PubMed1984

[Obtaining flour and protein concentrate from seeds of Melilotus albus. Study of the protein quality].

The present research was carried out to determine the nutritive quality of the flour and protein concentrate from Melilotus albus (white clover) seeds. The flour was studied first. The protein analysis showed methionine to be the first limiting amino acid with a chemical score of 25, with threonine as the second. The biological value obtained was 27. Supplementation studies were performed with different levels of methionine and it was found that the 0.3% level resulted in the best net performance. The biological value obtained under these conditions was 60. The protein efficiency ratio (PER) was also determined, with a value of 1.40 after being corrected with respect to casein. The protein was isolated after studying the pH optimum solubility and precipitation conditions until the flour coumarin compounds were eliminated. Further biological experiments were carried out with the supplemented isolated protein. Under these conditions, a PER value of 2.4 and a biological value of 69 were obtained. No toxicity was observed in rats of both sexes by administration of the protein concentrate during 60 days, at least in the parameters studied during this period.

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PubMed1983

[The suppressive effect of melilotus extract on the thermal edema of rats].

The effect of melilotus extract (ME) and Esberiven (ES) which contain coumarin on the thermal edema, which is one of high protein edema, was evaluated by both quantitative and qualitative assays. The intraperitoneal injection of ME immediately after burn greatly reduced the amount of swelling and effectively inhibited the occurrence of necrosis and induration in the injured leg-skin as compared with the saline controls in which a 3rd degree of thermal injury was observed. Administration of ES also induced a similar suppressive effect. Furthermore, either intraperitoneal or subcutaneous local injection of ME 4 hr before burn was effective in reducing the edema and thermal injury. No increase of the lymph flow and output of lymphocytes and protein from the thoracic duct lymph was observed in thermally injured rats given an injection of ME. The massive infiltration of neutrophils and macrophages 6 to 24 hr after the subcutaneous injection of ME was histologically observed in the dermal lesion of normal rats. Twenty-four hr later, macrophages, fibroblasts, and lymphocytes became predominant. The present data taken together suggest that ME exerts the suppressive effect on thermal injury by either prior or post administration, and these effects might be induced in an indirect manner, through the action of phagocytic cells accumulated in the injured lesion, not via lymphatic drainages of excess fluid and protein.

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PubMed1960