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Journal articles on the topic 'Leghemoglobine'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

Fuchsman, W. H., and R. G. Palmer. "Conservation of leghemoglobin heterogeneity and structures in cultivated and wild soybean." Canadian Journal of Botany 63, no. 11 (November 1, 1985): 1951–56. http://dx.doi.org/10.1139/b85-275.

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The leghemoglobins from a genetically diverse selection of 69 cultivated soybean (Glycine max (L.) Merr.) cultivars and plant introductions and 18 wild soybean (Glycine soja Sieb. & Zucc.) plant introductions all consist of the same set of major leghemoglobins (a, c1, c2, c3), as determined by analytical isoelectric focusing. The conservation of both leghemoglobin heterogeneity and also all four major leghemoglobin structures provides strong circumstantial evidence that leghemoglobin heterogeneity is functional. Glycine max and G. soja produced the same leghemoglobins in the presence of Bradyrhizobium japonicum (Kirchner) Jordan and in the presence of fast-growing Rhizobium japonicum.

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2

Lülsdorf, M. M., and F. B. Holl. "Leghemoglobin variability in the genus Phaseolus." Canadian Journal of Botany 69, no. 2 (February 1, 1991): 353–58. http://dx.doi.org/10.1139/b91-048.

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Leghemoglobins are oxygen-binding proteins in the legume root nodule that generally show structural heterogeneity. Fifty accessions of the genus Phaseolus were screened for leghemoglobin electrophoretic variation. Heterogeneity was observed in two of the six Phaseolus species investigated; the single leghemoglobin components found in samples of Phaseolus vulgaris and Phaseolus acutifolius nodule extracts, as well as in other Phaseolus species, appear to be the exception among nitrogen-fixing plants that have been evaluated for leghemoglobin profiles. Interspecific hybrids were produced to transfer existing leghemoglobin variability into the P. vulgaris background. Leghemoglobins were also shown to be inherited codominantly in interspecific hybrids. The amino terminal amino acid sequence of leghemoglobin II of a P. vulgaris × Phaseolus filiformis hybrid and leghemoglobins I and II from Phaseolus lunatus nodules were determined. The 37 amino terminal amino acids of these components were identical to the published sequence for P. vulgaris. Key words: nitrogen fixation, interspecific hybrids, electrophoresis.

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3

Günther, Catrin, Armin Schlereth, Michael Udvardi, and Thomas Ott. "Metabolism of Reactive Oxygen Species Is Attenuated in Leghemoglobin-Deficient Nodules of Lotus japonicus." Molecular Plant-Microbe Interactions® 20, no. 12 (December 2007): 1596–603. http://dx.doi.org/10.1094/mpmi-20-12-1596.

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Leghemoglobins together with high rates of respiration are believed to be major sources of reactive oxygen species (ROS) in root nodules of leguminous plants. High capacities of antioxidative systems apparently protect this organ from oxidative damage. Using leghemoglobin-RNA interference (LbRNAi) lines of Lotus japonicus, we found that loss of leghemoglobin results in significantly lower H2O2 levels in nodules. Transcript levels and catalytic activities of ascorbate-glutathione cycle enzymes involved in H2O2 detoxification as well as concentrations of reduced ascorbate were also altered in LbRNAi nodules. Thus, symbiotic leghemoglobins contribute significantly to ROS generation in functional nodules.

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4

Frühling, Martin, Hélène Roussel, Vivienne Gianinazzi-Pearson, Alfred Pühler, and Andreas M. Perlick. "The Vicia faba Leghemoglobin Gene VfLb29 Is Induced in Root Nodules and in Roots Colonized by the Arbuscular Mycorrhizal Fungus Glomus fasciculatum." Molecular Plant-Microbe Interactions® 10, no. 1 (January 1997): 124–31. http://dx.doi.org/10.1094/mpmi.1997.10.1.124.

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To investigate similarities between symbiotic interactions of broad bean (Vicia faba) with rhizobia and mycorrhizal fungi, plant gene expression induced by both microsymbionts was compared. We demonstrated the exclusive expression of 19 broad bean genes, including VfENOD2, VfENOD5, VfENOD12 and three different leghemoglobin genes, in root nodules. In contrast, the leghemoglobin gene VfLb29 was found to be induced not only in root nodules, but also in broad bean roots colonized by the mycorrhizal fungus Glomus fasciculatum. In uninfected roots, none of the 20 nodulin transcripts investigated was detectable. VfLb29 has an unusually low sequence homology with all other broad bean leghemoglobins as well as with leghemoglobins from other legumes. It can be regarded as a novel kind of leghemoglobin gene not described until now and the induction of which is common to symbiotic interactions of broad bean with both Rhizobium and a mycorrhizal fungus.

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5

Ott, Thomas, John Sullivan, Euan K. James, Emmanouil Flemetakis, Catrin Günther, Yves Gibon, Clive Ronson, and Michael Udvardi. "Absence of Symbiotic Leghemoglobins Alters Bacteroid and Plant Cell Differentiation During Development of Lotus japonicus Root Nodules." Molecular Plant-Microbe Interactions® 22, no. 7 (July 2009): 800–808. http://dx.doi.org/10.1094/mpmi-22-7-0800.

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During development of legume root nodules, rhizobia and their host plant cells undergo profound differentiation, which is underpinned by massive changes in gene expression in both symbiotic partners. Oxygen concentrations in infected and surrounding uninfected cells drop precipitously during nodule development. To assess what effects this has on plant and bacterial cell differentiation and gene expression, we used a leghemoglobin-RNA-interference (LbRNAi) line of Lotus japonicus, which is devoid of leghemoglobins and has elevated levels of free-oxygen in its nodules. Bacteroids in LbRNAi nodules showed altered ultrastructure indicating changes in bacterial differentiation. Transcript analysis of 189 plant and 192 bacterial genes uncovered many genes in both the plant and bacteria that were differentially regulated during nodulation of LbRNAi plants compared with the wild type (containing Lb and able to fix nitrogen). These included fix and nif genes of the bacteria, which are involved in microaerobic respiration and nitrogen fixation, respectively, and plant genes involved in primary and secondary metabolism. Metabolite analysis revealed decreased levels of many amino acids in nodules of LbRNAi plants, consistent with the defect in symbiotic nitrogen fixation of this line.

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6

Yerokun, O. M., and M. O. Onyesolu. "On the Development of Neuro-Fuzzy Expert System for Detection of Leghemoglobin (NFESDL) in Legumes." advances in multidisciplinary & scientific research journal publication 9, no. 1 (January 24, 2021): 1–14. http://dx.doi.org/10.22624/aims/digital/v9n1p1.

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The regular supply of affordable complete meals most especially protein from animals has been threatened. Protein sourced from animals carry too many health risks. Obesity, cancer, diabetes, etc., have been traced to the consumption of meats, most especially beef. Medical experts claim that some ailments are as a result of the chemically processed feeds given to raise animals. Therefore, an alternative to meat from plants is imperative. This led to the development of a neuro-fuzzy expert system for detection of leghemoglobin in legumes. This work utilized production rule-base technique and forward-chaining mechanisms with linguistic antecedent conditions to detect the presence of leghemoglobin in plants. To further remove clumsiness and ambiguity in the identification process, metrics/weights were obtained and attached to each morphological feature. MATLAB platform was employed for the development of the system. Class and objects were used to model the information elicited. The result is a system that detects the presence of leghemoglobin in plants. Keywords: Expert system, inference system, neuro-fuzzy, dataset, leghemoglobin

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7

Moreau, Sophie, Michael J. Davies, Christel Mathieu, Didier Hérouart, and Alain Puppo. "Leghemoglobin-derived Radicals." Journal of Biological Chemistry 271, no. 51 (December 20, 1996): 32557–62. http://dx.doi.org/10.1074/jbc.271.51.32557.

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8

Tagore, G. S., S. L. Namdeo, S. K. Sharma, and Narendra Kumar. "Effect ofRhizobiumand Phosphate Solubilizing Bacterial Inoculants on Symbiotic Traits, Nodule Leghemoglobin, and Yield of Chickpea Genotypes." International Journal of Agronomy 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/581627.

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A field experiment was carried out during therabiseason of 2004-05 to find out the effect ofRhizobiumand phosphate solubilizing bacterial (PSB) inoculants on symbiotic traits, nodule leghemoglobin, and yield of five elite genotypes of chickpea. Among the chickpea genotypes, IG-593 performed better in respect of symbiotic parameters including nodule number, nodule fresh weight, nodule dry weight, shoot dry weight, yield attributes and yield. Leghemoglobin content (2.55 mg g−1of fresh nodule) was also higher under IG-593. Among microbial inoculants, theRhizobium+ PSB was found most effective in terms of nodule number (27.66 nodules plant−1), nodule fresh weight (144.90 mg plant−1), nodule dry weight (74.30 mg plant−1), shoot dry weight (11.76 g plant−1), and leghemoglobin content (2.29 mg g−1of fresh nodule) and also showed its positive effect in enhancing all the yield attributing parameters, grain and straw yields.

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9

Saari, Leonard L., and Robert V. Klucas. "Nonenzymatic reduction of ferric leghemoglobin." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 912, no. 2 (April 1987): 198–202. http://dx.doi.org/10.1016/0167-4838(87)90089-6.

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10

Mendoza, Danilo M., Praphasri Chongpraditnun, Mitsuo Chino, Keiji Suzuki, and Shigenori Kurashige. "Preparation of antibody of mungbean leghemoglobin." Soil Science and Plant Nutrition 39, no. 1 (March 1993): 161–68. http://dx.doi.org/10.1080/00380768.1993.10416985.

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11

Konieczny, A., E. �. Jensen, K. A. Marcker, and A. B. Legocki. "Molecular cloning of lupin leghemoglobin cDNA." Molecular Biology Reports 12, no. 1 (1987): 61–66. http://dx.doi.org/10.1007/bf00580652.

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12

Mendonça, Elenira Henrique Miranda, and Marlene Aparecida Schiavinato. "Growth of Crotalaria juncea L. supplied with mineral nitrogen." Brazilian Archives of Biology and Technology 48, no. 2 (March 2005): 181–85. http://dx.doi.org/10.1590/s1516-89132005000200003.

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Plants of Crotalaria juncea inoculated with Rhizobium were treated with nutrient solution containing 10 or 20mg of either N/NO3 or N/NH4.plant-1.week-1 . The control plants received nutrient solution without N. An investigation was conducted on the effect of these sources of N on growth and nitrogen fixation of plants with 30, 60 and 90 days after sowing (DAS). Those that received mineral N presented higher growth than -N plants, but the presence of nodules occurred in all the treatments. Plants treated with NH4 presented higher N content until 60 days. The highest concentrations of leghemoglobin and protein in nodules were found at 30 DAS and there was no difference in leghemoglobin content between treatments for any age and in protein from 60 DAS. Nitrogenase activity did not vary from 60 to 90 days, with the exception of plants that received 20mg N/NO3, where it was higher at 60 days

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13

Lee, Kk, L. L. Shearman, B. K. Erickson, and R. V. Klucas. "Ferric Leghemoglobin in Plant-Attached Leguminous Nodules." Plant Physiology 109, no. 1 (September 1, 1995): 261–67. http://dx.doi.org/10.1104/pp.109.1.261.

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14

Konieczny, Andrzej. "Nucleotide sequence of lupin leghemoglobin I cDNA." Nucleic Acids Research 15, no. 16 (1987): 6742. http://dx.doi.org/10.1093/nar/15.16.6742.

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15

Lobato, A. K. S., R. C. L. Costa, C. F. Oliveira Neto, B. G. Santos Filho, M. C. Gonçalves-Vidigal, P. S. Vidigal Filho, C. R. Silva, et al. "Consequences of the water deficit on water relations and symbiosis in Vigna unguiculata cultivars." Plant, Soil and Environment 55, No. 4 (May 5, 2009): 139–45. http://dx.doi.org/10.17221/1615-pse.

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The study aimed at evaluating and comparing changes provoked by the water deficit on water relations and nitrogen fixation in two <I>Vigna unguiculata</I> cultivars, as well as at indicating which cultivar is more tolerant under water deficiency. The experimental design used was entirely randomized in factorial scheme, with 2 cultivars (Pitiuba and Pérola) and 2 water regimes (control and stress). The parameters evaluated were the leaf relative water content, stomatal conductance, transpiration rate, nodule number, nodule dry matter, nitrate reductase enzyme activity, ureide concentration and leghemoglobin in nodule. The stomatal conductance of the Pitiuba and Pérola cultivars under water deficit were 0.20 and 0.01 mmol H<sub>2</sub>O/m<sup>2</sup>/s, respectively. The nitrate reductase activity of the plants under stress was significantly reduced in both cultivars. The leghemoglobin in the Pitiuba and Pérola cultivars under water stress had the concentrations of 58 and 41 g/kg dry matter, respectively. The parameters investigated in this study suggest that the Pitiuba cultivar under water deficit suffers from smaller changes, when compared with Pérola cultivar.

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16

Vieweg, Martin F., Martin Frühling, Hans-Joachim Quandt, Ute Heim, Helmut Bäumlein, Alfred Pühler, Helge Küster, and Andreas M. Perlick. "The Promoter of the Vicia faba L. Leghemoglobin Gene VfLb29 Is Specifically Activated in the Infected Cells of Root Nodules and in the Arbuscule-Containing Cells of Mycorrhizal Roots from Different Legume and Nonlegume Plants." Molecular Plant-Microbe Interactions® 17, no. 1 (January 2004): 62–69. http://dx.doi.org/10.1094/mpmi.2004.17.1.62.

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The VfLb29 leghemoglobin gene promoter was polymerase chain reaction-amplified from a Vicia faba genomic library and was fused to the gusAint coding region. Expression of the chimeric gene was analyzed in transgenic hairy roots of the legumes V. faba, V. hirsuta, and Medicago truncatula as well as in transgenic Nicotiana tabacum plants. The VfLb29 promoter was found to be specifically active not only in the infected cells of the nitrogen-fixing zone of root nodules but also in arbuscule-containing cells of transgenic V. faba and M. truncatula roots colonized by the endomycorrhizal fungus Glomus intraradices. In addition to these two legumes, specific expression in arbuscule-containing cells was also observed in the nonlegume N. tabacum. All studies were done in comparison to the V. faba leghemoglobin gene promoter VfLb3 that as VfLb29 was expressed in the infected cells of root nodules but showed no activity in endomycorrhiza. An activation of the VfLb29 promoter due to hypoxia in metabolically active tissues was excluded. The conserved activation in arbuscule-containing cells of legumes and the nonlegume N. tabacum suggests a conserved trigger for this promoter in legume and nonlegume endomycorrhiza symbioses.

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17

Strózycki, Pawel M., and Andrzej B. Legocki. "Leghemoglobins from an evolutionarily old legume, Lupinus luteus." Plant Science 110, no. 1 (September 1995): 83–93. http://dx.doi.org/10.1016/0168-9452(95)04185-w.

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18

Christensen, Tove, Niels N. Sandal, Jens Stougaard, and Kjeld A. Marcker. "5′ flanking sequence of the soybean leghemoglobin lbc3gene." Nucleic Acids Research 17, no. 11 (1989): 4383. http://dx.doi.org/10.1093/nar/17.11.4383.

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19

Mathieu, Christel, Kumari Swaraj, Michael J. Davies, Jean-Charles Trinchant, and Alain Puppo. "Absence of Synproportionation Between Oxy and Ferryl Leghemoglobin." Free Radical Research 27, no. 2 (January 1997): 165–71. http://dx.doi.org/10.3109/10715769709097848.

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20

Vivo, Amparo, José Manuel Andreu, Sonsoles de la Viña, and María Rosario de Felipe. "Leghemoglobin in Lupin Plants (Lupinus albus cv Multolupa)." Plant Physiology 90, no. 2 (June 1, 1989): 452–57. http://dx.doi.org/10.1104/pp.90.2.452.

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21

Makarov, A. A., G. N. Mgeladze, D. R. Monaselidze, and N. G. Esipova. "Manifestation of intraglobular dynamics at microcalorimetry of leghemoglobin crystals." Journal of Polymer Science: Polymer Symposia 69, no. 1 (March 8, 2007): 101–9. http://dx.doi.org/10.1002/polc.5070690115.

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22

Czerminski, Ryszard, and Ron Elber. "Computational studies of ligand diffusion in globins: I. Leghemoglobin." Proteins: Structure, Function, and Genetics 10, no. 1 (January 1991): 70–80. http://dx.doi.org/10.1002/prot.340100107.

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23

Kosmachevskaya, O. V., and A. F. Topunov. "Formation of glycated recombinant leghemoglobin in Escherichia coli cells." Applied Biochemistry and Microbiology 46, no. 3 (May 2010): 297–302. http://dx.doi.org/10.1134/s0003683810030087.

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24

Basak, P., R. Pattanayak, S. Nag, and M. Bhattacharyya. "pH-induced conformational isomerization of leghemoglobin from Arachis hypogea." Biochemistry (Moscow) 79, no. 11 (November 2014): 1255–61. http://dx.doi.org/10.1134/s0006297914110133.

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25

Jun, Hyung-Kyun, Gautam Sarath, and Fred W. Wagner. "Detection and purification of modified leghemoglobins from soybean root nodules." Plant Science 100, no. 1 (January 1994): 31–40. http://dx.doi.org/10.1016/0168-9452(94)90131-7.

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26

Lee, H. Caroline, Jonathan B. Wittenberg, and Jack Peisach. "Role of hydrogen bonding to bound dioxygen in soybean leghemoglobin." Biochemistry 32, no. 43 (January 26, 1993): 11500–11506. http://dx.doi.org/10.1021/bi00094a005.

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27

Becana, M., Y. Gogorcena, P. M. Aparicio-Tejo, and M. Sánchez-Díaz. "Nitrogen Fixation and Leghemoglobin Content during Vegetative Growth of Alfalfa." Journal of Plant Physiology 123, no. 2 (April 1986): 117–25. http://dx.doi.org/10.1016/s0176-1617(86)80132-8.

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28

Mendonça, Elenira H. M., Paulo Mazzafera, and Marlene A. Schiavinato. "Purification of leghemoglobin from nodules of Crotalaria infected with Rhizobium." Phytochemistry 50, no. 2 (January 1999): 313–16. http://dx.doi.org/10.1016/s0031-9422(98)00532-9.

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29

Morikis, Dimitrios, and Peter E. Wright. "Hydrogen Exchange in the Carbon Monoxide Complex of Soybean Leghemoglobin." European Journal of Biochemistry 237, no. 1 (April 1996): 212–20. http://dx.doi.org/10.1111/j.1432-1033.1996.0212n.x.

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30

Stetzkowski, F., R. Banerjee, M. C. Marden, D. K. Beece, S. F. Bowne, W. Doster, L. Eisenstein, H. Frauenfelder, L. Reinisch, and E. Shyamsunder. "Dynamics of dioxygen and carbon monoxide binding to soybean leghemoglobin." Journal of Biological Chemistry 260, no. 15 (July 1985): 8803–9. http://dx.doi.org/10.1016/s0021-9258(17)39423-1.

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31

Ji, Lin, Stephen Wood, Manuel Becana, and Robert V. Klucas. "Purification and Characterization of Soybean Root Nodule Ferric Leghemoglobin Reductase." Plant Physiology 96, no. 1 (May 1, 1991): 32–37. http://dx.doi.org/10.1104/pp.96.1.32.

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32

Roberts, Mary P., Sajida Jafar, and Beth C. Mullin. "Leghemoglobin-like sequences in the DNA of four actinorhizal plants." Plant Molecular Biology 5, no. 6 (1985): 333–37. http://dx.doi.org/10.1007/bf00037553.

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33

Stróżycki, P. M., W. M. Karłowski, Y. Dessaux, A. Petit, and A. B. Legocki. "Lupine leghemoglobin I : expression in transgenic Lotus and tobacco tissues." Molecular and General Genetics MGG 263, no. 2 (March 2000): 173–82. http://dx.doi.org/10.1007/s004380051158.

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34

Putnoky, P., E. Grosskopf, D. T. Ha, G. B. Kiss, and A. Kondorosi. "Rhizobium fix genes mediate at least two communication steps in symbiotic nodule development." Journal of Cell Biology 106, no. 3 (March 1, 1988): 597–607. http://dx.doi.org/10.1083/jcb.106.3.597.

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To identify bacterial genes involved in symbiotic nodule development, ineffective nodules of alfalfa (Medicago sativa) induced by 64 different Fix-mutants of Rhizobium meliloti were characterized by assaying for symbiotic gene expression and by morphological studies. The expression of leghemoglobin and nodulin-25 genes from alfalfa and of the nifHD genes from R. meliloti were monitored by hybridizing the appropriate DNA probes to RNA samples prepared from nodules. The mutants were accordingly divided into three groups. In group I none of the genes were expressed, in group II only the plant genes were expressed and in group III all three genes were transcribed. Light and electron microscopical analysis of nodules revealed that nodule development was halted at different stages in nodules induced by different group I mutants. In most cases nodules were empty lacking infection threads and bacteroids or nodules contained infection threads and a few released bacteroids. In nodules induced by a third mutant class bacteria were released into the host cells, however the formation of the peribacteroid membrane was not normal. On this basis we suggest that peribacteroid membrane formation precedes leghemoglobin and nodulin-25 induction, moreover, after induction of nodulation by the nod genes at least two communication steps between the bacteria and the host plants are necessary for the development of the mature nodule. By complementing each mutant of group I with a genomic R. meliloti library made in pLAFRl, four new fix loci were identified, indicating that several bacterial genes are involved in late nodule development.

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35

Wiebauer, K., J. J. Herrero, and W. Filipowicz. "Nuclear pre-mRNA processing in plants: distinct modes of 3'-splice-site selection in plants and animals." Molecular and Cellular Biology 8, no. 5 (May 1988): 2042–51. http://dx.doi.org/10.1128/mcb.8.5.2042.

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The report that human growth hormone pre-mRNA is not processed in transgenic plant tissues (A. Barta, K. Sommergruber, D. Thompson, K. Hartmuth, M.A. Matzke, and A.J.M. Matzke, Plant Mol. Biol. 6:347-357, 1986) has suggested that differences in mRNA splicing processes exist between plants and animals. To gain more information about the specificity of plant pre-mRNA processing, we have compared the splicing of the soybean leghemoglobin pre-mRNA with that of the human beta-globin pre-mRNA in transfected plant (Orychophragmus violaceus and Nicotiana tabacum) protoplasts and mammalian (HeLa) cells. Of the three introns of leghemoglobin pre-mRNA, only intron 2 was correctly and efficiently processed in HeLa cells. The 5' splice sites of the remaining two introns were faithfully recognized, but correct processing of the 3' sites took place only rarely (intron 1) or not at all (intron 3); cryptic 3' splice sites were used instead. While the first intron in human beta-globin pre-mRNA was not spliced in transfected plant protoplasts, intron 2 processing occurred at a low level, indicating that some mammalian introns can be recognized by the plant intron-splicing machinery. However, excision of intron 2 proved to be incorrect, involving the authentic 5' splice site and a cryptic 3' splice site. Our results indicate that the mechanism of 3'-splice-site selection during intron excision differs between plants and animals. This conclusion is supported by analysis of the 3'-splice-site consensus sequences in animal and plant introns which revealed that polypyrimidine tracts, characteristic of animal introns, are not present in plant pre-mRNAs. It is proposed that an elevated AU content of plant introns is important for their processing.

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36

Wiebauer, K., J. J. Herrero, and W. Filipowicz. "Nuclear pre-mRNA processing in plants: distinct modes of 3'-splice-site selection in plants and animals." Molecular and Cellular Biology 8, no. 5 (May 1988): 2042–51. http://dx.doi.org/10.1128/mcb.8.5.2042-2051.1988.

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The report that human growth hormone pre-mRNA is not processed in transgenic plant tissues (A. Barta, K. Sommergruber, D. Thompson, K. Hartmuth, M.A. Matzke, and A.J.M. Matzke, Plant Mol. Biol. 6:347-357, 1986) has suggested that differences in mRNA splicing processes exist between plants and animals. To gain more information about the specificity of plant pre-mRNA processing, we have compared the splicing of the soybean leghemoglobin pre-mRNA with that of the human beta-globin pre-mRNA in transfected plant (Orychophragmus violaceus and Nicotiana tabacum) protoplasts and mammalian (HeLa) cells. Of the three introns of leghemoglobin pre-mRNA, only intron 2 was correctly and efficiently processed in HeLa cells. The 5' splice sites of the remaining two introns were faithfully recognized, but correct processing of the 3' sites took place only rarely (intron 1) or not at all (intron 3); cryptic 3' splice sites were used instead. While the first intron in human beta-globin pre-mRNA was not spliced in transfected plant protoplasts, intron 2 processing occurred at a low level, indicating that some mammalian introns can be recognized by the plant intron-splicing machinery. However, excision of intron 2 proved to be incorrect, involving the authentic 5' splice site and a cryptic 3' splice site. Our results indicate that the mechanism of 3'-splice-site selection during intron excision differs between plants and animals. This conclusion is supported by analysis of the 3'-splice-site consensus sequences in animal and plant introns which revealed that polypyrimidine tracts, characteristic of animal introns, are not present in plant pre-mRNAs. It is proposed that an elevated AU content of plant introns is important for their processing.

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37

Trevaskis, B., R. A. Watts, C. R. Andersson, D. J. Llewellyn, M. S. Hargrove, J. S. Olson, E. S. Dennis, and W. J. Peacock. "Two hemoglobin genes in Arabidopsis thaliana: The evolutionary origins of leghemoglobins." Proceedings of the National Academy of Sciences 94, no. 22 (October 28, 1997): 12230–34. http://dx.doi.org/10.1073/pnas.94.22.12230.

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38

NARULA, Surinder S., Claudio DALVIT, Cyril A. APPLEBY, and Peter E. WRIGHT. "NMR studies of the conformations of leghemoglobins from soybean and lupin." European Journal of Biochemistry 178, no. 2 (December 1988): 419–35. http://dx.doi.org/10.1111/j.1432-1033.1988.tb14466.x.

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39

Sarath, Gautam, Hillel P. Cohen, and Fred W. Wagner. "High-performance liquid chromatographic separation of leghemoglobins from soybean root nodules." Analytical Biochemistry 154, no. 1 (April 1986): 224–31. http://dx.doi.org/10.1016/0003-2697(86)90519-1.

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40

Mendoza, Danilo M., Satoshi Mori, and Mitsuo Chino. "Determination of the n-terminal amino acid sequence of mengbean leghemoglobin." Soil Science and Plant Nutrition 39, no. 3 (September 1993): 475–83. http://dx.doi.org/10.1080/00380768.1993.10419788.

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Nishiwaki, Toshikazu, Takashi Sato, Hiroyuki Yashima, Taro Ikarashi, Takuji Ohyama, James E. Harper, Shoichiro Akao, and Hiroshi Kouchi. "Changes in concentration of leghemoglobin components in hypernodulation mutants of soybean." Soil Science and Plant Nutrition 43, sup1 (January 1997): 1091–96. http://dx.doi.org/10.1080/00380768.1997.11863723.

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Davidowitz, Eliot J., Alan Dow, and Naomi Lang-Unnasch. "Nucleotide sequence of a cDNA clone encoding a leghemoglobin fromMedicago sativa." Nucleic Acids Research 17, no. 8 (1989): 3307. http://dx.doi.org/10.1093/nar/17.8.3307.

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Klucas, Robert V., and Cyril A. Appleby. "Nicotinate, Nicotinamide, and the Reactivity of Leghemoglobin in Soybean Root Nodules." Plant Physiology 95, no. 2 (February 1, 1991): 551–55. http://dx.doi.org/10.1104/pp.95.2.551.

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Becana, Manuel, and Robert V. Klucas. "Oxidation and Reduction of Leghemoglobin in Root Nodules of Leguminous Plants." Plant Physiology 98, no. 4 (April 1, 1992): 1217–21. http://dx.doi.org/10.1104/pp.98.4.1217.

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L�bler, Marian, and Ann M. Hirsch. "An alfalfa (Medicago sativa L.) cDNA encoding an acidic leghemoglobin (MsLb3)." Plant Molecular Biology 20, no. 4 (November 1992): 733–36. http://dx.doi.org/10.1007/bf00046457.

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Hargrove, Mark S., Jennifer K. Barry, Eric Allen Brucker, Michael B. Berry, George N. Phillips, John S. Olson, Raúl Arredondo-Peter, Jeanenne M. Dean, Robert V. Klucas, and Gautam Sarath. "Characterization of recombinant soybean leghemoglobin a and apolar distal histidine mutants." Journal of Molecular Biology 266, no. 5 (March 1997): 1032–42. http://dx.doi.org/10.1006/jmbi.1996.0833.

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Herrada, Gilles, Alain Puppo, Sophie Moreau, David A. Day, and Jean Rigaud. "How is leghemoglobin involved in peribacteroid membrane degradation during nodule senescence?" FEBS Letters 326, no. 1-3 (July 1, 1993): 33–38. http://dx.doi.org/10.1016/0014-5793(93)81755-o.

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Hattori, J., and D. A. Johnson. "The detection of leghemoglobin-line sequences in legumes and non-legumes." Plant Molecular Biology 4, no. 5 (September 1985): 285–92. http://dx.doi.org/10.1007/bf02418247.

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Davidowitz, Eliot J., Gary Creissen, Evan Vincze, Gy�rgy B. Kiss, and Naomi Lang-Unnasch. "Sequence analysis of alfalfa (Medicago sativa) leghemoglobin cDNA and genomic clones." Plant Molecular Biology 16, no. 1 (January 1991): 161–65. http://dx.doi.org/10.1007/bf00017926.

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Álvarez-Salgado, Emma, and Raúl Arredondo-Peter. "Effect of the synthesis of rice non-symbiotic hemoglobins 1 and 2 in the recombinant Escherichia coli TB1 growth." F1000Research 4 (October 12, 2015): 1053. http://dx.doi.org/10.12688/f1000research.7195.1.

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Abstract:

Non-symbiotic hemoglobins (nsHbs) are widely distributed in land plants, including rice. These proteins are classified into type 1 (nsHbs-1) and type 2. The O2-affinity of nsHbs-1 is very high mostly because of an extremely low O2-dissociation rate constant resulting in that nsHbs-1 apparently do not release O2 after oxygenation. Thus, it is possible that the in vivo function of nsHbs-1 is other than O2-transport. Based on the properties of multiple Hbs it was proposed that nsHbs-1 could play diverse roles in rice organs, however the in vivo activity of rice nsHbs-1 has been poorly analyzed. An in vivo analysis for rice nsHbs-1 is essential to elucidate the biological function(s) of these proteins. Rice Hb1 and Hb2 are nsHbs-1 that have been generated in recombinant Escherichia coli TB1. The rice Hb1 and Hb2 amino acid sequence, tertiary structure and rate and equilibrium constants for the reaction of O2 are highly similar. Thus, it is possible that rice Hb1 and Hb2 function similarly in vivo. As an initial approach to test this hypothesis we analyzed the effect of the synthesis of rice Hb1 and Hb2 in the recombinant E. coli TB1 growth. Effect of the synthesis of the O2-carrying soybean leghemoglobin a, cowpea leghemoglobin II and Vitreoscilla Hb in the recombinant E. coli TB1 growth was also analyzed as an O2-carrier control. Our results showed that synthesis of rice Hb1, rice Hb2, soybean Lba, cowpea LbII and Vitreoscilla Hb inhibits the recombinant E. coli TB1 growth and that growth inhibition was stronger when recombinant E. coli TB1 synthesized rice Hb2 than when synthesized rice Hb1. These results suggested that rice Hb1 and Hb2 could function differently in vivo.

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