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Featured researches published by David J. Bonfil.


FEBS Letters | 1998

A putative HCO−3 transporter in the cyanobacterium Synechococcus sp. strain PCC 79421

David J. Bonfil; Michal Ronen-Tarazi; Dieter Sültemeyer; Judy Lieman-Hurwitz; Daniella Schatz; Aaron Kaplan

Cyanobacteria possess an inducible mechanism which enables them to concentrate inorganic carbon (Ci) within the cells. An inactivation library was used to raise the high‐CO2‐requiring mutant of Synechococcus PCC 7942, IL‐2, impaired in HCO− 3 transport. Analysis of the relevant genomic DNA detected several modifications, probably due to the single crossover recombination, leading to inactivation of ORF467 (designated ictB) in IL‐2. IctB contains 10 trans‐membrane regions and is homologous to several transport‐related proteins from various organisms. Kinetic analyses of HCO− 3 uptake in the wild type and IL‐2 suggested the presence of two or three HCO− 3 carriers exhibiting different affinities to HCO− 3.


Euphytica | 1997

Changes in wheat seed storage protein fingerprint due to soil mineral content

David J. Bonfil; Henryk Czosnek; U. Kafkafi

Wheat seed storage protein fingerprint is used to determine the gluten protein pattern in studies aimed at improving flour quality. Wild wheat with high seed protein content is used extensively in wheat breeding programs. Although the wild wheat growth and protein content may be influenced by environmental conditions, the gluten-protein pattern is generally considered as indicative of a genotype, without the superimposition of environmental influences. The effects of soil type, habitat, and deficiencies of N, P, K and S on seed storage protein composition were examined in nine accessions of wild wheat (Triticum turgidum var. dicoccoides) and three varieties (two T. aestivum and one T. durum). Soil from ten natural habitats of the wild wheat that had not previously received any fertilizers or manures was sampled and used to grow wheat in a greenhouse. Seed storage protein composition was characterized by SDS-PAGE. Although deficiencies in soil nutrient caused variations in the seed storage proteins, the genotype was the main factor determining the seed storage protein composition. Seed storage protein composition of genotypes varied when grown under different mineral nutrient conditions. Only one genotype was stable showing almost identical protein patterns under all growing conditions studied without any qualitative change in fingerprint pattern. In the other genotypes, as well as the cultivars, the seed storage protein was affected at least to some extent by the soil. The ‘soil effect’ is summarized in terms of three main quantitative changes in the seeds: 1 – the relative amounts of the high-molecular-weight proteins; 2 – the relative amounts of proteins in the range of 45 and 65 kD; 3 – the percentage distribution of the HMW glutenin and other groups of seed storage proteins. The soild induced also qualitative differences in the composition of seed storage proteins, mostly in those of 45–65 kD. These differences were observed whenever a deficiency of S, N, P, K or Mg was identified. Therefore, in breeding programs that use seed storage protein fingerprints of wild wheat germplasms should be exercise caution when the germplasms selected from wild habitats.


Archive | 1996

Cyanobacterial Mutants Defective in HCO 3 - Uptake

Michal Ronen-Tarazi; Judy Lieman-Hurwitz; David J. Bonfil; Vera Shinder; Aaron Kaplan

Photosynthetic microorganisms are capable of adapting to a wide range of CO2 concentrations. When cyanobacterial cells are transferred from high to low concentrations of CO2, they undergo an adaptation process. This includes modulation of the expression of certain genes, some of which are involved in the operation of the inorganic carbon (Ci)-concentrating mechanism (CCM, see Miller et al. 1990; Kaplan et al. 1991; Raven 1991; Badger, Price 1992; Ogawa 1993 and Kaplan et al. 1994 for recent reviews and literature citations). The active accumulation of Ci to levels as high as 50-100 mM Ci, consequent on the activity of the CCM, enables the cells to perform efficient photosynthesis in spite of the relatively low affinity of their ribulose 1,5- bisphosphate carboxylase (rubisco) for CO2. Moreover, the elevated concentration of CO2 in close proximity to rubisco, within the carboxysomes, activates the enzyme, reduces competition by O2 and inhibits photorespiration (Schwarz et al. 1995)


Archive | 1999

The Inorganic Carbon-Concentrating Mechanism of Cyanobacteria

Aaron Kaplan; Michal Ronen-Tarazi; Dan Tchernov; David J. Bonfil; Hagit Zer; Daniella Schatz; Assaf Vardi; Miriam Hassidim; Leonora Reinhold

In this chapter we briefly present and discuss recent progress in the elucidation of certain physiological and molecular aspects of the cyanobacterial inorganic carbon (Ci)-concentrating mechanism (CCM). The reader is referred to earlier chapters and reviews [1—14] for a comprehensive account of other important aspects, including the acclimation of cyanobacteria to changing CO2 concentration.


Botany | 1998

The inorganic carbon-concentrating mechanism in cyanobacteria: induction and ecological significance

Aaron Kaplan; Michal Ronen-Tarazi; Hagit Zer; Rakefet Schwarz; Dan Tchernov; David J. Bonfil; Daniella Schatz; Assaf Vardi; Miriam Hassidim; Leonora Reinhold


Euphytica | 2000

Wild wheat adaptation in different soil ecosystems as expressed in the mineral concentration of the seeds

David J. Bonfil; U. Kafkafi


Archive | 1999

Enhancing inorganic carbon fixation by photosynthetic organisms

Aaron Kaplan; Judy Lieman-Hurwitz; Daniella Schatz; Ron Mittler; Michal Ronen-Tarazi; David J. Bonfil


Botany | 1998

Cyanobacterial mutants impaired in bicarbonate uptake isolated with the aid of an inactivation library

Michal Ronen-Tarazi; David J. Bonfil; Daniella Schatz; Aaron Kaplan


Archive | 2008

Integrated Nutrient Management: Experience and Concepts from the Middle East

U. Kafkafi; David J. Bonfil


FEBS Letters | 1998

A putative HCO − 3 transporter in the cyanobacterium Synechococcus sp. strain PCC 7942 1 The relevant DNA sequence is available in the GenBank (accession number U62616). 1

David J. Bonfil; Michal Ronen-Tarazi; Dieter Sültemeyer; Judy Lieman-Hurwitz; Daniella Schatz; Aaron Kaplan

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Aaron Kaplan

Hebrew University of Jerusalem

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Michal Ronen-Tarazi

Hebrew University of Jerusalem

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Daniella Schatz

Weizmann Institute of Science

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Judy Lieman-Hurwitz

Hebrew University of Jerusalem

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U. Kafkafi

Hebrew University of Jerusalem

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Assaf Vardi

Weizmann Institute of Science

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Hagit Zer

Hebrew University of Jerusalem

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Leonora Reinhold

Hebrew University of Jerusalem

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Miriam Hassidim

Hebrew University of Jerusalem

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