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  • 1
    ISSN: 1432-041X
    Keywords: Pl-nectin ; Cell-substrate adhesion ; Sea urchin ; Embryogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A new embryonic extracellular matrix protein has been purified from eggs of the sea urchin Paracentrotus lividus. The molecule is a 210 kD dimer consisting of two 105 kD subunits that are held together by S-S bridges. In the unfertilized egg, the protein is found within granules uniformly distributed throughout the cytoplasm. After the egg is fertilized, the antigen is polarized to the apical surface of ectodermal and endodermal cells during all of the developmental stages examined, until the pluteus larva is formed. The protein promotes the adhesion of blastula cells to the substrate and is antigenically distinct from echinonectin, a well characterized substrate adhesion molecule. This report adds a new candidate to the list of known extracellular matrix molecules for the regulation of differentiation and morphogenesis in the sea urchin embryo.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: 3-Amino- 1,2,4-triazole (amitrole) provided to germinating barley at 20°C in the light led to bleached seedling leaves and photodynamic destruction of chloroplast structure, whereas normal greening and chloroplast ultrastructure was obtained when the seedlings developed in the presence of amitrole in the light at 30°C. Mass spectrometric analysis of the extractable herbicide demonstrated the same content of amitrole in leaves developed at 20 and 30°C. A very similar temperature-sensitive syndrome is characteristic for the nuclear gene mutant ligrina-o34 in barley. Amitrole and the mutation were shown to inhibit the cyclization of lycopene, leading to severe deficiencies in β-carotene and its xanthophyll derivative lutein. Besides accumulation of lycopene, also its precursors phytoene, phytofluene and ξ-carotene accumulated. Inhibition of carotenoid biosynthesis by amitrole and the mutation at 20°C in the light led to a strong reduction of both transcript and protein levels for chloroplastic glutamine synthetase (GS2) while transcript amount and protein of the cytosolic isoenzyme (GS1) were unaffected. At 30°C increased levels of mRNA for the chloroplastic isoform GS2 were observed in wild type, mutant and amitrole-treated seedlings, but protein levels remained unchanged. Turnover rates of the GS2 protein were the same at 20 and 30°C. This extensive translational control of chloroplastic GS2 synthesis was also observed in a heat shock experiment, which revealed transiently increased mRNA levels for chloroplastic GS2 but unchanged protein levels.Permissive synthesis of β-carotene and chloroplastic glutamine synthetase (GS2) at 30°C in the presence of amitrole or the tigrina-o34 mutation might be due to two alternative pathways of ionone ring formation using either lycopene or neurosporene as substrates for cyclization.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-5028
    Keywords: Chlamydomonas ; cytochrome b6f complexes ; cytochrome b6 ; RNA editing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have introduced a proline codon in place of a leucine codon at position 204 of the petB gene of Chlamydomonas reinhardtii. This gene modification mimics the presence of proline codons at the same position in the petB genes of maize and tobacco, which are subsequently edited to leucine codons at the RNA level. Following transformation, we observed no editing at this position in C. reinhardtii, independent of the type of proline codon we have used: the CCA codon, edited in maize, or a CCT codon. Strains carrying the introduced mutation were non phototrophic and displayed a block in photosynthetic electron transfer, consistent with a lack of cytochrome b6f activity. Thus the presence of a proline residue at position 204 in cytochrome b6 is detrimental to photosynthesis. We show that the mutant phenotype arose from a defective assembly of cytochrome b6f complexes and not from altered electron transfer properties in the assembled protein complex. Biochemical comparison of the proline-containing transformants with a cytochrome b6 mutant deficient in heme-attachment indicates that their primary defect is at the level of assembly of apocytochrome b6 with the bh heme, thereby preventing assembly of the whole cytochrome b6f complex.
    Type of Medium: Electronic Resource
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