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  • Cell wall pH  (2)
  • photosynthesis  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 148 (1980), S. 510-512 
    ISSN: 1432-2048
    Keywords: Auxin ; Cell wall pH ; Growth (roots) ; Proton flux and growth ; Root growth ; Zea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract At concentrations inhibitory to the elongation of corn (Zea mays L.) roots, the auxins, indole-3-acetic acid (IAA) and α-naphthaleneacetic acid (α-NAA), cause an increase in the pH of the bathing medium; this increase occurs with an average latent period shorter than the latent period for the inhibitory effect of these auxins on elongation. Indole-2-carboxylic acid, an inactive structural analogue of IAA, and β-naphthaleneacetic acid, an inactive analogue of α-NAA, affect neither growth nor the pH of the medium. Since acid pH is known to promote and basic pH to inhibit root elongation, the data are consistent with the hypothesis that hormone-induced modification of cell-wall pH plays a role in the control of elongation of roots, as has been proposed for elongation of stems and coleoptiles.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Planta 148 (1980), S. 510-512 
    ISSN: 1432-2048
    Keywords: Auxin ; Cell wall pH ; Growth (roots) ; Proton flux and growth ; Root growth ; Zea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract At concentrations inhibitory to the elongation of corn (Zea mays L.) roots, the auxins, indole-3-acetic acid (IAA) and α-naphthaleneacetic acid (α-NAA), cause an increase in the pH of the bathing medium; this increase occurs with an average latent period shorter than the latent period for the inhibitory effect of these auxins on elongation. Indole-2-carboxylic acid, an inactive structural analogue of IAA, and β-naphthaleneacetic acid, an inactive analogue of α-NAA, affect neither growth nor the pH of the medium. Since acid pH is known to promote and basic pH to inhibit root elongation, the data are consistent with the hypothesis that hormone-induced modification of cell-wall pH plays a role in the control of elongation of roots, as has been proposed for elongation of stems and coleoptiles.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
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  • 3
    ISSN: 1573-5079
    Keywords: EPR ; iron-sulphur ; photosynthesis ; P700 ; reaction center
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A site directed mutant of the Photosystem I reaction center of Chlamydomonas reinhardtii has been described previously. [Hallahan et al. (1995) Photosynth Res 46: 257–264]. The mutation, PsaA: D576L, changes the conserved aspartate residue adjacent to one of the cysteine ligands binding the Fe-SX center to PsaA. The mutation, which prevents photosynthetic growth, was observed to change the EPR spectrum of the Fe-SA/B centers bound to the PsaC subunit. We suggested that changes in binding of PsaC to the PsaA/PsaB reaction center prevented efficient electron transfer. Second site suppressors of the mutation have now been isolated which have recovered the ability to grow photosynthetically. DNA analysis of four suppressor strains showed the original D576L mutation is intact, and that no mutations are present elsewhere within the Fe-SX binding region of either PsaA or PsaB, nor within PsaC or PsaJ. Subsequent genetic analysis has indicated that the suppressor mutation(s) is nuclear encoded. The suppressors retain the altered binding of PsaC, indicating that this change is not the cause of failure to grow photosynthetically. Further analysis showed that the rate of electron transfer from the quinone electron carrier A1 to Fe-SX is slowed in the mutant (by a factor of approximately two) and restored to wild type rates in the suppressors. ENDOR spectra of A1 ·– in wild-type and mutant preparations are identical, indicating that the electronic structure of the phyllosemiquinone is not changed. The results suggest that the quinone to Fe-SX center electron transfer is sensitive to the structure of the iron-sulfur center, and may be a critical step in the energy conversion process. They also indicate that the structure of the reaction center may be modified as a result of changes in proteins outside the core of the reaction center.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-5079
    Keywords: Chlamydomonas ; mutation ; photosynthesis ; Photosystem 1 ; PsaA ; reaction center
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The psaA and psaB genes of the chloroplast genome in oxygenic photosynthetic organisms code for the major peptides of the Photosystem 1 reaction center. A heterodimer of the two polypeptides PsaA and PsaB is thought to bind the reaction center chlorophyll, P700, and the early electron acceptors A0, A1 and Fe-SX. Fe-SX is a 4Fe4S center requiring 4 cysteine residues as ligands from the protein. As PsaA and PsaB have only three and two conserved cysteine residues respectively, it has been proposed by several groups that Fe-SX is an unusual inter-peptide center liganded by two cysteines from each peptide. This hypothesis has been tested by site directed mutagenesis of PsaA residue C575 and the adjacent D576. The C575D mutant does not assemble Photosystem 1. The C575H mutant contains a photoxidisable chlorophyll with EPR properties of P700, but no other Photosystem 1 function has been detected. The D576L mutant assembles a modified Photosystem 1 in which the EPR properties of the Fe-SA/B centers are altered. The results confirm the importance of the conserved cysteine motif region in Photosystem 1 structure.
    Type of Medium: Electronic Resource
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