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  • 1
    Electronic Resource
    Electronic Resource
    Comparison of the expression of a plastidic chaperonin 60 in different plant tissues and under photosynthetic and non-photosynthetic conditions (1996)
    Springer
    Planta 200 (1996), S. 326-334 
    Details
    ISSN: 1432-2048
    Keywords: Chaperone ; Chloroplasts ; Chromoplasts ; Heat-shock protein ; Secale
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A partial cDNA which codes for the β-subunit of a plastidic chaperonin 60 (cpn60-β) from rye (Secale cereale L.) leaves was identified and sequenced, except for 46 amino acids of the N-terminus of the mature protein and the transit sequence. This is the first cpn60-β sequence determined for a monocotyledonous plant. Specific antibodies against cpn60-β were affinity-purified from an antiserum raised against the total soluble protein fraction of ribosome-deficient plastids. The localization of cpn60-β in chloroplasts or non-green plastids was confirmed by immunodetection in Percoll gradient-purified organelles. The expression and occurrence of cpn60-β was analysed by immunoblotting with the specific antibodies and Northern hybridization. The cpn60-β protein was constitutively expressed in various green and non-green tissues. It was evenly distributed along the major part of a rye leaf, while highest transcript levels occurred in the youngest and oldest leaf sections. The expression of the cpn60-β protein was not enhanced by a heat-shock treatment at 42 °C. The cpn60-β transcript and protein were more strongly expressed in various non-green, for instance etiolated, 70S-ribosome-deficient 32 °C-grown, or herbicide-bleached tissues, than in green leaves of rye. A rapid increase in the cpn60-β transcript level was also observed when green leaves were transferred from light to darkness while the protein level was not affected. The dark-induced increase in the cpn60-β transcript was totally suppressed in the presence of 2% sucrose. Inhibitor treatments suggested that the change in cpn60-β transcript level was not related to changes of the ATP supply of the tissue. While the large subunit of the photosynthetic protein ribulose-1,5-bisphosphate carboxylase was largely degraded during ripening of tomato fruits, high levels of cpn60-β were detected in tomato chromoplasts and in the yellow flower petals of Narcissus. Low levels of cpn60-β were detected in root tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00200300
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  • 2
    Electronic Resource
    Electronic Resource
    Origin and developmental changes of envelope proteins and translocator activities from plastids of Secale cereale L. (1985)
    Springer
    Planta 166 (1985), S. 452-465 
    Details
    ISSN: 1432-2048
    Keywords: Adenylate kinase ; ATPase (plastid envelope) ; Phosphate translocator ; Plastid envelope ; Protein synthesis (plastid) ; Secale (plastid envelope) ; Translocator (dicarboxylate, phosphate)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To determine the sites of synthesis of chloroplast-envelope proteins, we have analysed several enzyme and translocator functions ascribed to the envelope membranes, and investigated the envelope polypeptide composition of plastids isolated from 70S ribosome-deficient leaves of rye (Secale cereale L.) generated by growing the plants at a temperature of 32°C. Since the ribosomedeficient plastids are also achlorophyllous in light-grown leaves, not only were chloroplasts from mature, green leaves used for comparison, but also those from yellowing, aged leaves as well as etioplasts from dark-grown leaves raised at a temperature of 22° C. A majority of the plastidenvelope polypeptides appeared to be of cytoplasmic origin. The envelopes of ribosome-deficient plastids possessed ATPase (EC 3.6.1.3) activity; this was not, however, dependent on divalent cations, in contrast to the Mn2+- or Mg2+-dependent ATPase which is associated with chloroplast envelopes. Adenylate kinase (EC 2.7.4.3) was present in the stromal fraction of ribosome-deficient plastids and the stromal form of this enzyme is, therefore, of cytoplasmic origin. In contrast to previous findings, adenylate kinase was not, however, specifically associated with the chloroplast-envelope membranes, either in rye or in spinach. Measurements of the uptake of l-[14C]-malate into ribosome-deficient plastids indicated the presence and cytoplasmic origin of the dicarboxylate translocator. Malate uptake into rye etioplasts was, however, low. The phosphate translocator was assayed by the uptake of 3-phospho-[14C]glycerate. While rapid 3-phosphoglycerate uptake was observed for rye chloroplasts and etioplasts, it was hardly detectable for ribosome-deficient, plastids and rather low for chloroplasts from aged leaves. A polypeptide of M r approx. 30000 ascribed to the phosphate translocator was greatly reduced in the envelope patterns of ribosome-deficient plastids and of chloroplasts from aged leaves.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00391269
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