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   <subfield code="a">10.1007/BF00200300</subfield>
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   <subfield code="a">(NATIONALLICENCE)springer-10.1007/BF00200300</subfield>
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   <subfield code="a">Comparison of the expression of a plastidic chaperonin 60 in different plant tissues and under photosynthetic and non-photosynthetic conditions</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[G. Schmitz, M. Schmidt, J. Feierabend]</subfield>
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   <subfield code="a">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.</subfield>
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   <subfield code="a">Springer-Verlag, 1996</subfield>
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   <subfield code="a">Chaperone</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Chloroplasts</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Chromoplasts</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Heat-shock protein</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Secale</subfield>
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   <subfield code="a">cpn60 : chaperonin 60</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">HSP : heat shock protein</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">Rubisco : ribulose-1,5-bisphosphate carboxylase/oxygenase</subfield>
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   <subfield code="a">Schmitz</subfield>
   <subfield code="D">G.</subfield>
   <subfield code="u">Botanisches Institut, J.W. Goethe-Universität, Postfach 11 1932, D-60054, Frankfurt am Main, Germany</subfield>
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   <subfield code="a">Schmidt</subfield>
   <subfield code="D">M.</subfield>
   <subfield code="u">Botanisches Institut, J.W. Goethe-Universität, Postfach 11 1932, D-60054, Frankfurt am Main, Germany</subfield>
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   <subfield code="a">Feierabend</subfield>
   <subfield code="D">J.</subfield>
   <subfield code="u">Botanisches Institut, J.W. Goethe-Universität, Postfach 11 1932, D-60054, Frankfurt am Main, Germany</subfield>
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   <subfield code="g">200/3(1996-11-01), 326-334</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">Springer special CC-BY-NC licence</subfield>
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