ArticlePlanta1996
Comparison of the expression of a plastidic chaperonin 60 in different plant tissues and under photosynthetic and non-photosynthetic conditions.
Article in Planta, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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0 citing papers in PubMed, 16 citations in OpenAlex.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A partial cDNA which codes for the beta-subunit of a plastidic chaperonin 60 (cpn60-beta) 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-beta sequence determined for a monocotyledonous plant. Specific antibodies against cpn60-beta were affinity-purified from an antiserum raised against the total soluble protein fraction of ribosome-deficient plastids. The localization of cpn60-beta in chloroplasts or non-green plastids was confirmed by immunodetection in Percoll gradient-purified organelles. The expression and occurrence of cpn60-beta was analysed by immunoblotting with the specific antibodies and Northern hybridization. The cpn60-beta 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-beta protein was not enhanced by a heat-shock treatment at 42 degrees C. The cpn60-beta transcript and protein were more strongly expressed in various non-green, for instance etiolated, 70S-ribosome-deficient 32 degree C-grown, or herbicide-bleached tissues, than in green leaves of rye. A rapid increase in the cpn60-beta 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-beta transcript was totally suppressed in the presence of 2% sucrose. Inhibitor treatments suggested that the change in cpn60-beta 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-beta were detected in tomato chromoplasts and in the yellow flower petals of Narcissus. Low levels of cpn60-beta were detected in root tissue.
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