Indirect Evidence for Conformational Changes in Protein from Wheat Seedlings, Preadapted to Chilling and High Temperature

Weidner, Manfred; Heuel, R.

doi:10.1016/s0044-328x(79)80222-6

Cited by 9 publications

(1 citation statement)

References 22 publications

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“…It has long been recognized that gel electrophoretic profiles of plant protein change gradually according to long-term seasonal temperature fluctuations (2,3,18). Few data are available, however, dealing with rapid changes in protein banding patterns as a result of temperature shifts (25,27). The short-lived, heat-labile protein which has been detected by gradient PAGE may possibly play an important role in the investigation of the molecular basis of high temperature influence on wheat-once it has been identified.…”

Section: Methodsmentioning

confidence: 99%

Phenotypical Temperature Adaptation of Protein Synthesis in Wheat Seedlings

Weidner¹,

Mathée²,

Schmitz³

1982

Plant Physiol.

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The phenomenon of phenotypical, or capacity, temperature adaptation (17) of protein synthesis in wheat seedlings, 10 to 12 d old, has been characterized previously (22,24). The optimum temperature, as well as the temperature coefficient (u) of [14C] leucine incorporation in the 'total protein' fraction, seems to be under the control of the preadaptation temperature. Both parameters show lowest values in case of cold-adapted plants, while heat-adapted plants exhibit the highest values.The present investigation deals with the following aspects of the phenomenon. First, we considered it important to probe into the vulnerability, or stability, of this adaptation process against exogenous influences. Thus, dark-grown, etiolated wheat seedlings and fluorophenylalanine-treated plants, with a 50%o inhibition of the rate of protein synthesis, were exposed to different temperature regimes. Second, protein degradation measurements were carried out. A correct assessment of temperature adaptation of protein synthesis requires a knowledge of the turnover rates of the protein moiety which is labeled under the specific conditions applied. Third, we intended to find out if temperature adaptation ofprotein synthesis is a universal phenomenon or if proteins with a deviating

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Section: Methodsmentioning

confidence: 99%

Phenotypical Temperature Adaptation of Protein Synthesis in Wheat Seedlings

Weidner¹,

Mathée²,

Schmitz³

1982

Plant Physiol.

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Heat modification of ribulose-1,5-bisphosphate carboxylase/oxygenase by temperature pretreatment of wheat (Triticum aestivum L.) seedlings

Weidner

Fehling

1985

Planta

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The effect of low-, ambient- and high-temperature pretreatments (48 h at 4° C, 20° C or 36° C) of wheat seedlings (spring wheat Triticum aestivum L., cv. Kolibri) on the solubility properties of ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBPCase; EC 4.1.1.39) was studied. The extractable protein moiety of heat-pretreated plants exhibited increased solubility in dilute buffer (50 mM k-phosphate, pH 6.8), compared with protein extracted from 4° C- or 20° C-plants. The salting-out characteristics for ammonium-sulfate precipitation confirmed this finding since a delayed precipitation of extractable protein from 36°C-plants was observed. Using polyacrylamide gel electrophoresis, the in-vivo temperature-induced differences in protein solubility could be traced back to a change in the solubility of RuBPCase. The RuBPCase was purified from wheat seedlings, and the purified enzyme also exhibited differential solubility. In order to evaluate this further, purified RuBPCase was subjected to probing for conformational properties. A decrease of fluorescence of the RuBPCase 1-anilino-8-naphtalene sulfonate complex revealed that the RuBPCase from 36° C-plants had a more hydrophilic protein surface. Titration of the sulfhydryl groups of native RuBP-Case with 5,5'-dithiobis (2-nitrobenzoic acid) pointed to a reduced accessibility of the R-SH groups in the case of the 36° C-type of RuBPCase. The large subunit of RuBPCase from 4° C/20° C-plants tended to give rise to an artificial lower-molecular-weight polypeptide which could not be found in crude or purified RuBPCase from heat-pretreated wheat seedlings.

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Destruction and reconstitution of the dictyosome in the chrysophycean flagellate,Poterioochromonas malhamensis, after heat-shock, and other heat-shock effects

Schnepf

Schmitt

1981

Protoplasma

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Indirect Evidence for Conformational Changes in Protein from Wheat Seedlings, Preadapted to Chilling and High Temperature

Cited by 9 publications

References 22 publications

Phenotypical Temperature Adaptation of Protein Synthesis in Wheat Seedlings

Phenotypical Temperature Adaptation of Protein Synthesis in Wheat Seedlings

Heat modification of ribulose-1,5-bisphosphate carboxylase/oxygenase by temperature pretreatment of wheat (Triticum aestivum L.) seedlings

Destruction and reconstitution of the dictyosome in the chrysophycean flagellate,Poterioochromonas malhamensis, after heat-shock, and other heat-shock effects

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