Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Thermally aggregated, endogenous proteins in Escherichia coli cells form the S fraction, which is separable by sucrose density gradient centrifugation. To date, relatively little is known about the mechanisms of elimination of the heat-aggregated proteins from E. coli cells and the composition of the S fraction. We have identified several proteins of the S fraction using 2D-gel electrophoresis and microsequencing. A thermostable II class fructose-1,6-bisphosphate aldolase (Fda protein) appeared to be one of numerous proteins of the S fraction. Fda was purified from E. coli overproducer strain and used as a model substrate for investigation of the role of Hsps in prevention and repair of thermal denaturation of proteins both in vivo and in vitro. We found that the heat inactivation of Fda was reversible and that its reactivation in vivo and in vitro required mainly the assistance of the DnaK/DnaJ chaperone system. The dnaK756 and dnaJ259 mutations had a negative effect on the reactivation of thermally inactivated Fda. Moreover, we showed that the reactivation process in vitro was enhanced when GroEL/GroES were added together with DnaK/DnaJ. GroEL/GroES alone were inefficient in the resolubilization or reactivation of the heat-aggregated Fda. It is supposed that the denaturation of the thermostable Fda in vivo results rather from a temporary and transient deficit of Hsps than from the direct heat effect.
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PMID:DnaK/DnaJ chaperone system reactivates endogenous E. coli thermostable FBP aldolase in vivo and in vitro; the effect is enhanced by GroE heat shock proteins. 1152 40

The present study examines butachlor-induced inhibition of growth, photosynthetic pigments such as chlorophyll a, phycocyanin, allophycocyanin, phycoerythrin, photosystems I and II, whole chain electron transport, oxygen evolution, carbon fixation, ATP content, total thiol and glutathione contents of Aulosira fertilissima. For ascertaining if above mentioned changes are due to disturbance in plasma membrane integrity or proteins, fatty acid profiling and proteomics were done. Gas chromatographic (GC) analysis of fatty acid methyl esters (FAME) depicted a decrease in alpha-linolenic acid (C18:3) which appears responsible for plasma membrane instability. Enhanced lipid peroxidation and electrolyte leakage further attested the butachlor-induced cell damage. Butachlor-treated Aulosira exhibited significant and reproducible alternations in eight proteins as assessed by 2DE and LC-MS analysis of which phycocyanin alpha-chain, allophycocyanin beta-chain, C-phycocyanin alpha-subunit, ATP synthase beta-chain and FBP aldolase were associated with photosynthesis and respiration, peroxiredoxin with antioxidative defense system and GroES and NusB with protein folding and transcription termination respectively. However, a prolonged (15 d) butachlor treatment of Aulosira downregulated all the proteins except NusB. Reverse transcription PCR of the protein genes affirmed that aforesaid proteins were the gene products not artifacts. Downregulated GroES and over expressed NusB are critical proteins for cell death.
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PMID:Understanding butachlor toxicity in Aulosira fertilissima using physiological, biochemical and proteomic approaches. 1987 24