Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.5.1.47 (cysteine synthase)
 625 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In this study, the phosphoproteome of Corynebacterium glutamicum, an industrially important soil bacterium of the Corynebacterium/Mycobacterium/Nocardia (CMN) group of Gram-positive bacteria, was investigated by two different detection methods: first, by in vivo radio-labeling using [(33)P]-phosphoric acid with subsequent autoradiography and second, by immunostaining with phosphoamino acid-specific monoclonal antibodies. After two-dimensional gel electrophoresis (2-DE), around 60 [(33)P]-labeled protein spots were visualized and around 90 antibody-decorated protein spots detected; 31 of the protein spots were detected with both methods. By peptide mass fingerprinting, 41 different proteins were identified, namely 5-enolpyruvylshikimate 3-phosphate synthase, aconitase, acyl-CoA carboxylase, acyl-CoA synthetase, ATP (synthase alpha- and beta-chain), carbamoyl-phosphate synthase, citrate synthase, cysteine synthase, DnaK, the elongation factors G, P, Ts and Tu, enolase, fructose bisphosphate aldolase, fumarase, Gap dehydrogenase, glutamine synthetase I, glycine hydroxymethyltransferase, GroEL2, GTPase, heat-inducible transcriptional repressor DnaJ2, inorganic pyrophosphatase, isocitrate dehydrogenase, ketol-acid reductoisomerase, lactate dehydrogenase, leucine-tRNA ligase, lipoamide dehydrogenase, methionine synthase, O-acetylhomoserine sulfhydrylase, pyruvate carboxylase, pyruvate kinase, pyruvate oxidase, ribosomal protein S1, RNA polymerase (beta-subunit), succinyl-CoA:CoA transferase, transketolase and UDP-N-acetylmuramoyl-L-alanine ligase, besides a hypothetical 35k protein and a hypothetical glucose kinase. Both detection techniques were used to create a phosphoproteome map. Additionally, the influence of nitrogen deprivation on the phosphoproteome of C. glutamicum was investigated.
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PMID:Towards a phosphoproteome map of Corynebacterium glutamicum. 1292 88

The response of E. coli to Hg(2+) exposure was investigated using proteomic and metalloproteomic approaches. E. coli was cultured in the LB medium containing HgCl2 and/or selenomethionine. The growth curve of E. coli was measured to estimate the toxicity of Hg(2+) or selenomethionine. After two-dimensional gel electrophoresis (2-DE), distribution of Hg in 2-DE gel was detected with synchrotron radiation X-ray fluorescence (SRXRF) at 4W1B, Beijing Synchrotron Radiation Facility. The proteins with differential expression and those containing Hg were identified with electrospray ionization tandem mass spectrometry (ESI-MS/MS) and peptide mass fingerprinting analysis. The results showed that Hg(2+) can inhibit the growth of E. coli, while supplement of selenomethionine can shorten the lag period induced by Hg(2+), indicating an antagonistic effect of selenomethionine against Hg(2+) toxicity. Mechanistically, Hg was observed to be able to bind pyruvate kinase, a glycolytic enzyme, and modulate the expression of five other proteins, including down-regulation of outer membrane protein W and up-regulation of transcription termination factor rho, cysteine synthase, transaldolase A and alkyl hydroperoxide reductase subunit C. Therefore, our results indicated that mercury may influence osmosis of plasma membrane, antioxidant defense, and glycometabolism of the microorganism. This study demonstrates the high sensitivity of SRXRF in identifying metal-associated proteins compared to conventional proteomic approaches.
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PMID:Cellular response of E. coli upon Hg2+ exposure--a case study of advanced nuclear analytical approach to metalloproteomics. 2377 Nov 80