The role of peptide deformylase in protein biosynthesis: A proteomic study
| العنوان: | The role of peptide deformylase in protein biosynthesis: A proteomic study |
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| المؤلفون: | Knut Büttner, Heike Brötz, Falko Hochgräfe, Christoph Freiberg, Dörte Becher, Michael Hecker, Julia E. Bandow |
| المصدر: | PROTEOMICS. 3:299-306 |
| بيانات النشر: | Wiley, 2003. |
| سنة النشر: | 2003 |
| مصطلحات موضوعية: | Spectrometry, Mass, Electrospray Ionization, Time Factors, Proteome, Electrospray ionization, Molecular Sequence Data, Bacillus subtilis, Hydroxamic Acids, Biochemistry, Mass Spectrometry, Amidohydrolases, chemistry.chemical_compound, Peptide deformylase, Cytosol, Bacterial Proteins, Mutant protein, Protein biosynthesis, Electrophoresis, Gel, Two-Dimensional, Amino Acid Sequence, Isoelectric Point, Actinonin, Molecular Biology, biology, biology.organism_classification, Anti-Bacterial Agents, Protein Structure, Tertiary, Isoelectric point, chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Mutation, Peptide deformylase activity, Peptides |
| الوصف: | Recently we investigated the influence of classical and emerging antibiotics on the proteome of Bacillus subtilis including in our studies actinonin, a potent novel inhibitor of peptide deformylase. The protein synthesis pattern under actinonin treatment changed so dramatically that a direct comparison to the control pattern was impossible. Dual channel imaging revealed that actinonin treatment caused the majority of newly synthesised proteins to accumulate in spots different from the ones usually observed, indicating a more acidic isoelectric point. Two strategies were used to investigate the nature of the charge shift. In the first place, protein patterns of a conditional peptide deformylase mutant under nonrepressing and repressing conditions were compared. Secondly, several protein pairs excised from two-dimensional (2-D) gels of the peptide deformylase mutant, exponentially growing untreated wild-type and the actinonin treated wild-type were investigated with matrix-assisted laser desorption/ionization and electrospray ionization (ESI) time of flight mass spectrometry (TOF MS) for the existence of N-terminal formylation. Under nonrepressing conditions the mutant protein pattern resembled that of the wild-type. The loss of peptide deformylase activity under repressing conditions led to the same pI shift observed for actinonin treatment in the wild-type. Quadrupole TOF-MS on 11 protein pairs proved that the remaining N-terminal formyl residue was indeed responsible for the charge shift. Eight of these protein pairs were also present on 2-D gels of exponentially growing B. subtilis, where the more acidic, still formylated protein species represented the smaller parts. |
| تدمد: | 1615-9861 1615-9853 |
| DOI: | 10.1002/pmic.200390043 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30730837315b094030fbc4d3cd5cb029 https://doi.org/10.1002/pmic.200390043 |
| Rights: | CLOSED |
| رقم الانضمام: | edsair.doi.dedup.....30730837315b094030fbc4d3cd5cb029 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 16159861 16159853 |
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| DOI: | 10.1002/pmic.200390043 |