The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Cross‐talk between phosphorylation and lysine acetylation in a genome‐reduced bacterium
Open accessAbstract
Protein post-translational modifications (PTMs) represent important regulatory states that when combined have been hypothesized to act as molecular codes and to generate a functional diversity beyond genome and transcriptome. We systematically investigate the interplay of protein phosphorylation with other post-transcriptional regulatory mechanisms in the genome-reduced bacterium Mycoplasma pneumoniae. Systematic perturbations by deletion of its only two protein kinases and its unique protein phosphatase identified not only the protein-specific effect on the phosphorylation network, but also a modulation of proteome abundance and lysine acetylation patterns, mostly in the absence of transcriptional changes. Reciprocally, deletion of the two putative N-acetyltransferases affects protein phosphorylation, confirming cross-talk between the two PTMs. The measured M. pneumoniae phosphoproteome and lysine acetylome revealed that both PTMs are very common, that (as in Eukaryotes) they often co-occur within the same protein and that they are frequently observed at interaction interfaces and in multifunctional proteins. The results imply previously unreported hidden layers of post-transcriptional regulation intertwining phosphorylation with lysine acetylation and other mechanisms that define the functional state of a cell.
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Cites
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Lysine acetylation targets protein complexes and co-regulates major cellular functions
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Microtubule Acetylation Promotes Kinesin-1 Binding and Transport
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Proteome organization in a genome-reduced bacterium
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Self-citationTranscriptome complexity in a genome-reduced bacterium
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Self-citationAn Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function
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Cited by
Protein Analysis by Shotgun/Bottom-up Proteomics
Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491
The growing landscape of lysine acetylation links metabolism and cell signalling
Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324
Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present
Bantscheff, M., Lemeer, S., Savitski, M. M., & Kuster, B. (2012) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-012-6203-4 · Cited by 801
Next-generation proteomics: towards an integrative view of proteome dynamics
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Self-citationGlobal analysis of phosphorylation and ubiquitylation cross-talk in protein degradation
Swaney, D. L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N. J., & Villén, J. (2013) · Nature Methods · doi:10.1038/nmeth.2519 · Cited by 599
Metadata
- Authors
- van Noort, V., Seebacher, J., Bader, S., Mohammed, S., Vonkova, I., Betts, M. J., Kühner, S., Kumar, R., Maier, T., O'Flaherty, M., Rybin, V., Schmeisky, A., Yus, E., Stülke, J., Serrano, L., Russell, R. B., Heck, A. J., Bork, P., & Gavin, A.
- Venue
- Molecular Systems Biology
- Published
- 2012-01
- Volume
- 8
- Issue
- 1
- Pages
- 571-571
- ISSN
- 1744-4292 (ISSN-L)
- OpenAlex
- W2111896563
- Cited by
- 175
- References
- 11
- FWCI
- 12.37
- Type
- journal article
- Language
- en
- Open access
- gold
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- van Noort, V., Seebacher, J., Bader, S., Mohammed, S., Vonkova, I., Betts, M. J., Kühner, S., Kumar, R., Maier, T., O'Flaherty, M., Rybin, V., Schmeisky, A., Yus, E., Stülke, J., Serrano, L., Russell, R. B., Heck, A. J., Bork, P., & Gavin, A. (2012). Cross‐talk between phosphorylation and lysine acetylation in a genome‐reduced bacterium. Molecular Systems Biology. https://doi.org/10.1038/msb.2012.4
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