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Malonyl-Proteome Profiles of Staphylococcus Aureus Reveal Lysine Malonylation Modification in Enzymes Involved in Energy Metabolism
Aixiang HUANG
Yunnan Agricultural University
Corresponding Author
License:
This work is licensed under a CC BY 4.0 License. Read Full License
View the published version at Proteome Science.
Background
Protein lysine malonylation, a novel post-translational modification (PTM), has been recently linked with energy metabolism in bacteria. Staphylococcus aureus is the third most important foodborne pathogen worldwide. Nonetheless, substrates and biological roles of malonylation are still poorly understood in this pathogen.
Results
Using anti-malonyl-lysine antibody enrichment and high-resolution LC-MS/MS analysis, 440 lysine-malonylated sites were identified in 281 proteins of S. aureus strain. The frequency of valine in position -1 and alanine at +2 and +4 position was high. KEGG pathway analysis showed that six categories were highly enriched: ribosome, glycolysis/gluconeogenesis, pentose phosphate pathway (PPP), tricarboxylic acid cycle (TCA), valine, leucine, isoleucine degradation, and aminoacyl-tRNA biosynthesis. In total, 31 malonylated sites in S. aureus shared homology with lysine-malonylated sites previously identified in E. coli, indicating malonylated proteins are highly conserved among bacteria. Key rate-limiting enzymes in central carbon metabolic pathways were also found to be malonylated in S. aureus, namely pyruvate kinase (PYK), 6-phosphofructokinase, phosphoglycerate kinase, dihydrolipoyl dehydrogenase, and F1F0-ATP synthase. Notably, malonylation sites were found at or near protein active sites, including KH domain, thioredoxin, alanine dehydrogenase (ALD), dihydrolipoyl dehydrogenase (LpdA), pyruvate oxidase CidC and catabolite control protein A (CcpA), thus suggesting that lysine malonylation may affect the activity of such enzymes.
Conclusions
Data presented herein expand the current knowledge on lysine malonylation in prokaryotes and indicate potential roles of protein malonylation in bacterial physiology and metabolism.
Keywords
post-translational modification (PTM), lysine malonylation, Staphylococcus aureus, energy metabolism, enzymes
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Reviewer #2 agreed
On 23 Nov, 2020
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Reviewer #1 agreed
On 22 Nov, 2020
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On 21 Nov, 2020
This version was not preprinted
Version 1
Posted 23 Oct, 2020
Published
On 12 Jan, 2021
No community comments so far
Review #2 received
Received 10 Nov, 2020
Editorial decision: Major revision
On 10 Nov, 2020
Reviewer #4 agreed
On 04 Nov, 2020
Review #3 received
Received 02 Nov, 2020
Reviewer #3 agreed
On 29 Oct, 2020
Review #1 received
Received 29 Oct, 2020
Reviewer #2 agreed
On 27 Oct, 2020
Reviewers invited
Invitations sent on 26 Oct, 2020
Reviewer #1 agreed
On 26 Oct, 2020
First submitted
On 19 Oct, 2020
Editor assigned
On 19 Oct, 2020
Submission checks complete
On 18 Oct, 2020
Editor invited
On 18 Oct, 2020
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This preprint is under consideration at Proteome Science. A preprint is a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Research
Malonyl-Proteome Profiles of Staphylococcus Aureus Reveal Lysine Malonylation Modification in Enzymes Involved in Energy Metabolism
Aixiang HUANG
Yunnan Agricultural University
Corresponding Author
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Published
Version (no preprint)
Posted 06 Dec, 2020
Review #2 received
Received 06 Dec, 2020
Editorial decision: Minor revision
On 06 Dec, 2020
Review #1 received
Received 26 Nov, 2020
Reviewer #2 agreed
On 23 Nov, 2020
Reviewers invited
Invitations sent on 22 Nov, 2020
Reviewer #1 agreed
On 22 Nov, 2020
Editor assigned
On 21 Nov, 2020
Submission checks complete
On 21 Nov, 2020
Editor invited
On 21 Nov, 2020
This version was not preprinted
Version 1
Posted 23 Oct, 2020
Published
On 12 Jan, 2021
No community comments so far
Review #2 received
Received 10 Nov, 2020
Editorial decision: Major revision
On 10 Nov, 2020
Reviewer #4 agreed
On 04 Nov, 2020
Review #3 received
Received 02 Nov, 2020
Reviewer #3 agreed
On 29 Oct, 2020
Review #1 received
Received 29 Oct, 2020
Reviewer #2 agreed
On 27 Oct, 2020
Reviewers invited
Invitations sent on 26 Oct, 2020
Reviewer #1 agreed
On 26 Oct, 2020
First submitted
On 19 Oct, 2020
Editor assigned
On 19 Oct, 2020
Submission checks complete
On 18 Oct, 2020
Editor invited
On 18 Oct, 2020
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
Subject Areas
Bioinformatics
License:
This work is licensed under a CC BY 4.0 License. Read Full License
View the published version at Proteome Science.
Background
Protein lysine malonylation, a novel post-translational modification (PTM), has been recently linked with energy metabolism in bacteria. Staphylococcus aureus is the third most important foodborne pathogen worldwide. Nonetheless, substrates and biological roles of malonylation are still poorly understood in this pathogen.
Results
Using anti-malonyl-lysine antibody enrichment and high-resolution LC-MS/MS analysis, 440 lysine-malonylated sites were identified in 281 proteins of S. aureus strain. The frequency of valine in position -1 and alanine at +2 and +4 position was high. KEGG pathway analysis showed that six categories were highly enriched: ribosome, glycolysis/gluconeogenesis, pentose phosphate pathway (PPP), tricarboxylic acid cycle (TCA), valine, leucine, isoleucine degradation, and aminoacyl-tRNA biosynthesis. In total, 31 malonylated sites in S. aureus shared homology with lysine-malonylated sites previously identified in E. coli, indicating malonylated proteins are highly conserved among bacteria. Key rate-limiting enzymes in central carbon metabolic pathways were also found to be malonylated in S. aureus, namely pyruvate kinase (PYK), 6-phosphofructokinase, phosphoglycerate kinase, dihydrolipoyl dehydrogenase, and F1F0-ATP synthase. Notably, malonylation sites were found at or near protein active sites, including KH domain, thioredoxin, alanine dehydrogenase (ALD), dihydrolipoyl dehydrogenase (LpdA), pyruvate oxidase CidC and catabolite control protein A (CcpA), thus suggesting that lysine malonylation may affect the activity of such enzymes.
Conclusions
Data presented herein expand the current knowledge on lysine malonylation in prokaryotes and indicate potential roles of protein malonylation in bacterial physiology and metabolism.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7