PXD007289 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Acetylome of Acinetobacter baumannii SK17 reveals a highly-conserved modification of histone-like protein HU |
Description | Lysine acetylation is a prevalent post-translational modification in both eukaryotes and prokaryotes. Whereas this modification is known to play pivotal roles in eukaryotes, the function and extent of this modification in prokaryotic cells remain largely unexplored. Here we report the acetylome of a pair of antibiotic-sensitive and -resistant nosocomial pathogen Acinetobacter baumannii SK17-S and SK17-R. A total of 145 lysine acetylation sites on 125 proteins was identified, and there are 23 acetylated proteins found in both strains, including histone-like protein HU which was found to be acetylated at Lys13. HU is a dimeric DNA-binding protein critical for maintaining chromosomal architecture and other DNA-dependent functions. To analyze the effects of site-specific acetylation, homogenously Lys13-acetylated HU protein, HU(K13ac) was prepared by genetic code expansion. Whilst not exerting an obvious effect on the oligomeric state, Lys13 acetylation alters both the thermal stability and DNA binding kinetics of HU. Accordingly, this modification likely destabilizes the chromosome structure and regulates bacterial gene transcription. By preparing and characterizing site-specifically acetylated bacterial protein for the first time, this work indicates that acetyllysine plays an important role in bacterial epigenetics and presents a promising target against bacterial infections. |
HostingRepository | PRIDE |
AnnounceDate | 2018-10-23 |
AnnouncementXML | Submission_2018-10-23_15:43:51.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD007289 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Jhih-Tain /Oliver Yang |
SpeciesList | scientific name: Acinetobacter baumannii; NCBI TaxID: 470; |
ModificationList | Oxidation; Acetyl; Carbamidomethyl |
Instrument | LTQ Orbitrap Velos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2017-08-17 08:13:25 | ID requested | |
⏵ 1 | 2018-10-23 15:43:52 | announced | |
Publication List
Liao JH, Tsai CH, Patel SG, Yang JT, Tu IF, Lo Cicero M, Lipka-Lloyd M, Wu WL, Shen WJ, Ho MR, Chou CC, Sharma GR, Okanishi H, Luk LYP, Tsai YH, Wu SH, SK17 Reveals a Highly-Conserved Modification of Histone-Like Protein HU. Front Mol Biosci, 4():77(2017) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: Acinetobacter baumannii, Acetylome, LC MSMS |
Contact List
Jiahn-Haur Liao |
contact affiliation | Academia Sinica Institute of Biological Chemistry(IBC), Dr. Shih-Hsiung Wu's lab, Taipei, Taiwan (R.O.C.) |
contact email | liaojh@gate.sinica.edu.tw |
lab head | |
Jhih-Tain /Oliver Yang |
contact affiliation | Academia Sinica |
contact email | tai-ji-fox@hotmail.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD007289
- Label: PRIDE project
- Name: Acetylome of Acinetobacter baumannii SK17 reveals a highly-conserved modification of histone-like protein HU