PXD007289

PXD007289 is an original dataset announced via ProteomeXchange.

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

Revision	Datetime	Status	ChangeLog Entry
0	2017-08-17 08:13:25	ID requested
⏵ 1	2018-10-23 15:43:52	announced

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]

curator keyword: Biological

submitter keyword: Acinetobacter baumannii, Acetylome, LC MSMS

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

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PRIDE project URI

• PRIDE
  1. PXD007289
     1. Label: PRIDE project
     2. Name: Acetylome of Acinetobacter baumannii SK17 reveals a highly-conserved modification of histone-like protein HU