Chemical Proteomic Profiling of Protein Fatty-Acylation in Microbial Pathogens

被引:3
|
作者
Peng, Tao [1 ]
Hang, Howard C. [2 ]
机构
[1] Peking Univ, Shenzhen Grad Sch, Sch Chem Biol & Biotechnol, State Key Lab Chem Oncogen, Shenzhen 518055, Guangdong, Peoples R China
[2] Rockefeller Univ, Lab Chem Biol & Microbial Pathogenesis, New York, NY 10065 USA
来源
关键词
N-MYRISTOYLTRANSFERASE; S-PALMITOYLATION; GLOBAL ANALYSIS; DRUG TARGET; LIPIDATION; REPORTERS; REVEALS; MYRISTOYLATION; IDENTIFICATION; INHIBITION;
D O I
10.1007/82_2018_126
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein fatty-acylation describes the covalent modification of protein with fatty acids during or after translation. Chemical proteomic profiling methods have provided new opportunities to explore protein fatty-acylation in microbial pathogens. Recent studies suggest that protein fatty-acylation is essential to survival and pathogenesis of eukaryotic pathogens such as parasites and fungi. Moreover, fatty-acylation in host cells can be exploited or manipulated by pathogenic bacteria. Herein, we first review the prevalent classes of fatty-acylation in microbial pathogens and the chemical proteomic profiling methods for their global analysis. We then summarize recent fatty-acylation profiling studies performed in eukaryotic pathogens and during bacterial infections, highlighting how they contribute to functional characterization of fatty-acylation under these contexts.
引用
收藏
页码:93 / 110
页数:18
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