Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry

被引：1
|
作者：
Fernandez-Rojas, Meiby [1 ]
Fuller, Cassandra N. [1 ]
Tose, Lilian Valadares [1 ]
Willetts, Matthew [2 ]
Park, Melvin A. [2 ]
Bhanu, Natarajan, V [3 ]
Garcia, Benjamin A. [3 ]
Fernandez-Lima, Francisco [1 ,4 ]
机构：
[1] Florida Int Univ, Dept Chem & Biochem, Miami, FL 33199 USA
[2] Bruker Daltonics Inc, Billerica, MA USA
[3] Washington Univ, Sch Med, St Louis, MO USA
[4] Florida Int Univ, Biomol Sci Inst, Miami, FL 33199 USA
来源：
JOVE-JOURNAL OF VISUALIZED EXPERIMENTS | 2024年 / 203期
基金：
美国国家科学基金会;
关键词：
NUCLEOSOME CORE PARTICLE; POSTTRANSLATIONAL MODIFICATIONS; CRYSTAL-STRUCTURE; CHROMATIN; BIOMARKERS;
D O I：
10.3791/65589
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Histone proteins are highly abundant and conserved among eukaryotes and playa large role in gene regulation as a result of structures known as posttranslational modifications (PTMs). Identifying the position and nature of each PTM or pattern of PTMs in reference to external or genetic factors allows this information to be statistically correlated with biological responses such as DNA transcription ,replication, or repair. In the present work, a high-throughput analytical protocol for the detection of histone PTMs from biological samples is described. The use of complementary liquid chromatography, trapped ion mobility spectrometry, and time-of-flight mass spectrometry (LC-TIMS-ToF MS/MS) enables the separation and PTM assignment of the most biologically relevant modifications in a single analysis. The described approach takes advantage of recent developments in dependent data acquisition (DDA) using parallel accumulation in the mobility trap, followed by sequential fragmentation and collision-induced dissociation. Histone PTMs are confidently assigned based on their retention time, mobility, and fragmentation pattern.
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页数：20
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