Extensive histone post-translational modification in honey bees

被引:58
作者
Dickman, Mark J. [1 ]
Kucharski, Robert [2 ]
Maleszka, Ryszard [2 ]
Hurd, Paul J. [3 ]
机构
[1] Univ Sheffield, ChELSI Inst, Dept Chem & Biol Engn, Sheffield S1 3JD, S Yorkshire, England
[2] Australian Natl Univ, Res Sch Biol, Canberra, ACT 0200, Australia
[3] Univ London, Sch Biol & Chem Sci, London E1 4NS, England
基金
英国医学研究理事会; 澳大利亚研究理事会;
关键词
Apis mellifera; Mass spectrometry; Social insect; Phenotypic polymorphism; Developmental canalization; Epigenetic modifications; DNA METHYLATION; H3; CHROMATIN; PATTERNS; CPG;
D O I
10.1016/j.ibmb.2012.11.003
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
Histone post-translational modifications (FTMs) play a key role in regulating a variety of cellular processes including the establishment, maintenance and reversal of transcriptional programmes in eukaryotes. However, little is known about such modifications in the economically and ecologically important insect pollinator, the honey bee (Apis mellifera). Using mass spectrometry approaches, we show that histone H3.1, H3.3 and H4 of the honey bee are extensively modified by lysine acetylation and lysine methylation. We analysed histones isolated from queen ovaries and 96 hr-old larvae, in toto we quantified 23 specific modification states on 23 distinct peptides. In addition, we have identified and characterised patterns of histone PTMs that reside on the same peptide, generating detailed combinatorial information. Overall, we observed similar profiles of histone FTMs in both samples, with combinatorial patterns of lysine methylations on H3K27 and H3K36 more frequently identified in histones extracted from queen ovaries than from larvae. To our knowledge, this comprehensive dataset represents the first identification and quantitation of histone PTMs in this eusocial insect and emerging epigenetic model. (C) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码:125 / 137
页数:13
相关论文
共 40 条
[1]   The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly [J].
Ahmad, K ;
Henikoff, S .
MOLECULAR CELL, 2002, 9 (06) :1191-1200
[2]  
[Anonymous], ENCY MOL CELL BIOL M
[3]   Spatial distribution of di- and tri-methyl lysine 36 of histone H3 at active genes [J].
Bannister, AJ ;
Schneider, R ;
Myers, FA ;
Thorne, AW ;
Crane-Robinson, C ;
Kouzarides, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (18) :17732-17736
[4]   Regulation of chromatin by histone modifications [J].
Bannister, Andrew J. ;
Kouzarides, Tony .
CELL RESEARCH, 2011, 21 (03) :381-395
[5]   High-resolution profiling of histone methylations in the human genome [J].
Barski, Artern ;
Cuddapah, Suresh ;
Cui, Kairong ;
Roh, Tae-Young ;
Schones, Dustin E. ;
Wang, Zhibin ;
Wei, Gang ;
Chepelev, Iouri ;
Zhao, Keji .
CELL, 2007, 129 (04) :823-837
[6]   Linking DNA methylation and histone modification: patterns and paradigms [J].
Cedar, Howard ;
Bergman, Yehudit .
NATURE REVIEWS GENETICS, 2009, 10 (05) :295-304
[7]   Histone H1 Subtypes Differentially Modulate Chromatin Condensation without Preventing ATP-Dependent Remodeling by SWI/SNF or NURF [J].
Clausell, Jaime ;
Happel, Nicole ;
Hale, Tracy K. ;
Doenecke, Detlef ;
Beato, Miguel .
PLOS ONE, 2009, 4 (10)
[8]   Epigenetics and the environment: emerging patterns and implications [J].
Feil, Robert ;
Fraga, Mario F. .
NATURE REVIEWS GENETICS, 2012, 13 (02) :97-109
[9]   DNA methylation dynamics, metabolic fluxes, gene splicing, and alternative phenotypes in honey bees [J].
Foret, Sylvain ;
Kucharski, Robert ;
Pellegrini, Matteo ;
Feng, Suhua ;
Jacobsen, Steven E. ;
Robinson, Gene E. ;
Maleszka, Ryszard .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2012, 109 (13) :4968-4973
[10]   The Methyl-CpG-binding protein MeCP2 links DNA methylation to histone methylation [J].
Fuks, F ;
Hurd, PJ ;
Wolf, D ;
Nan, XS ;
Bird, AP ;
Kouzarides, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (06) :4035-4040