874b6b80ca09e346e07c32a0cc516fa3  pmc_29495465.pdf
a1db26f25036b85b1e1e0cac02e7cae854d2cd12  pmc_29495465.pdf
dc5b14739857fe8fcbd0a93dbcc2c250066ea9206278bcd60e4e53a0694b4825  pmc_29495465.pdf

Title:          Post-Translational Modifications of H2A Histone Variants and Their Role in Cancer
Subject:        Histone variants are chromatin components that replace replication-coupled histones in a fraction of nucleosomes and confer particular characteristics to chromatin. H2A variants represent the most numerous and diverse group among histone protein families. In the nucleosomal structure, H2A-H2B dimers can be removed and exchanged more easily than the stable H3-H4 core. The unstructured N-terminal histone tails of all histones, but also the C-terminal tails of H2A histones protrude out of the compact structure of the nucleosome core. These accessible tails are the preferential target sites for a large number of post-translational modifications (PTMs). While some PTMs are shared between replication-coupled H2A and H2A variants, many modifications are limited to a specific histone variant. The present review focuses on the H2A variants H2A.Z, H2A.X, and macroH2A, and summarizes their functions in chromatin and how these are linked to cancer development and progression. H2A.Z primarily acts as an oncogene and macroH2A and H2A.X as tumour suppressors. We further focus on the regulation by PTMs, which helps to understand a degree of context dependency.
Keywords:       histone variants; post-translational modifications; cancer; epigenetics; H2A.Z; H2A.X; macroH2A
Author:         David Corujo and Marcus Buschbeck
Creator:        LaTeX with hyperref package
Producer:       pdfTeX-1.40.17
CreationDate:   Tue Feb 27 13:10:38 2018 CET
ModDate:        Tue Feb 27 13:10:38 2018 CET
Tagged:         no
UserProperties: no
Suspects:       no
Form:           none
JavaScript:     no
Pages:          25
Encrypted:      no
Page size:      595.276 x 841.89 pts (A4)
Page rot:       0
File size:      1113285 bytes
Optimized:      no
PDF version:    1.5

name                                 type              encoding         emb sub uni object ID
------------------------------------ ----------------- ---------------- --- --- --- ---------
LGLCUS+URWPalladioL-Ital             Type 1            Custom           yes yes no      74  0
NVFTWA+URWPalladioL-Bold             Type 1            Custom           yes yes no      75  0
OXBKYU+TeXGyreAdventor-Bold          Type 1            Custom           yes yes no      76  0
ZHWGVT+URWPalladioL-Roma             Type 1            Custom           yes yes no      77  0
RHMGQW+VnURWPalladioL                Type 1            Custom           yes yes no      78  0
LCJEVJ+TimesNewRomanPS-BoldItalicMT  Type 1C           WinAnsi          yes yes no      84  0
GOCQIR+EURM10                        Type 1            Builtin          yes yes no     184  0
IPKMDK+PalatinoLinotype,Italic       TrueType          WinAnsi          yes yes no     189  0
IPKMDM+PalatinoLinotype,Bold         TrueType          WinAnsi          yes yes no     190  0
IPKMDN+PalatinoLinotype              CID TrueType      Identity-H       yes yes yes    191  0
IPKMEO+PalatinoLinotype              TrueType          WinAnsi          yes yes no     192  0
FXXUVH+CMSY10                        Type 1            Builtin          yes yes no     482  0

java.lang.ClassCastException: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject cannot be cast to edu.harvard.hul.ois.jhove.module.pdf.PdfDictionary
	at edu.harvard.hul.ois.jhove.module.PdfModule.readDocCatalogDict(PdfModule.java:1284)
	at edu.harvard.hul.ois.jhove.module.PdfModule.parse(PdfModule.java:525)
	at edu.harvard.hul.ois.jhove.JhoveBase.processFile(JhoveBase.java:825)
	at edu.harvard.hul.ois.jhove.JhoveBase.process(JhoveBase.java:614)
	at edu.harvard.hul.ois.jhove.JhoveBase.dispatch(JhoveBase.java:465)
	at Jhove.main(Jhove.java:296)
Jhove (Rel. 1.6, 2011-01-04)
 Date: 2019-02-14 17:26:10 CET
 RepresentationInformation: pmc_29495465.pdf
  ReportingModule: BYTESTREAM, Rel. 1.3 (2007-04-10)
  LastModified: 2018-04-16 03:49:32 CEST
  Size: 1113285
  Format: bytestream
  Status: Well-Formed and valid
  SignatureMatches:
   PDF-hul
  MIMEtype: application/octet-stream
  Checksum: 571e6b90
   Type: CRC32
  Checksum: 874b6b80ca09e346e07c32a0cc516fa3
   Type: MD5
  Checksum: a1db26f25036b85b1e1e0cac02e7cae854d2cd12
   Type: SHA-1