A Novel Histone H4 Arginine 3 Methylation-sensitive Histone H4 Binding Activity and Transcriptional Regulatory Function for Signal Recognition Particle Subunits SRP68 and SRP72
Published 2012 View Full Article
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Title
A Novel Histone H4 Arginine 3 Methylation-sensitive Histone H4 Binding Activity and Transcriptional Regulatory Function for Signal Recognition Particle Subunits SRP68 and SRP72
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 48, Pages 40641-40651
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2012-10-10
DOI
10.1074/jbc.m112.414284
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- Histone H3R17me2a mark recruits human RNA Polymerase-Associated Factor 1 Complex to activate transcription
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- (2010) Kyoko L. Yap et al. CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY
- TDRD3 Is an Effector Molecule for Arginine-Methylated Histone Marks
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- Eset partners with Oct4 to restrict extraembryonic trophoblast lineage potential in embryonic stem cells
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- Minireview: Protein Arginine Methylation of Nonhistone Proteins in Transcriptional Regulation
- (2009) Young-Ho Lee et al. MOLECULAR ENDOCRINOLOGY
- PRMT5-mediated methylation of histone H4R3 recruits DNMT3A, coupling histone and DNA methylation in gene silencing
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- Characterization of the SRP68/72 interface of human signal recognition particle by systematic site-directed mutagenesis
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- Unbiased proteomic screen for binding proteins to modified lysines on histone H3
- (2009) Doug W. Chan et al. PROTEOMICS
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