A Novel Histone H4 Arginine 3 Methylation-sensitive Histone H4 Binding Activity and Transcriptional Regulatory Function for Signal Recognition Particle Subunits SRP68 and SRP72

Li, Jingjing; Zhou, Fan; Zhan, Deguo; Gao, Qinqin; Cui, Nan; Li, Jiwen; Iakhiaeva, Elena; Zwieb, Christian W; Lin, Biaoyang; Wong, Jiemin

doi:10.1074/jbc.m112.414284

Cited by 16 publications

(13 citation statements)

References 47 publications

(51 reference statements)

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“…Interestingly, methylation of histone H4 at the third arginine in the histone tail (H4R3me) blocks binding of SRP68/72 to chromatin. 106 Currently, it is unclear how germline mutations in SRP72 alter protein function.…”

Section: Molecular Pathogenesismentioning

confidence: 99%

Inherited Predisposition to Acute Myeloid Leukemia

Godley

2014

Seminars in Hematology

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Section: Molecular Pathogenesismentioning

confidence: 99%

Inherited Predisposition to Acute Myeloid Leukemia

Godley

2014

Seminars in Hematology

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“…However, another report was unable to reproduce this interaction [78], so further study is necessary. In contrast, H4R3me2s or H4R3me2a can interfere with the ability of the Signal Recognition Particle (SRP) proteins SRP68 and SRP72 to bind the H4 tail [79]. …”

Section: Introductionmentioning

confidence: 99%

The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond

Stopa

Krebs

Shechter

2015

Cell. Mol. Life Sci.

386

399

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Post-translational arginine methylation is responsible for regulation of many biological processes. The protein arginine methyltransferase 5 (PRMT5, also known as Hsl7, Jbp1, Skb1, Capsuleen, or Dart5) is the major enzyme responsible for mono- and symmetric dimethylation of arginine. An expanding literature demonstrates its critical biological function in a wide range of cellular processes. Histone and other protein methylation by PRMT5 regulate genome organization, transcription, stem cells, primordial germ cells, differentiation, the cell cycle, and spliceosome assembly. Metazoan PRMT5 is found in complex with the WD-repeat protein MEP50 (also known as Wdr77, androgen receptor coactivator p44, or Valois). PRMT5 also directly associates with a range of other protein factors, including pICln, Menin, CoPR5 and RioK1 that may alter its subcellular localization and protein substrate selection. Protein substrate and PRMT5–MEP50 post-translation modifications induce crosstalk to regulate PRMT5 activity. Crystal structures of C. elegans PRMT5 and human and frog PRMT5–MEP50 complexes provide substantial insight into the mechanisms of substrate recognition and procession to dimethylation. Enzymo-logical studies of PRMT5 have uncovered compelling insights essential for future development of specific PRMT5 inhibitors. In addition, newly accumulating evidence implicates PRMT5 and MEP50 expression levels and their methyltransferase activity in cancer tumorigenesis, and, significantly, as markers of poor clinical outcome, marking them as potential oncogenes. Here, we review the substantial new literature on PRMT5 and its partners to highlight the significance of understanding this essential enzyme in health and disease.

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“…Components of the signal recognition particle, SRP68 and SRP72 have also been shown to form a heterodimeric complex distinct from the signal recognition particle. In addition to its role in translation, the SRP68/72 complex was also found to bind histone H4 molecules that contain arginine 3 methylation [ 24 ].…”

Section: Resultsmentioning

confidence: 99%

Identification of replication-dependent and replication-independent linker histone complexes: Tpr specifically promotes replication-dependent linker histone stability

et al. 2016

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BackgroundThere are 11 variants of linker histone H1 in mammalian cells. Beyond their shared abilities to stabilize and condense chromatin, the H1 variants have been found to have non-redundant functions, the mechanisms of which are not fully understood. Like core histones, there are both replication-dependent and replication-independent linker histone variants. The histone chaperones and other factors that regulate linker histone dynamics in the cell are largely unknown. In particular, it is not known whether replication-dependent and replication-independent linker histones interact with distinct or common sets of proteins. To better understand linker histone dynamics and assembly, we used chromatography and mass spectrometry approaches to identify proteins that are associated with replication-dependent and replication-independent H1 variants. We then used a variety of in vivo analyses to validate the functional relevance of identified interactions.ResultsWe identified proteins that bind to all linker histone variants and proteins that are specific for only one class of variant. The factors identified include histone chaperones, transcriptional regulators, RNA binding proteins and ribosomal proteins. The nuclear pore complex protein Tpr, which was found to associate with only replication-dependent linker histones, specifically promoted their stability.ConclusionReplication-dependent and replication-independent linker histone variants can interact with both common and distinct sets of proteins. Some of these factors are likely to function as histone chaperones while others may suggest novel links between linker histones and RNA metabolism. The nuclear pore complex protein Tpr specifically interacts with histone H1.1 and H1.2 but not H1x and can regulate the stability of these replication-dependent linker histones.Electronic supplementary materialThe online version of this article (doi:10.1186/s12858-016-0074-9) contains supplementary material, which is available to authorized users.

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A Novel Histone H4 Arginine 3 Methylation-sensitive Histone H4 Binding Activity and Transcriptional Regulatory Function for Signal Recognition Particle Subunits SRP68 and SRP72

Cited by 16 publications

References 47 publications

Inherited Predisposition to Acute Myeloid Leukemia

Inherited Predisposition to Acute Myeloid Leukemia

The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond

Identification of replication-dependent and replication-independent linker histone complexes: Tpr specifically promotes replication-dependent linker histone stability

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