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Structure And Function Of The Nucleosome-Binding Pwwp Domain

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PWWP domain binds to both DNA and lysine methylated histone The PWWP domain has a unique feature known as an aromatic cage, which en-ables it to selectively identify and attach Recent years have witnessed remarkable strides in unraveling the structural and functional features of PWWP domain-containing proteins, propelling significant advances in The PWWP domain binds to both histone and DNA of a nucleosome in a bivalent way. PWWP domain-containing proteins are involved in different biological processes, and

Regulation of Chromatin Architecture by the PWWP Domain-Containing DNA ...

Here we show that its PWWP domain prefers binding to thymidine-rich DNA over GC-rich sequences. Crystal structures both in apo and ssDNA-bound states, reveal a domain

Nucleosome pulldown experiments show that DNA binding and H3K36me2/3 binding are important for the interaction of the DNMT3A PWWP domain with nucleosomes.

PWWP2A/B: Prominent players in the proteomic landscape

Qin, S., & Min, J. (2014). Structure and function of the nucleosome-binding PWWP domain. Trends in Biochemical Sciences, 39 (11), 536–547. doi:10.1016/j.tibs.2014. NSD3 is one of six H3K36-specific lysine methyltransferases in metazoans, and the methylation of H3K36 is associated with active transcription. NSD3 is a member of the nuclear receptor The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The

Based on this structure, we propose a model of the DNMT3A PWWP domain-H3K36me3 complex and build a model of DNMT3A (PWWP-ADD-CD) in a nucleosomal context. The trimethylated Concerted binding to the methylated histone tail and nucleosomal DNA underlies the high- affinity, specific recognition of H3K36me nucleosomes by the PSIP1-PWWP domain.

The PWWP domain is a conserved motif unique to eukaryotes, playing a critical role in various cellular processes. Proteins containing the PWWP domain are typically found in

  • PWWP domains and their modes of sensing DNA and histone
  • Structures of chromatin modulators in complex with nucleosome
  • CDD Conserved Protein Domain Family: PWWP

The PWWP domain of Dnmt3b, comprising a beta-barrel structure with 5 beta-sheets followed by a five-helix bundle, turned out to be a fold responsible for DNA binding (Qiu Dynamic changes of chromatin structure facilitate diverse biological events, including DNA replication, repair, recombination, and gene transcription. Recent evidence of 35/35 Match case Limit results 1 per page – 1 – Structure and function of the nucleosome-binding PWWP domain 1 2 Su Qin 1 and Jinrong Min 1, 2 3 1 Structural Genomics Consortium,

Structure and function of the nucleosome-binding PWWP domain

Structural studies reveal that PWWP domains possess a conserved aromatic cage for histone methyl-lysine recognition, and Structure of BS69 Bromo-ZnF-PWWP and its binding properties to H3K36me3 nucleosomes. (A) Schematic diagram showing the domain To better understand the functions of these proteins’ PWWP domains, we cloned, expressed and purified all the PWWP domains of these NSD proteins to characterize their

CPC–nucleosome binding is mediated by multivalent interactions ...

Positively charged Lys and Arg residues on the surface of the domain are expected to be the sites for DNA binding (Fig. 2a). The beta-barrel part of the PWWP domain is homologous to that of

The PWWP domain is a member of the Royal superfamily that functions as a chromatin methylation reader by recognizing both DNA and histone methylated lysines. The PWWP Structural studies reveal that PWWP domains possess a conserved aromatic cage for histone methyl-lysine recognition, and synergistically bind both histone and DNA, which contributes to

Furthermore, the PWWP domain often cooperates with other histone and DNA ‘reader’ or ‘modifier’ domains to evoke crosstalk between various epigenetic marks. Here, we discuss Download scientific diagram | Comparison of the location of the PWWP domain in our nucleosome-PWWP complex structure with previously proposed models a, Front view of the Structural studies reveal that PWWP domains possess a conserved aromatic cage for histone methyl-lysine recognition, and synergistically bind both histone and DNA, which contributes to

Recent years have witnessed remarkable strides in unraveling the structural and functional features of PWWP domain-containing proteins, propelling significant advances in Structural studies reveal that PWWP domains possess a conserved aro-matic cage for histone methyl-lysine recognition, and synergistically bind both histone and DNA, which con-tributes to scientific article published on 29 September 2014Structure and function of the nucleosome-binding PWWP domain(Q38256189)

A scientific resource for the PWWP protein domain containing information on structure, function, and domain binding.

Our crystal structure of the BRPF2 PWWP domain in complex with a 12-mer dsDNA reveals that the PWWP domain interacts with dsDNA by binding to its major groove, instead of the minor The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The PWWP2A is a chromatin-binding transcriptional regulator that mediates mitosis-progression. Here, the authors provide evidence that PWWP2A directly interacts with H2A.Z

Here, we review the very recent progress in structural studies of some selected chromatin modulators in complex with nucleosome, including those of histone demethylases Structure and function of the nucleosome-binding PWWP domain PWWP domain-containing proteins are often involved in chromatin-associated biological processes, such as All Dnmts possess multiple domains. For instance, Dnmt3a and Dnmt3b each contain a Pro-Trp-Trp-Pro (PWWP) domain that recognizes the histone H3K36me2/3 mark, an Atrx-Dnmt3