Structural Insight into Recognition of Methylated Histone Tails by Retinoblastoma-binding Protein 1

Gong, Weibin; Zhou, Tao; Mo, Jinjin; Perrett, Sarah; Wang, Jinfeng; Feng, Yingang

doi:10.1074/jbc.m111.299149

Cited by 31 publications

(48 citation statements)

References 37 publications

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“…RBBP1 and RBBP1L1 regulate epigenetic marks, such as methylation of lysines in histones H3 and H4, which are observed in leukemia and Prader-Willi/Angelman syndromes (2,11). The epigenetic regulation function of RBBP1 was proposed to be mediated by its three Royal Family domains (2,11,12), including the chromobarrel domain, Tudor domain, and Pro-Trp-Trp-Pro (PWWP) domain, but our previous study indicated that of these three domains, only the chromobarrel domain can bind with histone tails and is responsible for the epigenetic regulation function (13). RBBP1 and RBBP1L1 are also known as ARID4A and ARID4B, respectively, because they each contain an ATrich interaction domain (ARID) and bind to DNA nonspecifically, presumably through this domain (14).…”

mentioning

confidence: 99%

“…Our previous studies indicated that the RBBP1 Tudor domain has low sequence homology to other known Tudor domains and cannot recognize epigenetic marks (13). In order to further understand the function of the RBBP1 Tudor domain, we have now determined its solution structure, which shows an interdigitated double Tudor fold similar to the epigenetic mark reader JMJD2A.…”

mentioning

confidence: 99%

“…RBBP1 and RBBP1L1 are also known as ARID4A and ARID4B, respectively, because they each contain an ATrich interaction domain (ARID) and bind to DNA nonspecifically, presumably through this domain (14). The RBBP1 chromobarrel domain can also bind to DNA weakly, and this binding can increase the affinity of the chromobarrel domain for methylated histone tails (13).…”

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confidence: 99%

“…Bioinformatic analysis indicates that RBBP1 contains a Tudor domain at its N terminus (13). The Tudor domain is a conserved protein structural motif, originally identified as a region of 60 amino acids in the Drosophila Tudor protein (15,16).…”

mentioning

confidence: 99%

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Retinoblastoma-binding Protein 1 Has an Interdigitated Double Tudor Domain with DNA Binding Activity

Gong

Wang

Perrett

et al. 2014

Journal of Biological Chemistry

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Background: Retinoblastoma-binding protein 1 (RBBP1), a tumor suppressor, has a Tudor domain with unknown function. Results: The Tudor domain adopts an interdigitated double Tudor structure with DNA binding activity. Conclusion:The Tudor domain of the RBBP1 family is a DNA binding module. Significance: Our research provides further structural insights into RBBP1 function and the diversity of Tudor domains.

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Retinoblastoma-binding Protein 1 Has an Interdigitated Double Tudor Domain with DNA Binding Activity

Gong

Wang

Perrett

et al. 2014

Journal of Biological Chemistry

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“…1). However, some PWWP domains contain a truncated version of the aromatic cage, lacking one of the three aromatic residues, and thus are unable to bind histone methyl-lysines (Gong et al 2012).…”

Section: Structural Features Of Pwwp Domainsmentioning

confidence: 99%

PWWP domains and their modes of sensing DNA and histone methylated lysines

2016

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Chromatin plays an important role in gene transcription control, cell cycle progression, recombination, DNA replication and repair. The fundamental unit of chromatin, the nucleosome, is formed by a DNA duplex wrapped around an octamer of histones. Histones are susceptible to various post-translational modifications, covalent alterations that change the chromatin status. Lysine methylation is one of the major post-translational modifications involved in the regulation of chromatin function. 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 domain three-dimensional structure is based on an N-terminal hydrophobic β-barrel responsible for histone methyl-lysine binding, and a C-terminal α-helical domain. In this review, we set out to discuss the most recent literature on PWWP domains, focusing on their structural features and the mechanisms by which they specifically recognize DNA and histone methylated lysines at the level of the nucleosome.

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Structural and histone binding studies of the chromo barrel domain of TIP60

et al. 2018

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Tat-interactive protein 60 consists of an N-terminal chromo barrel domain (TIP60-CB) and a C-terminal acetyltransferase domain and acetylates histone and nonhistone proteins in diverse cellular processes. While TIP60-CB is thought to recognize histone tails, molecular details of this interaction remain unclear. Here, we attempted a quantitative analysis of the interaction between the human TIP60-CB and histone peptides, but did not observe any detectable binding by either fluorescence polarization or isothermal titration calorimetry assays. We also determined the crystal structure of the TIP60-CB alone. Analysis of the apo-structure reveals a putative peptide-binding site that might be occluded by the basic side chain of a residue in a unique β hairpin between the two N-terminal strands of the β barrel, leading to the inability of TIP60-CB to bind histones.

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Structural Insight into Recognition of Methylated Histone Tails by Retinoblastoma-binding Protein 1

Cited by 31 publications

References 37 publications

Retinoblastoma-binding Protein 1 Has an Interdigitated Double Tudor Domain with DNA Binding Activity

Retinoblastoma-binding Protein 1 Has an Interdigitated Double Tudor Domain with DNA Binding Activity

PWWP domains and their modes of sensing DNA and histone methylated lysines

Structural and histone binding studies of the chromo barrel domain of TIP60

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