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Journal articles on the topic 'Pwwp'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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1

Wang, Rui, Jie Gao, Jiahai Zhang, Xuecheng Zhang, Chao Xu, Shanhui Liao, and Xiaoming Tu. "Solution structure of TbTFIIS2-2 PWWP domain from Trypanosoma brucei and its binding to H4K17me3 and H3K32me3." Biochemical Journal 476, no. 2 (January 31, 2019): 421–31. http://dx.doi.org/10.1042/bcj20180870.

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Abstract Posttranslational modiﬁcations (PTMs) of core histones, such as histone methylation, play critical roles in a variety of biological processes including transcription regulation, chromatin condensation and DNA repair. In T. brucei, no domain recognizing methylated histone has been identified so far. TbTFIIS2-2, as a potential transcription elongation factors in T. brucei, contains a PWWP domain in the N-terminus which shares low sequence similarity compared with other PWWP domains and is absent from other TFIIS factors. In the present study, the solution structure of TbTFIIS2-2 PWWP domain was determined by NMR spectroscopy. TbTFIIS2-2 PWWP domain adopts a global fold containing a ﬁve-strand β-barrel and two C-terminal α-helices similar to other PWWP domains. Moreover, through systematic screening, we revealed that TbTFIIS2-2 PWWP domain is able to bind H4K17me3 and H3K32me3. Meanwhile, we identified the critical residues responsible for the binding ability of TbTFIIS2-2 PWWP domain. The conserved cage formed by the aromatic amino acids in TbTFIIS2-2 PWWP domain is essential for its binding to methylated histones.

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2

Chen, Taiping, Naomi Tsujimoto, and En Li. "The PWWP Domain of Dnmt3a and Dnmt3b Is Required for Directing DNA Methylation to the Major Satellite Repeats at Pericentric Heterochromatin." Molecular and Cellular Biology 24, no. 20 (October 15, 2004): 9048–58. http://dx.doi.org/10.1128/mcb.24.20.9048-9058.2004.

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ABSTRACT Dnmt3a and Dnmt3b are responsible for the establishment of DNA methylation patterns during development. These proteins contain, in addition to a C-terminal catalytic domain, a unique N-terminal regulatory region that harbors conserved domains, including a PWWP domain. The PWWP domain, characterized by the presence of a highly conserved proline-tryptophan-tryptophan-proline motif, is a module of 100 to 150 amino acids found in many chromatin-associated proteins. However, the function of the PWWP domain remains largely unknown. In this study, we provide evidence that the PWWP domains of Dnmt3a and Dnmt3b are involved in functional specialization of these enzymes. We show that both endogenous and green fluorescent protein-tagged Dnmt3a and Dnmt3b are particularly concentrated in pericentric heterochromatin. Mutagenesis analysis indicates that their PWWP domains are required for their association with pericentric heterochromatin. Disruption of the PWWP domain abolishes the ability of Dnmt3a and Dnmt3b to methylate the major satellite repeats at pericentric heterochromatin. Furthermore, we demonstrate that the Dnmt3a PWWP domain has little DNA-binding ability, in contrast to the Dnmt3b PWWP domain, which binds DNA nonspecifically. Collectively, our results suggest that the PWWP domains of Dnmt3a and Dnmt3b are essential for targeting these enzymes to pericentric heterochromatin, probably via a mechanism other than protein-DNA interactions.

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3

Qiu, Yu, Wen Zhang, Chen Zhao, Yan Wang, Weiwei Wang, Jiahai Zhang, Zhiyong Zhang, et al. "Solution structure of the Pdp1 PWWP domain reveals its unique binding sites for methylated H4K20 and DNA." Biochemical Journal 442, no. 3 (February 24, 2012): 527–38. http://dx.doi.org/10.1042/bj20111885.

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Methylation of H4K20 (Lys20 of histone H4) plays an important role in the regulation of diverse cellular processes. In fission yeast, all three states of H4K20 methylation are catalysed by Set9. Pdp1 is a PWWP (proline-tryptophan-tryptophan-proline) domain-containing protein, which associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. The structure of the Pdp1 PWWP domain, which is the first PWWP domain identified which binds to methyl-lysine at the H4K20 site, was determined in the present study by solution NMR. The Pdp1 PWWP domain adopts a classical PWWP fold, with a five-strand antiparallel β-barrel followed by three α-helices. However, it differs significantly from other PWWP domains in some structural aspects that account, in part, for its molecular recognition. Moreover, we revealed a unique binding pattern of the PWWP domain, in that the PWWP domain of Pdp1 bound not only to H4K20me3 (trimethylated Lys20 of histone H4), but also to dsDNA (double-stranded DNA) via an aromatic cage and a positively charged area respectively. EMSAs (electrophoretic mobility-shift assays) illustrated the ability of the Pdp1 PWWP domain to bind to the nucleosome core particle, and further mutagenesis experiments indicated the crucial role of this binding activity in histone H4K20 di- and tri-methylation in yeast cells. The present study may shed light on a novel mechanism of histone methylation regulation by the PWWP domain.

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4

Slater, Leanne M., Mark D. Allen, and Mark Bycroft. "Structural Variation in PWWP Domains." Journal of Molecular Biology 330, no. 3 (July 2003): 571–76. http://dx.doi.org/10.1016/s0022-2836(03)00470-4.

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5

Tan, Hong Kee, Chan-Shuo Wu, Jia Li, Zi Hui Tan, Jordan R. Hoffman, Christopher J. Fry, Henry Yang, Annalisa Di Ruscio, and Daniel G. Tenen. "DNMT3B shapes the mCA landscape and regulates mCG for promoter bivalency in human embryonic stem cells." Nucleic Acids Research 47, no. 14 (June 20, 2019): 7460–75. http://dx.doi.org/10.1093/nar/gkz520.

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Abstract DNMT3B is known as a de novo DNA methyltransferase. However, its preferential target sites for DNA methylation are largely unknown. Our analysis on ChIP-seq experiment in human embryonic stem cells (hESC) revealed that DNMT3B, mCA and H3K36me3 share the same genomic distribution profile. Deletion of DNMT3B or its histone-interacting domain (PWWP) demolished mCA in hESCs, suggesting that PWWP domain of DNMT3B directs the formation of mCA landscape. In contrast to the common presumption that PWWP guides DNMT3B-mediated mCG deposition, we found that deleting PWWP does not affect the mCG landscape. Nonetheless, DNMT3B knockout led to the formation of 2985 de novo hypomethylated regions at annotated promoter sites. Upon knockout, most of these promoters gain the bivalent marks, H3K4me3 and H3K27me3. We call them spurious bivalent promoters. Gene ontology analysis associated spurious bivalent promoters with development and cell differentiation. Overall, we found the importance of DNMT3B for shaping the mCA landscape and for maintaining the fidelity of the bivalent promoters in hESCs.

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6

Shun, Ming-Chieh, Yaïr Botbol, Xiang Li, Francesca Di Nunzio, Janet E. Daigle, Nan Yan, Judy Lieberman, Marc Lavigne, and Alan Engelman. "Identification and Characterization of PWWP Domain Residues Critical for LEDGF/p75 Chromatin Binding and Human Immunodeficiency Virus Type 1 Infectivity." Journal of Virology 82, no. 23 (September 17, 2008): 11555–67. http://dx.doi.org/10.1128/jvi.01561-08.

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ABSTRACT Lens epithelium-derived growth factor (LEDGF)/p75 functions as a bimodal tether during lentiviral DNA integration: its C-terminal integrase-binding domain interacts with the viral preintegration complex, whereas the N-terminal PWWP domain can bind to cellular chromatin. The molecular basis for the integrase-LEDGF/p75 interaction is understood, while the mechanism of chromatin binding is unknown. The PWWP domain is homologous to other protein interaction modules that together comprise the Tudor clan. Based on primary amino acid sequence and three-dimensional structural similarities, 24 residues of the LEDGF/p75 PWWP domain were mutagenized to garner essential details of its function during human immunodeficiency virus type 1 (HIV-1) infection. Mutating either Trp-21 or Ala-51, which line the inner wall of a hydrophobic cavity that is common to Tudor clan members, disrupts chromatin binding and virus infectivity. Consistent with a role for chromatin-associated LEDGF/p75 in stimulating integrase activity during infection, recombinant W21A protein is preferentially defective for enhancing integration into chromatinized target DNA in vitro. The A51P mutation corresponds to the S270P change in DNA methyltransferase 3B that causes human immunodeficiency, centromeric instability, and facial anomaly syndrome, revealing a critical role for this amino acid position in the chromatin binding functions of varied PWWP domains. Our results furthermore highlight the requirement for a conserved Glu in the hydrophobic core that mediates interactions between other Tudor clan members and their substrates. This initial systematic mutagenesis of a PWWP domain identifies amino acid residues critical for chromatin binding function and the consequences of their changes on HIV-1 integration and infection.

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7

Qin, Su, and Jinrong Min. "Structure and function of the nucleosome-binding PWWP domain." Trends in Biochemical Sciences 39, no. 11 (November 2014): 536–47. http://dx.doi.org/10.1016/j.tibs.2014.09.001.

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8

Ge, Ying-Zi, Min-Tie Pu, Humaira Gowher, Hai-Ping Wu, Jian-Ping Ding, Albert Jeltsch, and Guo-Liang Xu. "Chromatin Targeting ofde NovoDNA Methyltransferases by the PWWP Domain." Journal of Biological Chemistry 279, no. 24 (March 3, 2004): 25447–54. http://dx.doi.org/10.1074/jbc.m312296200.

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9

Kibe, Kanako, Kenjiro Shirane, Hiroaki Ohishi, Shuhei Uemura, Hidehiro Toh, and Hiroyuki Sasaki. "The DNMT3A PWWP domain is essential for the normal DNA methylation landscape in mouse somatic cells and oocytes." PLOS Genetics 17, no. 5 (May 28, 2021): e1009570. http://dx.doi.org/10.1371/journal.pgen.1009570.

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DNA methylation at CG sites is important for gene regulation and embryonic development. In mouse oocytes, de novo CG methylation requires preceding transcription-coupled histone mark H3K36me3 and is mediated by a DNA methyltransferase DNMT3A. DNMT3A has a PWWP domain, which recognizes H3K36me2/3, and heterozygous mutations in this domain, including D329A substitution, cause aberrant CG hypermethylation of regions marked by H3K27me3 in somatic cells, leading to a dwarfism phenotype. We herein demonstrate that D329A homozygous mice show greater CG hypermethylation and severer dwarfism. In oocytes, D329A substitution did not affect CG methylation of H3K36me2/3-marked regions, including maternally methylated imprinting control regions; rather, it caused aberrant hypermethylation in regions lacking H3K36me2/3, including H3K27me3-marked regions. Thus, the role of the PWWP domain in CG methylation seems similar in somatic cells and oocytes; however, there were cell-type-specific differences in affected regions. The major satellite repeat was also hypermethylated in mutant oocytes. Contrary to the CA hypomethylation in somatic cells, the mutation caused hypermethylation at CH sites, including CA sites. Surprisingly, oocytes expressing only the mutated protein could support embryonic and postnatal development. Our study reveals that the DNMT3A PWWP domain is important for suppressing aberrant CG hypermethylation in both somatic cells and oocytes but that D329A mutation has little impact on the developmental potential of oocytes.

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10

Zhang, Mengmeng, Ming Lei, Su Qin, Aiping Dong, Ally Yang, Yanjun Li, Peter Loppnau, Timothy R. Hughes, Jinrong Min, and Yanli Liu. "Crystal structure of the BRPF2 PWWP domain in complex with DNA reveals a different binding mode than the HDGF family of PWWP domains." Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms 1864, no. 3 (March 2021): 194688. http://dx.doi.org/10.1016/j.bbagrm.2021.194688.

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11

Wu, Hong, Hong Zeng, Robert Lam, Wolfram Tempel, Maria F. Amaya, Chao Xu, Ludmila Dombrovski, Wei Qiu, Yanming Wang, and Jinrong Min. "Structural and Histone Binding Ability Characterizations of Human PWWP Domains." PLoS ONE 6, no. 6 (June 20, 2011): e18919. http://dx.doi.org/10.1371/journal.pone.0018919.

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12

Wang, Rui, Jiahai Zhang, Shanhui Liao, and Xiaoming Tu. "Solution structure of TbTFIIS2-1 PWWP domain from Trypanosoma brucei." Proteins: Structure, Function, and Bioinformatics 84, no. 7 (April 7, 2016): 912–19. http://dx.doi.org/10.1002/prot.25035.

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13

Yokoyama, Akihiko, and Michael Cleary. "The Menin Tumor Suppressor Functions as a Molecular Adapter That Tethers LEDGF to MLL Proteins in Leukemogenesis." Blood 112, no. 11 (November 16, 2008): 1795. http://dx.doi.org/10.1182/blood.v112.11.1795.1795.

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Abstract MLL gene rearrangements are present in 5 to 10% of acute leukemias, which are generally associated with a poor prognosis. Chromosomal translocations at the MLL locus create MLL fusion genes that constitute 5’ portions of MLL and 3’ portions of partner genes. The resultant MLL fusion proteins transform myeloid progenitors by inappropriately activating a HOX-associated self renewal program. However, the molecular mechanisms underlying MLL oncoprotein function are not fully understood. Previously we identified menin as a component of the MLL macromolecular complex. Menin is a product of the MEN1 tumor suppressor gene, whose loss of function causes multiple endocrine neoplasia type 1 (MEN1). Despite its tumor suppressor role in endocrine tissues, menin functions as an essential oncogenic cofactor for MLL fusion protein-dependent leukemogenesis. This notion was supported by three lines of evidence: MLL fusion proteins lacking the menin binding motif do not transform myeloid progenitors; inactivation of menin causes growth arrest and subsequent differentiation of MLL oncogene transformed cells; and menin is required for MLL oncogene dependent transcriptional activation of HOX genes. These findings raised a fundamental question: how does menin contribute to MLL-dependent transcription? Because menin lacks known functional motifs, its molecular functions could not be deduced from its structure. We hypothesized that menin may function as an adapter that tethers MLL to unknown associated factors. To identify such associated factors, we performed affinity purification of the MLL-ENL/menin complex from nuclear extracts of cells that transiently over-expressed both MLL-ENL and menin. Mass spectrometry identified LEDGF, originally identified as a transcriptional co-activator, in the purified material as a novel associated factor. LEDGF associates conjointly with the MLL/menin complex but not with MLL or menin alone, supporting the hypothesis that menin plays an adapter role to bridge MLL and LEDGF. Further analysis revealed that LEDGF is critical for MLL fusion protein-dependent leukemogenesis. Fine mapping of the domain responsible for LEDGF binding determined MLL residues 109–153 as the LEDGF binding domain (LBD). Mutations in LBD resulted in loss of oncogenic activity of MLL fusion proteins. Moreover, knock down of LEDGF in MLL-transformed cells caused growth arrest and differentiation in the same manner as menin knock down. These results demonstrate that LEDGF is also required for the initiation and maintenance of MLL fusion protein-dependent transformation. In contrast to menin, LEDGF has a distinctive functional motif (the PWWP domain), which reportedly has chromatin binding activity. To further confirm that menin is an adapter that links MLL and LEDGF, we examined the oncogenic functions of an artificial MLL fusion protein whose menin binding motif is replaced by the PWWP domain of LEDGF. This PWWP-MLL-ENL fusion protein does not associate with menin because it lacks the menin binding motif, nevertheless transforms myeloid progenitors. Chromatin immunoprecipitation experiments show that the PWWP-MLL- ENL fusion protein localizes at the HOXA9 locus while menin is absent. Moreover, myeloid progenitors transformed by the PWWP-MLL-ENL fusion protein continue to proliferate after menin is genetically inactivated. Thus covalent tethering of the PWWP domain fully compensates for loss of menin’s cofactor function. Therefore, menin’s only role in MLL-associated leukemogenesis is to tether LEDGF to MLL fusion proteins. In summary, this study identifies a previously unknown essential oncogenic cofactor of MLL fusion proteins and proposes a stepwise association model in which the MLL fusion protein first associates with menin, then recruits LEDGF to its complex to become functionally active.

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14

Wang, Yu, Bharat Reddy, James Thompson, Hengbin Wang, Ken-ichi Noma, John R. Yates, and Songtao Jia. "Regulation of Set9-Mediated H4K20 Methylation by a PWWP Domain Protein." Molecular Cell 33, no. 4 (February 2009): 428–37. http://dx.doi.org/10.1016/j.molcel.2009.02.002.

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15

Eidahl, Jocelyn O., Brandon L. Crowe, Justin A. North, Christopher J. McKee, Nikoloz Shkriabai, Lei Feng, Matthew Plumb, et al. "Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes." Nucleic Acids Research 41, no. 6 (February 8, 2013): 3924–36. http://dx.doi.org/10.1093/nar/gkt074.

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16

Gong, Weibin, Xingzhe Yao, Qihui Liang, Yufeng Tong, Sarah Perrett, and Yingang Feng. "Resonance assignments for the tandem PWWP-ARID domains of human RBBP1." Biomolecular NMR Assignments 13, no. 1 (January 21, 2019): 177–81. http://dx.doi.org/10.1007/s12104-019-09873-2.

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17

Ferreira de Freitas, Renato, Yanli Liu, Magdalena M. Szewczyk, Naimee Mehta, Fengling Li, David McLeod, Carlos Zepeda-Velázquez, et al. "Discovery of Small-Molecule Antagonists of the PWWP Domain of NSD2." Journal of Medicinal Chemistry 64, no. 3 (February 1, 2021): 1584–92. http://dx.doi.org/10.1021/acs.jmedchem.0c01768.

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18

Wang, Haibo, Lucas Farnung, Christian Dienemann, and Patrick Cramer. "Structure of H3K36-methylated nucleosome–PWWP complex reveals multivalent cross-gyre binding." Nature Structural & Molecular Biology 27, no. 1 (December 9, 2019): 8–13. http://dx.doi.org/10.1038/s41594-019-0345-4.

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19

Vezzoli, Alessandro, Nicolas Bonadies, Mark D. Allen, Stefan M. V. Freund, Clara M. Santiveri, Brynn T. Kvinlaug, Brian J. P. Huntly, Berthold Göttgens, and Mark Bycroft. "Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1." Nature Structural & Molecular Biology 17, no. 5 (April 18, 2010): 617–19. http://dx.doi.org/10.1038/nsmb.1797.

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20

Yang, Jun, and Allen D. Everett. "Hepatoma derived growth factor binds DNA through the N-terminal PWWP domain." BMC Molecular Biology 8, no. 1 (2007): 101. http://dx.doi.org/10.1186/1471-2199-8-101.

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21

Rona, Germana B., Elis C. A. Eleutherio, and Anderson S. Pinheiro. "PWWP domains and their modes of sensing DNA and histone methylated lysines." Biophysical Reviews 8, no. 1 (January 14, 2016): 63–74. http://dx.doi.org/10.1007/s12551-015-0190-6.

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22

Mellid, Sara, Javier Coloma, Bruna Calsina, María Monteagudo, Juan M. Roldán-Romero, María Santos, Luis J. Leandro-García, et al. "Novel DNMT3A Germline Variant in a Patient with Multiple Paragangliomas and Papillary Thyroid Carcinoma." Cancers 12, no. 11 (November 9, 2020): 3304. http://dx.doi.org/10.3390/cancers12113304.

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Over the past few years, next generation technologies have been applied to unravel the genetics of rare inherited diseases, facilitating the discovery of new susceptibility genes. We recently found germline DNMT3A gain-of-function variants in two patients with head and neck paragangliomas causing a characteristic hypermethylated DNA profile. Here, whole-exome sequencing identifies a novel germline DNMT3A variant (p.Gly332Arg) in a patient with bilateral carotid paragangliomas, papillary thyroid carcinoma and idiopathic intellectual disability. The variant, located in the Pro-Trp-Trp-Pro (PWWP) domain of the protein involved in chromatin targeting, affects a residue mutated in papillary thyroid tumors and located between the two residues found mutated in microcephalic dwarfism patients. Structural modelling of the variant in the DNMT3A PWWP domain predicts that the interaction with H3K36me3 will be altered. An increased methylation of DNMT3A target genes, compatible with a gain-of-function effect of the alteration, was observed in saliva DNA from the proband and in one independent acute myeloid leukemia sample carrying the same p.Gly332Arg variant. Although further studies are needed to support a causal role of DNMT3A variants in paraganglioma, the description of a new DNMT3A alteration in a patient with multiple clinical features suggests a heterogeneous phenotypic spectrum related to DNMT3A germline variants.

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23

Maurer-Stroh, Sebastian, Nicholas J. Dickens, Luke Hughes-Davies, Tony Kouzarides, Frank Eisenhaber, and Chris P. Ponting. "The Tudor domain ‘Royal Family’: Tudor, plant Agenet, Chromo, PWWP and MBT domains." Trends in Biochemical Sciences 28, no. 2 (February 2003): 69–74. http://dx.doi.org/10.1016/s0968-0004(03)00004-5.

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24

Nameki, N. "Solution structure of the PWWP domain of the hepatoma-derived growth factor family." Protein Science 14, no. 3 (March 1, 2005): 756–64. http://dx.doi.org/10.1110/ps.04975305.

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25

Lukasik, S. M. "High resolution structure of the HDGF PWWP domain: A potential DNA binding domain." Protein Science 15, no. 2 (February 1, 2006): 314–23. http://dx.doi.org/10.1110/ps.051751706.

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26

Zhou, Jin-Xing, Zhang-Wei Liu, Yong-Qiang Li, Lin Li, Bangjun Wang, She Chen, and Xin-Jian He. "Arabidopsis PWWP domain proteins mediate H3K27 trimethylation on FLC and regulate flowering time." Journal of Integrative Plant Biology 60, no. 5 (February 24, 2018): 362–68. http://dx.doi.org/10.1111/jipb.12630.

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27

Alvarez-Venegas, Raúl, and Zoya Avramova. "Evolution of the PWWP-domain encoding genes in the plant and animal lineages." BMC Evolutionary Biology 12, no. 1 (2012): 101. http://dx.doi.org/10.1186/1471-2148-12-101.

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28

Zhang, Mengmeng, Yinxue Yang, Mengqi Zhou, Aiping Dong, Xuemei Yan, Peter Loppnau, Jinrong Min, and Yanli Liu. "Histone and DNA binding ability studies of the NSD subfamily of PWWP domains." Biochemical and Biophysical Research Communications 569 (September 2021): 199–206. http://dx.doi.org/10.1016/j.bbrc.2021.07.017.

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29

Stec, Ingrid, Sylvia B. Nagl, Gert-Jan B. van Ommen, and Johan T. den Dunnen. "The PWWP domain: a potential protein-protein interaction domain in nuclear proteins influencing differentiation?" FEBS Letters 473, no. 1 (May 1, 2000): 1–5. http://dx.doi.org/10.1016/s0014-5793(00)01449-6.

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30

Laguri, Cédric, Isabelle Duband-Goulet, Nikolas Friedrich, Marianne Axt, Pascal Belin, Isabelle Callebaut, Bernard Gilquin, Sophie Zinn-Justin, and Joël Couprie. "Human Mismatch Repair Protein MSH6 Contains a PWWP Domain That Targets Double Stranded DNA†." Biochemistry 47, no. 23 (June 2008): 6199–207. http://dx.doi.org/10.1021/bi7024639.

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31

Dhayalan, Arunkumar, Arumugam Rajavelu, Philipp Rathert, Raluca Tamas, Renata Z. Jurkowska, Sergey Ragozin, and Albert Jeltsch. "The Dnmt3a PWWP Domain Reads Histone 3 Lysine 36 Trimethylation and Guides DNA Methylation." Journal of Biological Chemistry 285, no. 34 (June 11, 2010): 26114–20. http://dx.doi.org/10.1074/jbc.m109.089433.

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32

Zhang, Jiahai, Kun Dai, Shanhui Liao, and Xiaoming Tu. "1H, 13C and 15N resonance assignments of TbTFIIS2-2 PWWP domain from Trypanosoma brucei." Biomolecular NMR Assignments 7, no. 2 (July 27, 2012): 207–9. http://dx.doi.org/10.1007/s12104-012-9411-0.

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33

Wang, Rui, Shanhui Liao, Kai Fan, Jiahai Zhang, and Xiaoming Tu. "1H, 13C and 15N resonance assignments of TFIIS2-1 PWWP domain from Trypanosoma brucei." Biomolecular NMR Assignments 7, no. 2 (September 18, 2012): 275–77. http://dx.doi.org/10.1007/s12104-012-9426-6.

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34

Rona, Germana B., Diego S. G. Almeida, Anderson S. Pinheiro, and Elis C. A. Eleutherio. "The PWWP domain of the human oncogene WHSC1L1/NSD3 induces a metabolic shift toward fermentation." Oncotarget 8, no. 33 (August 12, 2016): 54068–81. http://dx.doi.org/10.18632/oncotarget.11253.

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35

Huen, Michael S. Y., Jun Huang, Justin W. C. Leung, Shirley M. H. Sy, Ka Man Leung, Yick-Pang Ching, Sai Wah Tsao, and Junjie Chen. "Regulation of Chromatin Architecture by the PWWP Domain-Containing DNA Damage-Responsive Factor EXPAND1/MUM1." Molecular Cell 37, no. 6 (March 2010): 854–64. http://dx.doi.org/10.1016/j.molcel.2009.12.040.

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36

van Nuland, Rick, Frederik MA van Schaik, Marieke Simonis, Sebastiaan van Heesch, Edwin Cuppen, Rolf Boelens, HT Timmers, and Hugo van Ingen. "Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain." Epigenetics & Chromatin 6, no. 1 (2013): 12. http://dx.doi.org/10.1186/1756-8935-6-12.

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37

Wang, Juncheng, Su Qin, Fudong Li, Sai Li, Wei Zhang, Junhui Peng, Zhiyong Zhang, Qingguo Gong, Jihui Wu, and Yunyu Shi. "Crystal structure of human BS69 Bromo-ZnF-PWWP reveals its role in H3K36me3 nucleosome binding." Cell Research 24, no. 7 (March 28, 2014): 890–93. http://dx.doi.org/10.1038/cr.2014.38.

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38

HERNÁNDEZ-ROMANO, J., M. H. RODRÍGUEZ, V. PANDO, J. A. TORRES-MONZÓN, A. ALVARADO-DELGADO, A. N. LECONA VALERA, R. ARGOTTE RAMOS, J. MARTÍNEZ-BARNETCHE, and M. C. RODRÍGUEZ. "Conserved peptide sequences bind to actin and enolase on the surface of Plasmodium berghei ookinetes." Parasitology 138, no. 11 (August 5, 2011): 1341–53. http://dx.doi.org/10.1017/s0031182011001296.

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SUMMARYThe description of Plasmodium ookinete surface proteins and their participation in the complex process of mosquito midgut invasion is still incomplete. In this study, using phage display, a consensus peptide sequence (PWWP) was identified in phages that bound to the Plasmodium berghei ookinete surface and, in selected phages, bound to actin and enolase in overlay assays with ookinete protein extracts. Actin was localized on the surface of fresh live ookinetes by immunofluorescence and electron microscopy using specific antibodies. The overall results indicated that enolase and actin can be located on the surface of ookinetes, and suggest that they could participate in Plasmodium invasion of the mosquito midgut.

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39

Morchikh, Mehdi, Monica Naughtin, Francesca Di Nunzio, Johan Xavier, Pierre Charneau, Yves Jacob, and Marc Lavigne. "TOX4 and NOVA1 Proteins Are Partners of the LEDGF PWWP Domain and Affect HIV-1 Replication." PLoS ONE 8, no. 11 (November 27, 2013): e81217. http://dx.doi.org/10.1371/journal.pone.0081217.

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Hung, Yi-Lin, Hsia-Ju Lee, Ingjye Jiang, Shang-Chi Lin, Wei-Cheng Lo, Yi-Jan Lin, and Shih-Che Sue. "The First Residue of the PWWP Motif Modulates HATH Domain Binding, Stability, and Protein–Protein Interaction." Biochemistry 54, no. 26 (June 24, 2015): 4063–74. http://dx.doi.org/10.1021/acs.biochem.5b00454.

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Xu, Wenqi, Jiahui Li, Bowen Rong, Bin Zhao, Mei Wang, Ruofei Dai, Qilong Chen, et al. "Correction to: DNMT3A reads and connects histone H3K36me2 to DNA methylation." Protein & Cell 11, no. 3 (December 9, 2019): 230. http://dx.doi.org/10.1007/s13238-019-00678-6.

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The author would like to add the below information in this correction. A similar study from Chao Lu group was published online on 5 September 2019 in Nature, entitled “The histone mark H3K36me2 recruits DNMT3A and shapes the intergenic DNA methylation landscape” (Weinberg et al., 2019). Although both the studies reported the preferential recognition of H3K36me2 by DNMT3A PWWP, ours in addition uncovered a stimulation function by such interaction on the activity of DNMT3A. On the disease connections, we used a NSD2 gain-of-function model which led to the discovery of potential therapeutic implication of DNA inhibitors in the related cancers, while the other study only used NSD1 and DNMT3A loss-of-function models.

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42

Tian, Wei, Peiqiang Yan, Ning Xu, Arghya Chakravorty, Robert Liefke, Qiaoran Xi, and Zhanxin Wang. "The HRP3 PWWP domain recognizes the minor groove of double-stranded DNA and recruits HRP3 to chromatin." Nucleic Acids Research 47, no. 10 (April 24, 2019): 5436–48. http://dx.doi.org/10.1093/nar/gkz294.

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43

Botbol, Y., N. K. Raghavendra, S. Rahman, A. Engelman, and M. Lavigne. "Chromatinized templates reveal the requirement for the LEDGF/p75 PWWP domain during HIV-1 integration in vitro." Nucleic Acids Research 36, no. 4 (December 20, 2007): 1237–46. http://dx.doi.org/10.1093/nar/gkm1127.

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Gijsbers, Rik, Sofie Vets, Jan De Rijck, Karen E. Ocwieja, Keshet Ronen, Nirav Malani, Frederic D. Bushman, and Zeger Debyser. "Role of the PWWP domain of lens epithelium-derived growth factor (LEDGF)/p75 cofactor in lentiviral integration targeting." Journal of Biological Chemistry 293, no. 1 (January 5, 2018): 114. http://dx.doi.org/10.1074/jbc.w117.001458.

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45

Hohenstatt, Mareike L., Pawel Mikulski, Olga Komarynets, Constanze Klose, Ina Kycia, Albert Jeltsch, Sara Farrona, and Daniel Schubert. "PWWP-DOMAIN INTERACTOR OF POLYCOMBS1 Interacts with Polycomb-Group Proteins and Histones and Regulates Arabidopsis Flowering and Development." Plant Cell 30, no. 1 (January 2018): 117–33. http://dx.doi.org/10.1105/tpc.17.00117.

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46

Gijsbers, Rik, Sofie Vets, Jan De Rijck, Karen E. Ocwieja, Keshet Ronen, Nirav Malani, Frederic D. Bushman, and Zeger Debyser. "Role of the PWWP Domain of Lens Epithelium-derived Growth Factor (LEDGF)/p75 Cofactor in Lentiviral Integration Targeting." Journal of Biological Chemistry 286, no. 48 (October 10, 2011): 41812–25. http://dx.doi.org/10.1074/jbc.m111.255711.

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Kenzior, Alexander, and William R. Folk. "Arabidopsis thaliana MSI4/FVE associates with members of a novel family of plant specific PWWP/RRM domain proteins." Plant Molecular Biology 87, no. 4-5 (January 20, 2015): 329–39. http://dx.doi.org/10.1007/s11103-014-0280-z.

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48

Savitsky, Pavel, Tobias Krojer, Takao Fujisawa, Jean-Philippe Lambert, Sarah Picaud, Chen-Yi Wang, Erin K. Shanle, et al. "Multivalent Histone and DNA Engagement by a PHD/BRD/PWWP Triple Reader Cassette Recruits ZMYND8 to K14ac-Rich Chromatin." Cell Reports 17, no. 10 (December 2016): 2724–37. http://dx.doi.org/10.1016/j.celrep.2016.11.014.

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Dukatz, Michael, Katharina Holzer, Michel Choudalakis, Max Emperle, Cristiana Lungu, Pavel Bashtrykov, and Albert Jeltsch. "H3K36me2/3 Binding and DNA Binding of the DNA Methyltransferase DNMT3A PWWP Domain Both Contribute to its Chromatin Interaction." Journal of Molecular Biology 431, no. 24 (December 2019): 5063–74. http://dx.doi.org/10.1016/j.jmb.2019.09.006.

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Sue, Shih-Che, Wei-Tin Lee, Shi-Chi Tien, Shao-Chen Lee, Jiun-Guo Yu, Wen-Jin Wu, Wen-guey Wu, and Tai-huang Huang. "PWWP Module of Human Hepatoma-derived Growth Factor Forms a Domain-swapped Dimer with Much Higher Affinity for Heparin." Journal of Molecular Biology 367, no. 2 (March 2007): 456–72. http://dx.doi.org/10.1016/j.jmb.2007.01.010.

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