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PWWP module of human hepatoma-derived growth factor forms a domain-swapped dimer with much higher affinity for heparin.

Sue SC, Lee WT, Tien SC, Lee SC, Yu JG, Wu WJ, Wu WG, Huang TH
J Mol Biol 367 456-72 (2007)
Cited: 21 times
EuropePMC logo PMID: 17270212

Abstract

Hepatoma-derived growth factor (hHDGF)-related proteins (HRPs) comprise a new growth factor family sharing a highly conserved and ordered N-terminal PWWP module (residues 1-100, previously referred to as a HATH domain) and a variable disordered C-terminal domain. We have shown that the PWWP module is responsible for heparin binding and have solved its structure in solution. Here, we show that under physiological conditions, both the PWWP module and hHDGF can form dimers. Surface plasmon resonance (SPR) studies revealed that the PWWP dimer binds to heparin with affinity that is two orders of magnitude higher (K(d)=13 nM) than that of the monomeric PWWP module (K(d)=1.2 microM). The monomer-dimer equilibrium properties and NMR structural data together suggest that the PWWP dimer is formed through a domain-swapping mechanism. The domain-swapped PWWP dimer structures were calculated on the basis of the NMR data. The results show that the two PWWP protomers exchange their N-terminal hairpin to form a domain-swapped dimer. The two monomers in a dimer are linked by the long flexible L2 loops, a feature supported by NMR relaxation data for the monomer and dimer. The enhanced heparin-binding affinity of the dimer can be rationalized in the framework of the dimer structure.

Reviews - 2nlu mentioned but not cited (1)

  1. PWWP domains and their modes of sensing DNA and histone methylated lysines. Rona GB, Eleutherio ECA, Pinheiro AS. Biophys Rev 8 63-74 (2016)

Articles - 2nlu mentioned but not cited (1)

  1. Domain swapping and SMYD1 interactions with the PWWP domain of human hepatoma-derived growth factor. Chen LY, Huang YC, Huang ST, Hsieh YC, Guan HH, Chen NC, Chuankhayan P, Yoshimura M, Tai MH, Chen CJ. Sci Rep 8 287 (2018)


Reviews citing this publication (4)

  1. Structure and function of the nucleosome-binding PWWP domain. Qin S, Min J. Trends Biochem Sci 39 536-547 (2014)
  2. Keeping it in the family: diverse histone recognition by conserved structural folds. Yap KL, Zhou MM. Crit Rev Biochem Mol Biol 45 488-505 (2010)
  3. Survey of the year 2007 commercial optical biosensor literature. Rich RL, Myszka DG. J Mol Recognit 21 355-400 (2008)
  4. HDGF: a novel jack-of-all-trades in cancer. Bao C, Wang J, Ma W, Wang X, Cheng Y. Future Oncol 10 2675-2685 (2014)

Articles citing this publication (15)

  1. Hepatoma-derived growth factor binds DNA through the N-terminal PWWP domain. Yang J, Everett AD. BMC Mol Biol 8 101 (2007)
  2. The transcriptional co-activator LEDGF/p75 displays a dynamic scan-and-lock mechanism for chromatin tethering. Hendrix J, Gijsbers R, De Rijck J, Voet A, Hotta J, McNeely M, Hofkens J, Debyser Z, Engelborghs Y. Nucleic Acids Res 39 1310-1325 (2011)
  3. Cell surface heparan sulfates mediate internalization of the PWWP/HATH domain of HDGF via macropinocytosis to fine-tune cell signalling processes involved in fibroblast cell migration. Wang CH, Davamani F, Sue SC, Lee SC, Wu PL, Tang FM, Shih C, Huang TH, Wu WG. Biochem J 433 127-138 (2011)
  4. Hepatoma-derived growth factor-related protein-3 interacts with microtubules and promotes neurite outgrowth in mouse cortical neurons. El-Tahir HM, Abouzied MM, Gallitzendoerfer R, Gieselmann V, Franken S. J Biol Chem 284 11637-11651 (2009)
  5. Interactome study suggests multiple cellular functions of hepatoma-derived growth factor (HDGF). Zhao J, Yu H, Lin L, Tu J, Cai L, Chen Y, Zhong F, Lin C, He F, Yang P. J Proteomics 75 588-602 (2011)
  6. TOX4 and NOVA1 proteins are partners of the LEDGF PWWP domain and affect HIV-1 replication. Morchikh M, Naughtin M, Di Nunzio F, Xavier J, Charneau P, Jacob Y, Lavigne M. PLoS One 8 e81217 (2013)
  7. Secretion of hepatoma-derived growth factor is regulated by N-terminal processing. Thakar K, Kröcher T, Savant S, Gollnast D, Kelm S, Dietz F. Biol Chem 391 1401-1410 (2010)
  8. SUMOylation of the hepatoma-derived growth factor negatively influences its binding to chromatin. Thakar K, Niedenthal R, Okaz E, Franken S, Jakobs A, Gupta S, Kelm S, Dietz F. FEBS J 275 1411-1426 (2008)
  9. Structure, mechanics, and binding mode heterogeneity of LEDGF/p75-DNA nucleoprotein complexes revealed by scanning force microscopy. Vanderlinden W, Lipfert J, Demeulemeester J, Debyser Z, De Feyter S. Nanoscale 6 4611-4619 (2014)
  10. Hepatoma-derived growth factor-related protein-3: a new neurotrophic and neurite outgrowth-promoting factor for cortical neurons. Abouzied MM, El-Tahir HM, Gieselmann V, Franken S. J Neurosci Res 88 3610-3620 (2010)
  11. Exploring the glycosaminoglycan-protein interaction network by glycan-mediated pull-down proteomics. Gesslbauer B, Derler R, Handwerker C, Seles E, Kungl AJ. Electrophoresis 37 1437-1447 (2016)
  12. Interaction of HRP-2 isoforms with HDGF: chromatin binding of a specific heteromer. Thakar K, Votteler I, Kelkar D, Shidore T, Gupta S, Kelm S, Dietz F. FEBS J 279 737-751 (2012)
  13. Significance of heparin binding to basic residues in homologous to the amino terminus of hepatoma-derived growth factor and related proteins. Chen FF, Lin WH, Lin SC, Kuo JH, Chu HY, Huang WC, Chuang YJ, Lee SC, Sue SC. Glycobiology 22 649-661 (2012)
  14. NMR characterization of the electrostatic interaction of the basic residues in HDGF and FGF2 during heparin binding. Chiu LY, Hung KW, Tjong SC, Chiang YW, Sue SC. Biochim Biophys Acta 1844 1851-1859 (2014)
  15. Proteomic analysis of the hyaloid vascular system regression during ocular development. Albè E, Chang JH, Azar NF, Ivanov AR, Azar DT. J Proteome Res 7 4904-4913 (2008)


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