Publications
39 results found
Elderkin S, Maertens GN, Endoh M, et al., 2007, A phosphorylated form of mel-18 targets the Ring1B histone H2A ubliquitin ligase to chromatin, MOLECULAR CELL, Vol: 28, Pages: 107-120, ISSN: 1097-2765
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- Citations: 109
Maertens GN, Cherepanov P, Engelman A, 2006, Transcriptional co-activator p75 binds and tethers the Myc-interacting protein JPO2 to chromatin, JOURNAL OF CELL SCIENCE, Vol: 119, Pages: 2563-2571, ISSN: 0021-9533
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- Citations: 96
Turlure F, Maertens G, Rahman S, et al., 2006, A tripartite DNA-binding element, comprised of the nuclear localization signal and two AT-hook motifs, mediates the association of LEDGF/p75 with chromatin in vivo, Nucleic Acids Research, Vol: 34, Pages: 1653-1665, ISSN: 1362-4962
Lens epithelium-derived growth factor p75 (LEDGF/p75) is a DNA-binding, transcriptional co-activator that participates in HIV-1 integration site targeting. Using complementary approaches, we determined the mechanisms of LEDGF/p75 DNA-binding in vitro and chromatin-association in living cells. The binding of highly-purified, recombinant protein was assayed by surface plasmon resonance (SPR) and electrophoretic mobility gel shift. Neither assay revealed evidence for sequence-specific DNA-binding. Residues 146–197 spanning the nuclear localization signal (NLS) and two AT-hook motifs mediated non-specific DNA-binding, and DNA-binding deficient mutants retained the ability to efficiently stimulate HIV-1 integrase activity in vitro. Chromatin-association was assessed by visualizing the localization of EGFP fusion proteins in interphase and mitotic cells. Although a conserved N-terminal PWWP domain was not required for binding to condensed mitotic chromosomes, its deletion subtly affected the nucleoplasmic distribution of the protein during interphase. A dual AT-hook mutant associated normally with chromatin, yet when the mutations were combined with NLS changes or deletion of the PWWP domain, chromatin-binding function was lost. As the PWWP domain did not readily bind free DNA in vitro, our results indicate that chromatin-association is primarily affected through DNA-binding, with the PWWP domain likely contributing a protein interaction to the overall affinity of LEDGF/p75 for human chromatin.
Cherepanov P, Sun ZYJ, Rahman S, et al., 2005, Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75, NATURE STRUCTURAL & MOLECULAR BIOLOGY, Vol: 12, Pages: 526-532, ISSN: 1545-9993
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- Citations: 194
Maertens G, Vercammen J, Debyser Z, et al., 2005, Measuring protein-protein interactions inside living cells using single color fluorescence correlation spectroscopy. Application to human immunodeficiency virus type I integrase and LEDGF/p75, FASEB JOURNAL, Vol: 19, Pages: 1039-+, ISSN: 0892-6638
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- Citations: 36
Maertens G, Cherepanov P, Debyser Z, et al., 2004, Identification and characterization of a functional nuclear localization signal in the HIV-1 integrase interactor LEDGF/p75, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 279, Pages: 33421-33429, ISSN: 0021-9258
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- Citations: 82
Maertens G, Cherepanov P, Pluymers W, et al., 2003, LEDGF/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 278, Pages: 33528-33539, ISSN: 0021-9258
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- Citations: 403
Cherepanov P, Maertens G, Proost P, et al., 2003, HIV-1 integrase forms stable tetramers and associates with LEDGF/p75 protein in human cells, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 278, Pages: 372-381, ISSN: 0021-9258
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- Citations: 549
Vercammen J, Maertens G, Gerard M, et al., 2002, DNA-induced polymerization of HIV-1 integrase analyzed with fluorescence fluctuation spectroscopy, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 277, Pages: 38045-38052, ISSN: 0021-9258
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- Citations: 31
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