A Mammalian Chromatin Remodeling Complex with Similarities to the Yeast INO80 Complex

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Abstract

The mammalian Tip49a and Tip49b proteins belong to an evolutionarily conserved family of AAA+ ATPases. In Saccharomyces cerevisiae, orthologs of Tip49a and Tip49b, called Rvb1 and Rvb2, respectively, are subunits of two distinct ATP-dependent chromatin remodeling complexes, SWR1 and INO80. We recently demonstrated that the mammalian Tip49a and Tip49b proteins are integral subunits of a chromatin remodeling complex bearing striking similarities to the S. cerevisiae SWR1 complex (Cai, Y., Jin, J., Florens, L., Swanson, S. K., Kusch, T., Li, B., Workman, J. L., Washburn, M. P., Conaway, R. C., and Conaway, J. W. (2005) J. Biol. Chem. 280, 13665–13670). In this report, we identify a new mammalian Tip49a- and Tip49b-containing ATP-dependent chromatin remodeling complex, which includes orthologs of 8 of the 15 subunits of the S. cerevisiae INO80 chromatin remodeling complex as well as at least five additional subunits unique to the human INO80 (hINO80) complex. Finally, we demonstrate that, similar to the yeast INO80 complex, the hINO80 complex exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding. The mammalian Tip49a and Tip49b proteins belong to an evolutionarily conserved family of AAA+ ATPases. In Saccharomyces cerevisiae, orthologs of Tip49a and Tip49b, called Rvb1 and Rvb2, respectively, are subunits of two distinct ATP-dependent chromatin remodeling complexes, SWR1 and INO80. We recently demonstrated that the mammalian Tip49a and Tip49b proteins are integral subunits of a chromatin remodeling complex bearing striking similarities to the S. cerevisiae SWR1 complex (Cai, Y., Jin, J., Florens, L., Swanson, S. K., Kusch, T., Li, B., Workman, J. L., Washburn, M. P., Conaway, R. C., and Conaway, J. W. (2005) J. Biol. Chem. 280, 13665–13670). In this report, we identify a new mammalian Tip49a- and Tip49b-containing ATP-dependent chromatin remodeling complex, which includes orthologs of 8 of the 15 subunits of the S. cerevisiae INO80 chromatin remodeling complex as well as at least five additional subunits unique to the human INO80 (hINO80) complex. Finally, we demonstrate that, similar to the yeast INO80 complex, the hINO80 complex exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding. The related mammalian Tip49a and Tip49b proteins are members of a family of AAA+ (associated with various cellular activities) ATPases with roles in DNA repair, recombination, and transcriptional regulation (1Neuwald A.F. Aravind L. Spouge J.L. Koonin E.V. Genome Res. 1999; 9: 27-43Crossref PubMed Google Scholar, 2Caruthers J.M. McKay D. Curr. Opin. Struct. Biol. 2002; 12: 123-133Crossref PubMed Scopus (455) Google Scholar). In Saccharomyces cerevisiae, the Tip49a and Tip49b proteins (also known as Rvb1 and Rvb2) participate in chromatin remodeling as subunits of the multiprotein SWR1 and INO80 ATP-dependent chromatin remodeling complexes (3Mizuguchi G. Shen X. Landry J. Wu W.H. Sen S. Wu C. Science. 2004; 303: 343-348Crossref PubMed Scopus (1003) Google Scholar, 4Krogan N.J. Baetz K. Keogh M.C. Datta N. Sawa C. Kwok T.C. Thompson N.J. Davey M.G. Pootoolal J. Hughes T.R. Emili A. Buratowski S. Hieter P. Greenblatt J.F. Proc. Natl. Acad. Sci. U. S. A. 2004; 101: 13513-13518Crossref PubMed Scopus (202) Google Scholar, 5Kobor M.S. Venkatasubrahmanyam S. Meneghini M.D. Gin J.W. Jennings J.L. Link A.J. Madhani H.D. Rine J. PLoS Biol. 2004. 2004; : 2/E131Google Scholar). The SWR1 complex remodels chromatin by catalyzing ATP-dependent replacement of H2A-H2B histone dimers in nucleosomes by dimers containing histone variant Htz1 (referred to as H2AZ in mammalian cells) (3Mizuguchi G. Shen X. Landry J. Wu W.H. Sen S. Wu C. Science. 2004; 303: 343-348Crossref PubMed Scopus (1003) Google Scholar). In addition to Tip49a and Tip49b, the SWR1 complex includes the SNF2 family helicase Swr1, actin-related proteins Arp4 and Arp6, YEATS domain family member Yaf9, bromodomain protein Bdf1, and additional proteins Swc3–Swc7, which are of unknown function (3Mizuguchi G. Shen X. Landry J. Wu W.H. Sen S. Wu C. Science. 2004; 303: 343-348Crossref PubMed Scopus (1003) Google Scholar, 4Krogan N.J. Baetz K. Keogh M.C. Datta N. Sawa C. Kwok T.C. Thompson N.J. Davey M.G. Pootoolal J. Hughes T.R. Emili A. Buratowski S. Hieter P. Greenblatt J.F. Proc. Natl. Acad. Sci. U. S. A. 2004; 101: 13513-13518Crossref PubMed Scopus (202) Google Scholar, 5Kobor M.S. Venkatasubrahmanyam S. Meneghini M.D. Gin J.W. Jennings J.L. Link A.J. Madhani H.D. Rine J. PLoS Biol. 2004. 2004; : 2/E131Google Scholar). The INO80 complex catalyzes ATP-dependent sliding of nucleosomes along DNA and, based on genetic and other evidence, may be involved in the repair of DNA double strand breaks and in transcriptional regulation (6Shen X. Mizuguchi G. Hamiche A. Wu C. Nature. 2000; 406: 541-544Crossref PubMed Scopus (667) Google Scholar, 7Shen X. Hua X. Ranallo R. Wei-Hua W. Wu C. Science. 2002; 299: 112-114Crossref PubMed Scopus (292) Google Scholar, 8Steger D.J. Haswell E.S. Miller A.L. Wente S.R. O'Shea E.K. Science. 2003; 299: 114-116Crossref PubMed Scopus (315) Google Scholar, 9Fritsch O. Benvenuto G. Bowler C. Molinier J. Hohn B. Mol. Cell. 2004; 16: 479-485Abstract Full Text Full Text PDF PubMed Scopus (121) Google Scholar, 10Ohdate H. Lim C.R. Kokubo T. Matsubara K. Kimata Y. Kohno K. J. Biol. Chem. 2003; 278: 14647-14656Abstract Full Text Full Text PDF PubMed Scopus (32) Google Scholar, 11van Attikum H. Fritsch O. Hohn B. Gasser S.M. Cell. 2004; 119: 777-788Abstract Full Text Full Text PDF PubMed Scopus (505) Google Scholar, 12Morrison A.J. Highland J. Krogan N.J. Arbel-Eden A. Greenblatt J.F. Haber J.E. Shen X. Cell. 2004; 119: 767-775Abstract Full Text Full Text PDF PubMed Scopus (470) Google Scholar). The INO80 complex includes Tip49a and Tip49b, the SNF2 family helicase Ino80, actin-related proteins Arp4, Arp5, and Arp8, YEATS domain family member Taf14, HMG (high mobility group) domain protein Nhp10, and six additional proteins designated Ies1–Ies6 (6Shen X. Mizuguchi G. Hamiche A. Wu C. Nature. 2000; 406: 541-544Crossref PubMed Scopus (667) Google Scholar, 13Shen X. Ranallo R. Choi E. Wu C. Mol. Cell. 2003; 12: 147-155Abstract Full Text Full Text PDF PubMed Scopus (288) Google Scholar). Thus, the SWR1 and INO80 complexes share three proteins (Tip49a, Tip49b, and Arp4) and contain additional homologous components. In addition, each of the two complexes has a number of unique subunits. The orthologs of the Tip49a and Tip49b AAA+ ATPases also play roles in chromatin remodeling in higher eukaryotes. Tip49a and Tip49b are subunits of the mammalian and Drosophila melanogaster TRRAP-TIP60 histone acetyltransferase (HAT) 3The abbreviations used are: HAThistone acetyltransferaseATPγSadenosine 5′-O-(thiotriphosphate)HEKhuman embryonic kidneyhINO80human INO80-like proteinHPLChigh pressure liquid chromatographyMudPITmultidimensional protein identification technologyNFRKBnuclear factor related to κB-binding proteinORFopen reading frameTafTATA-binding protein-associated factorTip49a and Tip49bTATA-binding protein interacting 49-kDa proteins a and b. complexes (14Cai Y. Jin J. Tomomori-Sato C. Sato S. Sorokina I. Parmely T.J. Conaway R.C. Conaway J.W. J. Biol. Chem. 2003; 278: 42733-42736Abstract Full Text Full Text PDF PubMed Scopus (170) Google Scholar, 15Doyon Y. Selleck W. Lane W.S. Cote J. Mol. Cell. Biol. 2004; 24: 1884-1896Crossref PubMed Scopus (445) Google Scholar, 16Ikura T. Ogryzko V. Gigoriev M. Groisman R. Wang J. Horikoshi M. Scully R. Qin J. Nakatani Y. Cell. 2000; 102: 463-473Abstract Full Text Full Text PDF PubMed Scopus (876) Google Scholar, 17Kusch T. Florens L. Macdonald W.H. Swanson S.K. Glaser R.L. Yates J.R. Abmayr S.M. Washburn M.P. Workman J.L. Science. 2004; 306: 2084-2087Crossref PubMed Scopus (555) Google Scholar). In addition to Tip49a and Tip49b, the TRRAP-TIP60 complex includes ATM/phosphatidylinositol 3-kinase family member TRRAP, the SNF2 family p400 or Domino helicase, actin-related protein Arp4, bromodomain-containing protein BRD8, the enhancer of polycomb (EPC) and/or enhancer of polycomb-like (EPC-like) protein, inhibitor of growth 3 (ING3), DNA methyltransferase 1-associated protein (DMAP1), MRG15 and/or the related MRGX protein, the MRGBP protein, and TIP60, a HAT belonging to the MYST family. Characterization of the activities associated with the higher eukaryotic TRRAP-TIP60 complex revealed that it possesses HAT activity similar to that of the S. cerevisiae NuA4 HAT complex, which acetylates histones H2A and H4 (reviewed in Ref. 18Doyon Y. Cote J. Curr. Opin. Genet. Dev. 2004; 14: 147-154Crossref PubMed Scopus (291) Google Scholar). The human and D. melanogaster TRRAP-TIP60 complexes were found to play critical roles in double-stranded DNA break repair (16Ikura T. Ogryzko V. Gigoriev M. Groisman R. Wang J. Horikoshi M. Scully R. Qin J. Nakatani Y. Cell. 2000; 102: 463-473Abstract Full Text Full Text PDF PubMed Scopus (876) Google Scholar, 17Kusch T. Florens L. Macdonald W.H. Swanson S.K. Glaser R.L. Yates J.R. Abmayr S.M. Washburn M.P. Workman J.L. Science. 2004; 306: 2084-2087Crossref PubMed Scopus (555) Google Scholar). Notably, the D. melanogaster TRRAP-TIP60 complex is capable of acetylating nucleosomal phospho-H2Av and replacing it with unmodified H2Av, indicating that in flies this single complex performs functions closely related to those of the yeast NuA4 HAT and SWR1 histone exchange complexes (17Kusch T. Florens L. Macdonald W.H. Swanson S.K. Glaser R.L. Yates J.R. Abmayr S.M. Washburn M.P. Workman J.L. Science. 2004; 306: 2084-2087Crossref PubMed Scopus (555) Google Scholar). histone acetyltransferase adenosine 5′-O-(thiotriphosphate) human embryonic kidney human INO80-like protein high pressure liquid chromatography multidimensional protein identification technology nuclear factor related to κB-binding protein open reading frame TATA-binding protein-associated factor TATA-binding protein interacting 49-kDa proteins a and b. We recently identified a new mammalian Tip49a- and Tip49b-containing ATP-dependent chromatin remodeling complex that bears striking similarity to the S. cerevisiae SWR1 complex (19Cai Y. Jin J. Florence L. Swanson S.K. Kusch T. Li B. Workman J.L. Washburn M.P. Conaway R.C. Conaway J.W. J. Biol. Chem. 2005; 280: 13665-13670Abstract Full Text Full Text PDF PubMed Scopus (167) Google Scholar). Purification of this complex revealed that it includes the SNF2 family and SWR1-related SRCAP helicase, as well as orthologs of most of the known subunits of the S. cerevisiae SWR1 complex. In the course of our characterization of the structure and function of the SRCAP complex, we identified an additional mammalian Tip49a- and Tip49b-containing chromatin remodeling complex. Here we describe the properties of this new chromatin remodeling complex, which includes orthologs of 8 of the 15 subunits of the S. cerevisiae INO80 chromatin remodeling complex as well as at least 5 additional subunits unique to the human INO80 (hINO80) complex. Generation and Growth of Mammalian Cell Lines—Full-length cDNAs encoding the human Tip49a, Tip49b, Arp8, PAPA-1 (hIes2), C18orf37 (hIes6), Amida, and FLJ90652 proteins or a fragment of FLJ20309 (residues 106–544) were obtained from the American Type Culture Collection, subcloned with FLAG tags into pcDNA5/FRT, and introduced into HEK293/FRT cells using the Invitrogen Flp-in system. Full-length cDNAs encoding the human PAPA-1 and C18orf37 proteins were subcloned with FLAG tags into pcDNA3.1 and introduced into HeLa S3 cells. Parental and stably transformed HEK293/FRT and HeLa S3 cells were maintained in Dulbecco's modified Eagle's medium with 5% glucose and 10% fetal bovine serum. For large scale cultures, HeLa cells were grown in spinner culture in Joklik medium with 5% calf serum. Anti-FLAG Agarose Chromatography—Whole cell extracts were prepared from HEK293/FRT cells as follows. Cells were grown to 70–80% confluence in four to five 15-cm dishes. Cells were washed in dishes with phosphate-buffered saline and then lysed by resuspension in buffer (1 ml/dish) containing 40 mm Hepes-NaOH (pH 7.9), 0.45 m NaCl, 1.5 mm MgCl2, 10% glycerol, 1 mm dithiothreitol, and 0.2% Triton X-100. The resulting suspension was transferred to centrifuge tubes and incubated with rotation at 4 °C for 30 min. The cell lysate was centrifuged at 40,000 rpm for 60 min at 4 °C in a 70.1 Ti rotor (Beckman-Coulter). The resulting supernatant was subjected to anti-FLAG agarose chromatography. Nuclear extracts were prepared from HeLa S3 cells according to the method of Dignam et al. (20Dignam J.D. Lebovitz R.M. Roeder R.G. Nucleic Acids Res. 1983; 11: 1475-1489Crossref PubMed Scopus (9164) Google Scholar). Whole cell or nuclear extracts were adjusted to 0.3 m NaCl and 0.2% Triton X-100 and centrifuged at 40,000 rpm for 30 min at 4 °C in a Ti-45 rotor. Supernatants were then mixed with anti-FLAG (M2) agarose beads (Sigma) in a ratio of 100 μl of packed beads/6 ml of supernatant and gently rocked for 4 h at 4 °C. The beads were washed three times with a 50-fold excess of buffer containing 40 mm Hepes-NaOH (pH 7.9), 0.25 m NaCl, 0.2% Triton X-100, and 10% glycerol and once with the same buffer containing 0.1 m NaCl. Proteins were eluted from the beads twice by incubation for 30 min on a rotator at 4 °C with 100 μl of 40 mm Hepes-NaOH (pH 7.9), 0.1 m NaCl, 0.1 mm EDTA, 10% glycerol, and 0.2 mg/ml FLAG peptide (Sigma). Glycerol was omitted from the elution buffer for samples to be analyzed by mass spectrometry. ATPase Assays—Reaction mixtures of 20 μl contained 50 mm Hepes-NaOH (pH 7.6), 70 mm NaCl, 5 mm MgCl2, 0.5 mm EGTA, 0.1 mm EDTA, 10% glycerol, 0.02% Nonidet P-40, 0.2 mm dithiothreitol, 100 μg/ml bovine serum albumin, 40 μm ATP, 0.2 μCi of [α-32P]ATP (400 Ci/mmol, Amersham Biosciences). Where indicated, reaction mixtures contained the hINO80 complex purified from HeLa cells expressing FLAG-hIes2 (PAPA-1) and 150 ng of mononucleosomes or long oligonucleosomes prepared from HeLa cells as described (21Owen-Hughes T. Utley R.T. Steger D.J. West J.M. John S. Cote J. Havas K.M. Workman J.L. Methods Mol. Biol. 1999; 119: 319-331PubMed Google Scholar). After incubation at 37 °C for 30 min, reactions were stopped by the addition of 2 μl of 20 mm EDTA (pH 8.0). A 2-μl aliquot of each reaction mixture was spotted onto a cellulose polyethyleneimine TLC plate (JT Baker). The plate was then developed with 0.375 m potassium phosphate (pH 3.5). Reaction products were detected and quantitated using a Typhoon phosphorimaging device (GE Healthcare). Nucleosome Remodeling Assays—A 216-bp DNA fragment (dSH-A) was generated by PCR from pGUB-dSH in the presence of [α-32P]dCTP. pGUB-dSH was generated by deleting the SalI to HindIII fragment of pGUB (22Juan L.J. Utley R.T. Vignali M. Bohm L. Workman J.L. J. Biol. Chem. 1997; 272: 3635-3640Abstract Full Text Full Text PDF PubMed Scopus (52) Google Scholar). Mononucleosomes were reconstituted on this labeled DNA fragment by from HeLa long of nucleosomes was mixed with of DNA fragment in μl of buffer containing m NaCl, mm (pH 1 mm EDTA (pH 0.5 mm and 5 mm After 30 min at 30 the mixture was adjusted to and m NaCl by with mm (pH 1 mm EDTA (pH 0.5 mm and 5 mm dithiothreitol, with a incubation at 30 °C each to 0.2 and 0.1 m NaCl were using the same buffer Nonidet P-40, glycerol, and μg/ml bovine serum After the mononucleosomes were in at °C. hINO80 complex purified from HeLa cells expressing was incubated at 37 °C with μl of reconstituted mononucleosomes of labeled of in buffer containing 20 mm Hepes-NaOH (pH 7.9), 50 mm NaCl, mm MgCl2, 2 mm dithiothreitol, 0.5 mm μg/ml bovine serum albumin, 10% glycerol, 0.02% Triton X-100, 0.02% Nonidet P-40, and 1 mm After a 0.5 of HeLa cell long oligonucleosomes (21Owen-Hughes T. Utley R.T. Steger D.J. West J.M. John S. Cote J. Havas K.M. Workman J.L. Methods Mol. Biol. 1999; 119: 319-331PubMed Google and of DNA and were and reactions were incubated for an additional 30 min at 37 °C to DNA- or proteins that The reaction products were then to 5% in J. Fritsch T. A : and subjected to at 4 °C for h at V. were and to a of proteins was as described (19Cai Y. Jin J. Florence L. Swanson S.K. Kusch T. Li B. Workman J.L. Washburn M.P. Conaway R.C. Conaway J.W. J. Biol. Chem. 2005; 280: 13665-13670Abstract Full Text Full Text PDF PubMed Scopus (167) Google using a of the multidimensional protein identification technology of Washburn et al. M.P. D. Yates J.R. PubMed Scopus Google Scholar). proteins were and with modified mixtures were to a W.H. R. T.J. Yates J.R. J. 2002; Scopus Google packed with 5 μm by exchange and then by 5 μm and in 5% were eluted from the to the with six of After each were eluted from the with a of into a mass with a chromatography The R.G. J. E. A. H. Yates J.R. J. Res. 2002; PubMed Scopus Google was used to the and to The A.L. Yates J.R. J. PubMed Scopus Google was used to mass to human from the A.L. Yates J.R. J. PubMed Scopus Google human protein as of were a in of at least and a of for for and for and the were at least Tip49a and Tip49b with a INO80-like of our characterization of the and functions of mammalian TRRAP-TIP60 and SRCAP chromatin remodeling complexes, we generated cell stably expressing Tip49a or Tip49b with FLAG tags and then purified Tip49a- and proteins by anti-FLAG agarose chromatography. a for the of extracts prepared from cells were subjected to the same in anti-FLAG agarose from and cells to similar of proteins 1 and identify and and we of M.P. D. Yates J.R. PubMed Scopus Google Scholar, D. Washburn M.P. Yates J.R. Chem. PubMed Scopus Google a method for proteins in complex In a a mixture of proteins is into which are then by exchange and and analyzed by mass spectrometry. in of anti-FLAG agarose from and cells in addition to the known subunits of the TRRAP-TIP60 and SRCAP complexes, a of proteins found in TRRAP-TIP60 or SRCAP or in proteins was a SNF2 family helicase by the by of in and by the protein is an human of the S. cerevisiae helicase R. T. D. V. Res. 2004; PubMed Scopus Google Scholar). proteins were the actin-related proteins and Arp8, each of which has a yeast found in the INO80 complex in the SWR1 complex 1 and of the hINO80 the that or of proteins were subunits of a mammalian INO80 complex, we generated an HEK293/FRT cell stably expressing with an FLAG prepared from cells were subjected to anti-FLAG agarose and proteins in anti-FLAG agarose were identified by in with Tip49a and Tip49b, Arp5, and an additional proteins that were in the TRRAP-TIP60 or SRCAP proteins the protein-associated protein H. T. T. H. H. S.M. 2004; PubMed Scopus Google (also known as in Y. K. Y. K. E. E. N. J. Biol. Chem. 2000; Full Text Full Text PDF PubMed Scopus Google Scholar, G. M. A. C. M. G. L. A. E. 1999; PubMed Scopus Google nuclear factor related to κB-binding protein Biol. Google protein 1 or Y. Y. H. J. PubMed Scopus Google and proteins by the FLJ90652 C18orf37 and FLJ20309 proteins were in the same complex, we generated additional HeLa and HEK293/FRT cell stably expressing Amida, or with FLAG or a fragment of FLJ20309 (residues in 1 4 and anti-FLAG agarose prepared from expressing HeLa cells and from expressing HEK293/FRT cells to similar of revealed that Amida, and FLJ90652 each with the hINO80 helicase and the Tip49a, Tip49b, Arp4, Arp5, Arp8, Amida, and FLJ20309 which that are of a multiprotein complex Notably, unique subunits of the TRRAP-TIP60 or SRCAP complexes were detected by in of purified samples that of proteins are orthologs of subunits of the yeast INO80 complex. PAPA-1 is to the of the yeast INO80 complex, and we it is used as a in a the PAPA-1 from the of at the by at We that is in the as high mobility it to contain or high mobility the of the protein of a long the is and conserved The human C18orf37 protein is to the of the yeast INO80 complex. of protein family using the J. 2005; PubMed Scopus Google that proteins contain a modified most closely related to the family of transcriptional I. H. Y. M. M. Res. PubMed Scopus Google Scholar, I. H. Y. M. M. M. Cell Res. PubMed Scopus Google Scholar). We identified the protein as a of the mammalian TRRAP-TIP60 and SRCAP complexes (19Cai Y. Jin J. Florence L. Swanson S.K. Kusch T. Li B. Workman J.L. Washburn M.P. Conaway R.C. Conaway J.W. J. Biol. Chem. 2005; 280: 13665-13670Abstract Full Text Full Text PDF PubMed Scopus (167) Google Scholar). The five proteins to be unique to the human INO80 complex. is a large The of The of this protein is conserved in for in and in it to in a domain in are in the of a distinct well conserved in and found in the The FLJ20309 protein has a of conserved and the protein, FLJ20309 orthologs to be in in Amida, or in a domain of the The FLJ90652 protein has an domain that is related to The hINO80 ATP-dependent Nucleosome revealed that the S. cerevisiae INO80 complex possesses DNA- and nucleosome-activated ATPase and ATP-dependent nucleosome sliding the that the mammalian complex possesses similar we anti-FLAG agarose from HeLa cells for ATPase and nucleosome remodeling in the hINO80 complex, from in a reaction that was on the addition of DNA or mononucleosomes and oligonucleosomes ATPase histone on the the hINO80 complex ATP-dependent nucleosome anti-FLAG agarose from FLAG-hIes2 expressing HeLa cells were mixed with mononucleosomes reconstituted on a DNA fragment in the presence of or a mixture of and a inhibitor of ATPases. the of the HeLa and DNA were as to DNA- or proteins that Reaction products were then on The mobility of mononucleosomes on the of the nucleosome on the The mobility of a nucleosome in the of the DNA fragment is nucleosomes G. S. J. 11: PubMed Scopus Google Scholar, I. V. S. A. J. Mol. Biol. PubMed Scopus Google Scholar). The reconstituted nucleosomes used in our a mixture of and with the of nucleosomes at the DNA and the addition of of the purified hINO80 complex, nucleosomes were to a 5 and were obtained hINO80 complexes were from cells expressing or with and The in nucleosome by the hINO80 complex and is by Thus, the yeast INO80 complex, the hINO80 complex ATP-dependent nucleosome sliding. Notably, the yeast and human INO80 complexes nucleosomes from a to a and this we a to identify and a mammalian ATP-dependent chromatin remodeling complex that and properties with the S. cerevisiae INO80 complex new mammalian chromatin remodeling complex the SNF2 family helicase by the as well as additional proteins that to be orthologs of subunits of the yeast INO80 the Tip49a and Tip49b AAA+ the actin-related proteins Arp4, Arp5, and Arp8, and Notably, the hINO80 complex five additional proteins that to yeast the protein, the protein, the protein, and proteins by the FLJ90652 and FLJ20309 Finally, we that, in the of the yeast and human INO80 complexes, complexes similar chromatin remodeling the of the subunits of the hINO80 complex into the similarities and the yeast and mammalian chromatin remodeling of the of the yeast and mammalian chromatin remodeling function and domain a unique for protein or in the protein and a unique for protein or in the protein and and related to family of in C. in C. domain in the of orthologs in and high mobility or a unique for protein or in the protein and high mobility in a new

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