메뉴 건너뛰기




Volumn 429, Issue 1, 2010, Pages 113-125

Oligomeric assembly and interactions within the human RuvB-like RuvBL1 and RuvBL2 complexes

Author keywords

Analytical ultracentrifugation oligomerization analysis; ATPase associated with various cellular activities (AAA+ protein); Complex formation; Mass spectrometry (MS); RuvB like 1 (RuvBL1); RuvB like 2 (RuvBL2)

Indexed keywords

ANALYTICAL ULTRACENTRIFUGATION; ANALYTICAL ULTRACENTRIFUGATION OLIGOMERIZATION ANALYSIS; CELLULAR ACTIVITIES; COMPLEX FORMATION; COMPLEX FORMATIONS; RUVB-LIKE 1 (RUVBL1);

EID: 77954512714     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100489     Document Type: Article
Times cited : (39)

References (53)
  • 1
    • 66449130744 scopus 로고    scopus 로고
    • RVB1/RVB2: Running rings around molecular biology
    • Jha, S. and Dutta, A. (2009) RVB1/RVB2: running rings around molecular biology. Mol. Cell 34, 521-533
    • (2009) Mol. Cell , vol.34 , pp. 521-533
    • Jha, S.1    Dutta, A.2
  • 2
    • 33947724287 scopus 로고    scopus 로고
    • Control of transcription by Pontin and Reptin
    • Gallant, P. (2007) Control of transcription by Pontin and Reptin. Trends Cell Biol. 17, 187-192
    • (2007) Trends Cell Biol. , vol.17 , pp. 187-192
    • Gallant, P.1
  • 3
    • 67649522013 scopus 로고    scopus 로고
    • Enriching protein-protein and functional interaction networks in human embryonic stem cells
    • Zuo, C., Liang, S., Wang, Z., Li, H., Zheng, W. and Ma, W. (2009) Enriching protein-protein and functional interaction networks in human embryonic stem cells. Int. J. Mol. Med. 23, 811-819
    • (2009) Int. J. Mol. Med. , vol.23 , pp. 811-819
    • Zuo, C.1    Liang, S.2    Wang, Z.3    Li, H.4    Zheng, W.5    Ma, W.6
  • 5
    • 33846286030 scopus 로고    scopus 로고
    • Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex
    • Puri, T., Wendler, P., Sigala, B., Saibil, H. and Tsaneva, I. R. (2007) Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex. J. Mol. Biol. 366, 179-192
    • (2007) J. Mol. Biol. , vol.366 , pp. 179-192
    • Puri, T.1    Wendler, P.2    Sigala, B.3    Saibil, H.4    Tsaneva, I.R.5
  • 9
    • 0033529547 scopus 로고    scopus 로고
    • TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a
    • Kanemaki, M., Kurokawa, Y., Matsuura, T., Makino, Y., Masani, A., Okazaki, K., Morishita, T. and Tamura, T. A. (1999) TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a. J. Biol. Chem. 274, 22437-22444
    • (1999) J. Biol. Chem. , vol.274 , pp. 22437-22444
    • Kanemaki, M.1    Kurokawa, Y.2    Matsuura, T.3    Makino, Y.4    Masani, A.5    Okazaki, K.6    Morishita, T.7    Tamura, T.A.8
  • 11
    • 0035844141 scopus 로고    scopus 로고
    • Rvb1p and Rvb2p are essential components of a chromatin remodeling complex that regulates transcription of over 5% of yeast genes
    • Jonsson, Z. O., Dhar, S. K., Narlikar, G. J., Auty, R., Wagle, N., Pellman, D., Pratt, R. E., Kingston, R. and Dutta, A. (2001) Rvb1p and Rvb2p are essential components of a chromatin remodeling complex that regulates transcription of over 5% of yeast genes. J. Biol. Chem. 276, 16279-16288
    • (2001) J. Biol. Chem. , vol.276 , pp. 16279-16288
    • Jonsson, Z.O.1    Dhar, S.K.2    Narlikar, G.J.3    Auty, R.4    Wagle, N.5    Pellman, D.6    Pratt, R.E.7    Kingston, R.8    Dutta, A.9
  • 12
    • 0034601464 scopus 로고    scopus 로고
    • A chromatin remodelling complex involved in transcription and DNA processing
    • Shen, X., Mizuguchi, G., Hamiche, A. and Wu, C. (2000) A chromatin remodelling complex involved in transcription and DNA processing. Nature 406, 541-544
    • (2000) Nature , vol.406 , pp. 541-544
    • Shen, X.1    Mizuguchi, G.2    Hamiche, A.3    Wu, C.4
  • 13
    • 59649124959 scopus 로고    scopus 로고
    • The INO80 chromatin remodeling complex in transcription, replication and repair
    • Conaway, R. C. and Conaway, J. W. (2009) The INO80 chromatin remodeling complex in transcription, replication and repair. Trends Biochem. Sci. 34, 71-77
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 71-77
    • Conaway, R.C.1    Conaway, J.W.2
  • 14
    • 34748904017 scopus 로고    scopus 로고
    • A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP assembly
    • McKeegan, K. S., Debieux, C. M., Boulon, S., Bertrand, E. and Watkins, N. J. (2007) A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP assembly. Mol. Cell. Biol. 27, 6782-6793
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6782-6793
    • McKeegan, K.S.1    Debieux, C.M.2    Boulon, S.3    Bertrand, E.4    Watkins, N.J.5
  • 15
    • 9744222917 scopus 로고    scopus 로고
    • Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex
    • Watkins, N. J., Lemm, I., Ingelfinger, D., Schneider, C., Hossbach, M., Urlaub, H. and Luhrmann, R. (2004) Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex. Mol. Cell 16, 789-798
    • (2004) Mol. Cell , vol.16 , pp. 789-798
    • Watkins, N.J.1    Lemm, I.2    Ingelfinger, D.3    Schneider, C.4    Hossbach, M.5    Urlaub, H.6    Luhrmann, R.7
  • 16
    • 40749135820 scopus 로고    scopus 로고
    • Identification of ATPases Pontin and Reptin as Telomerase Components Essential for Holoenzyme Assembly
    • DOI 10.1016/j.cell.2008.01.019, PII S0092867408001190
    • Venteicher, A. S., Meng, Z., Mason, P. J., Veenstra, T. D. and Artandi, S. E. (2008) Identification of ATPases pontin and reptin as telomerase components essential for holoenzyme assembly. Cell 132, 945-957 (Pubitemid 351381739)
    • (2008) Cell , vol.132 , Issue.6 , pp. 945-957
    • Venteicher, A.S.1    Meng, Z.2    Mason, P.J.3    Veenstra, T.D.4    Artandi, S.E.5
  • 17
    • 51349153303 scopus 로고    scopus 로고
    • Regulation of microtubule assembly and organization in mitosis by the AAA+ ATPase Pontin
    • Ducat, D., Kawaguchi, S., Liu, H., Yates, J. R. and Zheng, 3rd, Y. (2008) Regulation of microtubule assembly and organization in mitosis by the AAA+ ATPase Pontin. Mol. Biol. Cell 19, 3097-3110
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3097-3110
    • Ducat, D.1    Kawaguchi, S.2    Liu, H.3    Yates, J.R.4    Zheng III, Y.5
  • 19
    • 26844527774 scopus 로고    scopus 로고
    • Relocalization of human chromatin remodeling cofactor TIP48 in mitosis
    • Sigala, B., Edwards, M., Puri, T. and Tsaneva, I. R. (2005) Relocalization of human chromatin remodeling cofactor TIP48 in mitosis. Exp. Cell Res. 310, 357-369
    • (2005) Exp. Cell Res. , vol.310 , pp. 357-369
    • Sigala, B.1    Edwards, M.2    Puri, T.3    Tsaneva, I.R.4
  • 20
    • 4043181214 scopus 로고    scopus 로고
    • Cancer genes and the pathways they control
    • Vogelstein, B. and Kinzler, K. W. (2004) Cancer genes and the pathways they control. Nat. Med. 10, 789-799
    • (2004) Nat. Med. , vol.10 , pp. 789-799
    • Vogelstein, B.1    Kinzler, K.W.2
  • 21
    • 52049115398 scopus 로고    scopus 로고
    • Pontin and reptin, two related ATPases with multiple roles in cancer
    • Huber, O., Menard, L., Haurie, V., Nicou, A., Taras, D. and Rosenbaum, J. (2008) Pontin and reptin, two related ATPases with multiple roles in cancer. Cancer Res. 68, 6873-6876
    • (2008) Cancer Res. , vol.68 , pp. 6873-6876
    • Huber, O.1    Menard, L.2    Haurie, V.3    Nicou, A.4    Taras, D.5    Rosenbaum, J.6
  • 22
    • 33646375978 scopus 로고    scopus 로고
    • Purification of a human SRCAP complex that remodels chromatin by incorporating the histone variant H2A.Z into nucleosomes
    • Ruhl, D. D., Jin, J., Cai, Y., Swanson, S., Florens, L., Washburn, M. P., Conaway, R. C., Conaway, J. W. and Chrivia, J. C. (2006) Purification of a human SRCAP complex that remodels chromatin by incorporating the histone variant H2A.Z into nucleosomes. Biochemistry 45, 5671-5677
    • (2006) Biochemistry , vol.45 , pp. 5671-5677
    • Ruhl, D.D.1    Jin, J.2    Cai, Y.3    Swanson, S.4    Florens, L.5    Washburn, M.P.6    Conaway, R.C.7    Conaway, J.W.8    Chrivia, J.C.9
  • 24
    • 8644257491 scopus 로고    scopus 로고
    • Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex
    • Jonsson, Z. O., Jha, S., Wohlschlegel, J. A. and Dutta, A. (2004) Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex. Mol. Cell 16, 465-477
    • (2004) Mol. Cell , vol.16 , pp. 465-477
    • Jonsson, Z.O.1    Jha, S.2    Wohlschlegel, J.A.3    Dutta, A.4
  • 25
    • 17244378084 scopus 로고    scopus 로고
    • Transcriptional regulation of a metastasis suppressor gene by Tip60 and β-catenin complexes
    • Kim, J. H., Kim, B., Cai, L., Choi, H. J., Ohgi, K. A., Tran, C., Chen, C., Chung, C. H., Huber, O., Rose, D. W. et al. (2005) Transcriptional regulation of a metastasis suppressor gene by Tip60 and β-catenin complexes. Nature 434, 921-926
    • (2005) Nature , vol.434 , pp. 921-926
    • Kim, J.H.1    Kim, B.2    Cai, L.3    Choi, H.J.4    Ohgi, K.A.5    Tran, C.6    Chen, C.7    Chung, C.H.8    Huber, O.9    Rose, D.W.10
  • 29
    • 0032969563 scopus 로고    scopus 로고
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., Aravind, L., Spouge, J. L. and Koonin, E. V. (1999) AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43 (Pubitemid 29095146)
    • (1999) Genome Research , vol.9 , Issue.1 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 32
    • 39049098269 scopus 로고    scopus 로고
    • Yeast Rvb1 and Rvb2 are ATP-dependent DNA helicases that form a heterohexameric complex
    • Gribun, A., Cheung, K. L., Huen, J., Ortega, J. and Houry, W. A. (2008) Yeast Rvb1 and Rvb2 are ATP-dependent DNA helicases that form a heterohexameric complex. J. Mol. Biol. 376, 1320-1333
    • (2008) J. Mol. Biol. , vol.376 , pp. 1320-1333
    • Gribun, A.1    Cheung, K.L.2    Huen, J.3    Ortega, J.4    Houry, W.A.5
  • 33
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding, S. E., Rowe, A. J. and Horton, J., eds, Royal Society of Chemistry, Cambridge
    • Laue, T. M., Shah, B. D., Ridgeway, T. M. and Pelletier, S. L. (1992) Computer-aided interpretation of analytical sedimentation data for proteins. In Analytical Ultracentrifugation in Biochemistry and Polymer Science (Harding, S. E., Rowe, A. J. and Horton, J., eds), pp. 90-125, Royal Society of Chemistry, Cambridge
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 34
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects: The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins, S. J. (1986) Protein volumes and hydration effects: the calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157, 169-180
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 36
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78, 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 37
    • 37349123478 scopus 로고    scopus 로고
    • Implications of the progressive self-association of wild-type human factor H for complement regulation and disease
    • Nan, R., Gor, J. and Perkins, S. J. (2008) Implications of the progressive self-association of wild-type human factor H for complement regulation and disease. J. Mol. Biol. 375, 891-900
    • (2008) J. Mol. Biol. , vol.375 , pp. 891-900
    • Nan, R.1    Gor, J.2    Perkins, S.J.3
  • 38
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia De La Torre, J., Huertas, M. L. and Carrasco, B. (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78, 719-730 (Pubitemid 30211830)
    • (2000) Biophysical Journal , vol.78 , Issue.2 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 39
    • 69949145065 scopus 로고    scopus 로고
    • Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights
    • Perkins, S. J., Okemefuna, A. I., Nan, R., Li, K. and Bonner, A. (2009) Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights. J. R. Soc. Interface. 6 (Suppl. 5), S679-S696
    • (2009) J. R. Soc. Interface. , vol.6 , Issue.SUPPL. 5
    • Perkins, S.J.1    Okemefuna, A.I.2    Nan, R.3    Li, K.4    Bonner, A.5
  • 40
    • 0034782444 scopus 로고    scopus 로고
    • HYDROMIC: Prediction of hydrodynamic properties of rigid macromolecular structures obtained from electron microscopy images
    • Garcia de la Torre, J., Llorca, O., Carrascosa, J. L. and Valpuesta, J. M. (2001) HYDROMIC: prediction of hydrodynamic properties of rigid macromolecular structures obtained from electron microscopy images. Eur. Biophys. J. 30, 457-462
    • (2001) Eur. Biophys. J. , vol.30 , pp. 457-462
    • Garcia De La Torre, J.1    Llorca, O.2    Carrascosa, J.L.3    Valpuesta, J.M.4
  • 41
    • 33748368713 scopus 로고    scopus 로고
    • Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes
    • McKay, A. R., Ruotolo, B. T., Ilag, L. L. and Robinson, C. V. (2006) Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes. J. Am. Chem. Soc. 128, 11433-11442
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11433-11442
    • McKay, A.R.1    Ruotolo, B.T.2    Ilag, L.L.3    Robinson, C.V.4
  • 42
    • 0035476451 scopus 로고    scopus 로고
    • Thermal decomposition of a gaseous multiprotein complex studied by blackbody infrared radiative dissociation: Investigating the origin of the asymmetric dissociation behavior
    • Felitsyn, N., Kitova, E. N. and Klassen, J. S. (2001) Thermal decomposition of a gaseous multiprotein complex studied by blackbody infrared radiative dissociation: investigating the origin of the asymmetric dissociation behavior. Anal. Chem. 73, 4647-4661
    • (2001) Anal. Chem. , vol.73 , pp. 4647-4661
    • Felitsyn, N.1    Kitova, E.N.2    Klassen, J.S.3
  • 43
    • 0037420384 scopus 로고    scopus 로고
    • Origin of asymmetric charge partitioning in the dissociation of gas-phase protein homodimers
    • Jurchen, J. C. and Williams, E. R. (2003) Origin of asymmetric charge partitioning in the dissociation of gas-phase protein homodimers. J. Am. Chem. Soc. 125, 2817-2826
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2817-2826
    • Jurchen, J.C.1    Williams, E.R.2
  • 44
    • 33745192792 scopus 로고    scopus 로고
    • Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies
    • Benesch, J. L., Aquilina, J. A., Ruotolo, B. T., Sobott, F. and Robinson, C. V. (2006) Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies. Chem. Biol. 13, 597-605
    • (2006) Chem. Biol. , vol.13 , pp. 597-605
    • Benesch, J.L.1    Aquilina, J.A.2    Ruotolo, B.T.3    Sobott, F.4    Robinson, C.V.5
  • 45
    • 35648957210 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes
    • Ruotolo, B. T., Hyung, S. J., Robinson, P. M., Giles, K., Bateman, R. H. and Robinson, C. V. (2007) Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes. Angew. Chem. Int. Ed. Engl. 46, 8001-8004
    • (2007) Angew. Chem. Int. Ed. Engl. , vol.46 , pp. 8001-8004
    • Ruotolo, B.T.1    Hyung, S.J.2    Robinson, P.M.3    Giles, K.4    Bateman, R.H.5    Robinson, C.V.6
  • 46
    • 45849105951 scopus 로고    scopus 로고
    • Surface-induced dissociation shows potential to be more informative than collision-induced dissociation for structural studies of large systems
    • Wysocki, V. H., Jones, C. M., Galhena, A. S. and Blackwell, A. E. (2008) Surface-induced dissociation shows potential to be more informative than collision-induced dissociation for structural studies of large systems. J. Am. Soc. Mass Spectrom. 19, 903-913
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 903-913
    • Wysocki, V.H.1    Jones, C.M.2    Galhena, A.S.3    Blackwell, A.E.4
  • 47
    • 75349085062 scopus 로고    scopus 로고
    • Comparison of the multiple oligomeric structures observed for the Rvb1 and Rvb2 proteins. Biochem
    • Cheung, K. L., Huen, J., Houry, W. A. and Ortega, J. (2010) Comparison of the multiple oligomeric structures observed for the Rvb1 and Rvb2 proteins. Biochem. Cell Biol. 88, 77-88
    • (2010) Cell Biol. , vol.88 , pp. 77-88
    • Cheung, K.L.1    Huen, J.2    Houry, W.A.3    Ortega, J.4
  • 48
    • 73149121603 scopus 로고    scopus 로고
    • Adenosine triphosphatase pontin is overexpressed in hepatocellular carcinoma and coregulated with reptin through a new post-translational mechanism
    • Haurie, V., Menard, L., Nicou, A., Touriol, C., Metzler, P., Fernandez, J., Taras, D., Lestienne, P., Balabaud, C., Bioulac-Sage, P. et al. (2009) Adenosine triphosphatase pontin is overexpressed in hepatocellular carcinoma and coregulated with reptin through a new post-translational mechanism. Hepatology 50, 1871-1883
    • (2009) Hepatology , vol.50 , pp. 1871-1883
    • Haurie, V.1    Menard, L.2    Nicou, A.3    Touriol, C.4    Metzler, P.5    Fernandez, J.6    Taras, D.7    Lestienne, P.8    Balabaud, C.9    Bioulac-Sage, P.10
  • 49
    • 59849088152 scopus 로고    scopus 로고
    • RAD51 foci formation in response to DNA damage is modulated by TIP49
    • Gospodinov, A., Tsaneva, I. and Anachkova, B. (2009) RAD51 foci formation in response to DNA damage is modulated by TIP49. Int. J. Biochem. Cell Biol. 41, 925-933
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 925-933
    • Gospodinov, A.1    Tsaneva, I.2    Anachkova, B.3
  • 51
    • 0036889385 scopus 로고    scopus 로고
    • Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP
    • Watkins, N. J., Dickmanns, A. and Luhrmann, R. (2002) Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP. Mol. Cell. Biol. 22, 8342-8352
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8342-8352
    • Watkins, N.J.1    Dickmanns, A.2    Luhrmann, R.3
  • 53
    • 1942439646 scopus 로고    scopus 로고
    • The highly conserved and multifunctional NuA4 HAT complex
    • Doyon, Y. and Cote, J. (2004) The highly conserved and multifunctional NuA4 HAT complex. Curr. Opin. Genet. Dev. 14, 147-154
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 147-154
    • Doyon, Y.1    Cote, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.