메뉴 건너뛰기




Volumn 468, Issue 1-2, 2010, Pages 48-57

Plasmodium falciparum Tudor Staphylococcal Nuclease interacting proteins suggest its role in nuclear as well as splicing processes

Author keywords

Interaction; Malaria; Plasmodium falciparum; Tudor SN

Indexed keywords

DNA BINDING PROTEIN; PROTOZOAL PROTEIN; MICROCOCCAL NUCLEASE; PEPTIDE; PROTEIN BINDING;

EID: 77957004259     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2010.08.004     Document Type: Article
Times cited : (17)

References (44)
  • 1
    • 33745685682 scopus 로고    scopus 로고
    • Potential protein partners for the human TIMAP revealed by bacterial two-hybrid screening
    • Adyshev D.M., Kolosova I.A., Verin A.D. Potential protein partners for the human TIMAP revealed by bacterial two-hybrid screening. Mol. Biol. Rep. 2006, 33:83-89.
    • (2006) Mol. Biol. Rep. , vol.33 , pp. 83-89
    • Adyshev, D.M.1    Kolosova, I.A.2    Verin, A.D.3
  • 2
    • 0034880251 scopus 로고    scopus 로고
    • Tudor protein is essential for the localization of mitochondrial RNAs in polar granules of Drosophila embryos
    • Amikura R., Hanyu K., Kashikawa M., Kobayashi S. Tudor protein is essential for the localization of mitochondrial RNAs in polar granules of Drosophila embryos. Mech. Dev. 2001, 107:97-104.
    • (2001) Mech. Dev. , vol.107 , pp. 97-104
    • Amikura, R.1    Hanyu, K.2    Kashikawa, M.3    Kobayashi, S.4
  • 3
    • 28044457006 scopus 로고    scopus 로고
    • High-efficiency transformation of Plasmodium falciparum by the lepidopteran transposable element piggy-Bac
    • Balu B., Shoue D.A., Fraser M.J., Adams J.H. High-efficiency transformation of Plasmodium falciparum by the lepidopteran transposable element piggy-Bac. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:16391-16396.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16391-16396
    • Balu, B.1    Shoue, D.A.2    Fraser, M.J.3    Adams, J.H.4
  • 4
    • 76749100261 scopus 로고    scopus 로고
    • In silico and biological survey of transcription-associated proteins implicated in the transcriptional machinery during the erythrocytic development of Plasmodium falciparum
    • Bischoff E., Vaquero C. In silico and biological survey of transcription-associated proteins implicated in the transcriptional machinery during the erythrocytic development of Plasmodium falciparum. BMC Genomics 2010, 11:34-38.
    • (2010) BMC Genomics , vol.11 , pp. 34-38
    • Bischoff, E.1    Vaquero, C.2
  • 5
    • 0242683460 scopus 로고    scopus 로고
    • Essential role of SMN in spliceosomal U snRNP assembly: implications for spinal muscular atrophy
    • Buhler D., Raker V., Luhrmann R., Fischer U. Essential role of SMN in spliceosomal U snRNP assembly: implications for spinal muscular atrophy. Hum. Mol. Genet. 1999, 8:2351-2357.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2351-2357
    • Buhler, D.1    Raker, V.2    Luhrmann, R.3    Fischer, U.4
  • 6
    • 0031027360 scopus 로고    scopus 로고
    • The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development
    • Callebaut I., Mornon J.P. The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development. Biochem. J. 1997, 321:125-132.
    • (1997) Biochem. J. , vol.321 , pp. 125-132
    • Callebaut, I.1    Mornon, J.P.2
  • 8
    • 0030670094 scopus 로고    scopus 로고
    • A CTD function linking transcription to splicing
    • Corden J.L., Patturajan N. A CTD function linking transcription to splicing. Trends Biochem. Sci. 1997, 22:413-416.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 413-416
    • Corden, J.L.1    Patturajan, N.2
  • 9
    • 4444339460 scopus 로고    scopus 로고
    • Comparative genomics of transcriptional control in human malaria parasite Plasmodium falciparum
    • Coulson R.M.R., Hall N., Ouzounis C.A. Comparative genomics of transcriptional control in human malaria parasite Plasmodium falciparum. Genome Res. 2004, 14:1548-1554.
    • (2004) Genome Res. , vol.14 , pp. 1548-1554
    • Coulson, R.M.R.1    Hall, N.2    Ouzounis, C.A.3
  • 10
    • 77956802116 scopus 로고    scopus 로고
    • Chromatin-mediated epigenetic regulation in the malaria parasite Plasmodium falciparum
    • Cui L., Miao J. Chromatin-mediated epigenetic regulation in the malaria parasite Plasmodium falciparum. Euk Cell. PMID: 20453074 2010.
    • (2010) Euk Cell. PMID: 20453074
    • Cui, L.1    Miao, J.2
  • 11
    • 0029786902 scopus 로고    scopus 로고
    • The EVES motif mediates both intermolecular and intramolecular regulation of c-Myb
    • Dash A.B., Orrico F.C., Ness S.A. The EVES motif mediates both intermolecular and intramolecular regulation of c-Myb. Genes Dev. 1996, 10:1858-1869.
    • (1996) Genes Dev. , vol.10 , pp. 1858-1869
    • Dash, A.B.1    Orrico, F.C.2    Ness, S.A.3
  • 12
    • 62649142373 scopus 로고    scopus 로고
    • Structure and ligand binding of the extended Tudor domain of D. melanogaster Tudor-SN
    • Friberg A., Corsini L., Mourão A., Sattler M. Structure and ligand binding of the extended Tudor domain of D. melanogaster Tudor-SN. J. Mol. Biol. 2009, 387:921-934.
    • (2009) J. Mol. Biol. , vol.387 , pp. 921-934
    • Friberg, A.1    Corsini, L.2    Mourão, A.3    Sattler, M.4
  • 13
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?
    • Gill G. SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?. Genes Dev. 2004, 18:2046-2059.
    • (2004) Genes Dev. , vol.18 , pp. 2046-2059
    • Gill, G.1
  • 15
    • 39449094608 scopus 로고    scopus 로고
    • Tudor domain proteins in protozoan parasites and characterization of Plasmodium falciparum Tudor Staphylococcal Nuclease
    • Hossain M.J., Korde R., Singh S., Mohmmed A., Dasaradhi P.V.N., Chauhan V.S., Malhotra P. Tudor domain proteins in protozoan parasites and characterization of Plasmodium falciparum Tudor Staphylococcal Nuclease. Int. J. Parasitol. 2008, 38:513-526.
    • (2008) Int. J. Parasitol. , vol.38 , pp. 513-526
    • Hossain, M.J.1    Korde, R.2    Singh, S.3    Mohmmed, A.4    Dasaradhi, P.V.N.5    Chauhan, V.S.6    Malhotra, P.7
  • 17
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley L.A., MacCallum R.M., Sternberg M.J.E. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 2000, 299:499-520.
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.E.3
  • 19
    • 0026552961 scopus 로고
    • Transcription mapping of a 100kb locus of Plasmodium falciparum identifies an intergenic region in which transcription terminates and reinitiates
    • Lanzer M., De Bruin D., Ravetch J.V. Transcription mapping of a 100kb locus of Plasmodium falciparum identifies an intergenic region in which transcription terminates and reinitiates. EMBO J. 1992, 11:1949-1955.
    • (1992) EMBO J. , vol.11 , pp. 1949-1955
    • Lanzer, M.1    De Bruin, D.2    Ravetch, J.V.3
  • 21
    • 46349107531 scopus 로고    scopus 로고
    • Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing
    • Li C.L., Yang W.Z., Chen Y.P., Yuan H.S. Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing. Nucleic Acids Res. 2008, 36:3579-3589.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3579-3589
    • Li, C.L.1    Yang, W.Z.2    Chen, Y.P.3    Yuan, H.S.4
  • 22
    • 77952546251 scopus 로고    scopus 로고
    • The AtTudor2, a protein with SN-Tudor domains, is involved in control of seed germination in Arabidopsis
    • Liu S., Jia J., Gao Y., Zhang B., Han Y. The AtTudor2, a protein with SN-Tudor domains, is involved in control of seed germination in Arabidopsis. Planta 2010, 232:197-207.
    • (2010) Planta , vol.232 , pp. 197-207
    • Liu, S.1    Jia, J.2    Gao, Y.3    Zhang, B.4    Han, Y.5
  • 23
    • 29744470060 scopus 로고    scopus 로고
    • Polycystin-1, STAT6, and P100 function in a pathway that transduces ciliary mechanosensation and is activated in polycystic kidney disease
    • Low S.H., Vasanth S., Larson C.H., Mukherjee S., Sharma N., Kinter M.T., Kane M.E., Obara T., Weimbs T. Polycystin-1, STAT6, and P100 function in a pathway that transduces ciliary mechanosensation and is activated in polycystic kidney disease. Dev. Cell 2006, 10:57-69.
    • (2006) Dev. Cell , vol.10 , pp. 57-69
    • Low, S.H.1    Vasanth, S.2    Larson, C.H.3    Mukherjee, S.4    Sharma, N.5    Kinter, M.T.6    Kane, M.E.7    Obara, T.8    Weimbs, T.9
  • 24
    • 33644656442 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum histones: organization, expression and acetylation
    • Miao J., Fan Q., Cui L., Li J., Cui L. The malaria parasite Plasmodium falciparum histones: organization, expression and acetylation. Gene 2006, 369:53-65.
    • (2006) Gene , vol.369 , pp. 53-65
    • Miao, J.1    Fan, Q.2    Cui, L.3    Li, J.4    Cui, L.5
  • 25
    • 11844252046 scopus 로고    scopus 로고
    • The C-terminal domain of RNA polymerase II functions as a phosphorylation dependent splicing activator in a heterologous protein
    • Millhouse S., Manley J.L. The C-terminal domain of RNA polymerase II functions as a phosphorylation dependent splicing activator in a heterologous protein. Mol. Cell. Biol. 2005, 25:533-544.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 533-544
    • Millhouse, S.1    Manley, J.L.2
  • 26
    • 32044445075 scopus 로고    scopus 로고
    • Evidence that Spt2/Sin1, an HMG-like factor plays roles in transcription elongation, chromatin structure and genome stability in Saccharomyces cerevisiae
    • Nourani A., Robert F., Winston F. Evidence that Spt2/Sin1, an HMG-like factor plays roles in transcription elongation, chromatin structure and genome stability in Saccharomyces cerevisiae. Mol. Cell. Biol. 2006, 26:1496-1509.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1496-1509
    • Nourani, A.1    Robert, F.2    Winston, F.3
  • 27
    • 0042835769 scopus 로고    scopus 로고
    • Tudor and nuclease-like domains containing protein p100 function as coactivators for signal transducer and activator of transcription 5
    • Paukku K., Yang J., Silvennoinen O. Tudor and nuclease-like domains containing protein p100 function as coactivators for signal transducer and activator of transcription 5. Mol. Endocrinol. 2003, 17:1805-1814.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1805-1814
    • Paukku, K.1    Yang, J.2    Silvennoinen, O.3
  • 29
    • 0028949730 scopus 로고
    • The putative Drosophila NMDARA1 gene is located on the second chromosome and is ubiquitously expressed in embryogenesis
    • Pellicena-Palle A., Salz H.K. The putative Drosophila NMDARA1 gene is located on the second chromosome and is ubiquitously expressed in embryogenesis. Biochim. Biophys. Acta 1995, 1261:301-303.
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 301-303
    • Pellicena-Palle, A.1    Salz, H.K.2
  • 31
    • 10044233755 scopus 로고    scopus 로고
    • Thermoplasma acidophilum TAA43 is an archaeal member of the eukaryotic meiotic branch of AAA ATPases
    • Santos L., Frickey T., Peters J., Baumeister W., Lupas A., Zwickl P. Thermoplasma acidophilum TAA43 is an archaeal member of the eukaryotic meiotic branch of AAA ATPases. Biol. Chem. 2004, 385:1105-1111.
    • (2004) Biol. Chem. , vol.385 , pp. 1105-1111
    • Santos, L.1    Frickey, T.2    Peters, J.3    Baumeister, W.4    Lupas, A.5    Zwickl, P.6
  • 34
    • 0034657917 scopus 로고    scopus 로고
    • Modulation of STAT signaling by STAT interacting proteins
    • Shuai K. Modulation of STAT signaling by STAT interacting proteins. Oncogene 2000, 19:2638-2644.
    • (2000) Oncogene , vol.19 , pp. 2638-2644
    • Shuai, K.1
  • 35
    • 44649147680 scopus 로고    scopus 로고
    • Transient silencing of Plasmodium falciparum Tudor Staphylococcal Nuclease suggests an essential role for the protein
    • Sunil S., Hossain M.J., Ramasamy G., Malhotra P. Transient silencing of Plasmodium falciparum Tudor Staphylococcal Nuclease suggests an essential role for the protein. Biochem. Biophys. Res. Commun. 2008, 2008:373-378.
    • (2008) Biochem. Biophys. Res. Commun. , vol.2008 , pp. 373-378
    • Sunil, S.1    Hossain, M.J.2    Ramasamy, G.3    Malhotra, P.4
  • 36
    • 27744568481 scopus 로고    scopus 로고
    • The Plasmodium protein network diverges from those of other eukaryotes
    • Suthram S., Sittler T., Ideker T. The Plasmodium protein network diverges from those of other eukaryotes. Nature 2005, 438:108-112.
    • (2005) Nature , vol.438 , pp. 108-112
    • Suthram, S.1    Sittler, T.2    Ideker, T.3
  • 37
    • 0029131021 scopus 로고
    • The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE
    • Tong X., Drapkin R., Yalamanchili R., Mosialos G., Kieff E. The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE. Mol. Cell. Biol. 1995, 15:4735-4744.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4735-4744
    • Tong, X.1    Drapkin, R.2    Yalamanchili, R.3    Mosialos, G.4    Kieff, E.5
  • 38
    • 0017311840 scopus 로고
    • Human malaria parasite in continuous culture
    • Trager W., Jensen J.B. Human malaria parasite in continuous culture. Science 1976, 193:673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 39
    • 35148895851 scopus 로고    scopus 로고
    • SND1, a component of RNA-induced silencing complex, is up-regulated in human colon cancers and implicated in early stage colon carcinogenesis
    • Tsuchiya N., Ochiai M., Nakashima K., Ubagai T., Sugimura T., Nakagama H. SND1, a component of RNA-induced silencing complex, is up-regulated in human colon cancers and implicated in early stage colon carcinogenesis. Cancer Res. 2007, 67:9568-9576.
    • (2007) Cancer Res. , vol.67 , pp. 9568-9576
    • Tsuchiya, N.1    Ochiai, M.2    Nakashima, K.3    Ubagai, T.4    Sugimura, T.5    Nakagama, H.6
  • 40
    • 17644374227 scopus 로고    scopus 로고
    • The transcriptional co-activator protein p100 recruits histone acetyltransferase activity to STAT6 and mediates interaction between the CREB-binding protein and STAT6
    • Valineva T., Yang J., Palovuori R., Silvennoinen O. The transcriptional co-activator protein p100 recruits histone acetyltransferase activity to STAT6 and mediates interaction between the CREB-binding protein and STAT6. J. Biol. Chem. 2005, 280:14989-14996.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14989-14996
    • Valineva, T.1    Yang, J.2    Palovuori, R.3    Silvennoinen, O.4
  • 41
    • 33748556882 scopus 로고    scopus 로고
    • Characterization of RNA helicase A as a component of STAT6 enhancement
    • Valineva T., Yang J., Silvennoinnen Characterization of RNA helicase A as a component of STAT6 enhancement. Nucleic Acid Res. 2006, 34:3938-3946.
    • (2006) Nucleic Acid Res. , vol.34 , pp. 3938-3946
    • Valineva, T.1    Yang, J.2    Silvennoinnen3
  • 43
    • 34547829272 scopus 로고    scopus 로고
    • Transcriptional co-activator protein p100 interacts with snRNP proteins and facilitates the assembly of the spliceosome
    • Yang J., Välineva T., Hong J., Bu T., Yao Z., Jensen O.N., Frilander M.J., Silvennoinen O. Transcriptional co-activator protein p100 interacts with snRNP proteins and facilitates the assembly of the spliceosome. Nucleic Acids Res. 2007, 35:4485-4494.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4485-4494
    • Yang, J.1    Välineva, T.2    Hong, J.3    Bu, T.4    Yao, Z.5    Jensen, O.N.6    Frilander, M.J.7    Silvennoinen, O.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.