메뉴 건너뛰기




Volumn 5, Issue 2, 2009, Pages 205-214

Identifications of SUMO-1 cDNA and its expression patterns in pacific white shrimp Litopeanaeus vannamei

Author keywords

Gene expression; Invertebrate; mRNA; RT PCR; Small ubiquitin like modifiers; Sumoylation

Indexed keywords

COMPLEMENTARY DNA; LVSUMO 1 PROTEIN; MESSENGER RNA; MUSCLE PROTEIN; PLASMID DNA; SUMO 1 PROTEIN; UNCLASSIFIED DRUG;

EID: 62649152906     PISSN: 14492288     EISSN: None     Source Type: Journal    
DOI: 10.7150/ijbs.5.205     Document Type: Article
Times cited : (8)

References (48)
  • 1
    • 55249095331 scopus 로고    scopus 로고
    • Phosphorylation of SUMO-1 Occurs in Vivo and Is Conserved through Evolution
    • Matic I, Macek B, Hilger M, Walther TC, Mann M. Phosphorylation of SUMO-1 Occurs in Vivo and Is Conserved through Evolution. J Proteome Res 2008; 7: 4050-4057
    • (2008) J Proteome Res , vol.7 , pp. 4050-4057
    • Matic, I.1    Macek, B.2    Hilger, M.3    Walther, T.C.4    Mann, M.5
  • 2
    • 1842410751 scopus 로고    scopus 로고
    • Preferential modification of nuclear proteins by a novel ubiquitin-like molecule
    • DOI 10.1074/jbc.272.22.14001
    • Kamitani T, Nguyen HP, Yeh ET. Preferential modification of nuclear proteins by a novel ubiquitin-like molecule. J Biol Chem 1997; 272: 14001-14004 (Pubitemid 27232794)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.22 , pp. 14001-14004
    • Kamitani, T.1    Nguyen, H.P.2    Yeh, E.T.H.3
  • 4
    • 0037470238 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of sumo1 and -2 conjugates is increased by stress
    • DOI 10.1074/jbc.M209694200
    • Kurepa J, Walker JM, Smalle J, Gosink MM, Davis SJ, Durham TL, Sung DY, Vierstra RD. The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress. J Biol Chem 2003; 278: 6862-6872 (Pubitemid 36800677)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 6862-6872
    • Kurepa, J.1    Walker, J.M.2    Smalle, J.3    Gosink, M.M.4    Davis, S.J.5    Durham, T.L.6    Sung, D.-Y.7    Vierstra, R.D.8
  • 5
    • 0029736651 scopus 로고    scopus 로고
    • PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • Boddy MN, Howe K, Etkin LD, Solomon E, Freemont PS. PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene 1996; 13: 971-982 (Pubitemid 26329084)
    • (1996) Oncogene , vol.13 , Issue.5 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 6
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • DOI 10.1083/jcb.135.6.1457
    • Matunis MJ, Coutavas E, Blobel G. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J Cell Biol 1996; 135: 1457-1470 (Pubitemid 26427644)
    • (1996) Journal of Cell Biology , vol.135 , Issue.6 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 7
  • 8
    • 0030249870 scopus 로고    scopus 로고
    • UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins
    • DOI 10.1006/geno.1996.0462
    • Shen Z, Pardington-Purtymun PE, Comeaux JC, Moyzis RK, Chen DJ. UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins. Genomics 1996; 36: 271-279 (Pubitemid 26307489)
    • (1996) Genomics , vol.36 , Issue.2 , pp. 271-279
    • Shen, Z.1    Pardington-Purtymun, P.E.2    Comeaux, J.C.3    Moyzis, R.K.4    Chen, D.J.5
  • 9
    • 0032567759 scopus 로고    scopus 로고
    • Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association
    • DOI 10.1083/jcb.140.2.259
    • Mahajan R, Gerace L, Melchior F. Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. J Cell Biol 1998; 140: 259-270 (Pubitemid 28078390)
    • (1998) Journal of Cell Biology , vol.140 , Issue.2 , pp. 259-270
    • Mahajan, R.1    Gerace, L.2    Melchior, F.3
  • 10
    • 0028934834 scopus 로고
    • Human Rangtpase-Activating Protein Rangap1 Is a Homolog of Yeast Rna1p Involved in Messenger-Rna Processing and Transport
    • Bischoff FR, Krebber H, Kempf T, Hermes I, Ponstingl H. Human Rangtpase-Activating Protein Rangap1 Is a Homolog of Yeast Rna1p Involved in Messenger-Rna Processing and Transport. Proc Natl Acad Sci U S A 1995; 92: 1749-1753
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1749-1753
    • Bischoff, F.R.1    Krebber, H.2    Kempf, T.3    Hermes, I.4    Ponstingl, H.5
  • 11
    • 0035947677 scopus 로고    scopus 로고
    • SUMO-1 Modification Regulates the DNA Binding Activity of Heat Shock Transcription Factor 2, a Promyelocytic Leukemia Nuclear Body Associated Transcription Factor
    • DOI 10.1074/jbc.M008066200
    • Goodson ML, Hong Y, Rogers R, Matunis MJ, Park-Sarge OK, Sarge KD. Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor. J Biol Chem 2001; 276: 18513-18518 (Pubitemid 37411430)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.21 , pp. 18513-18518
    • Goodson, M.L.1    Hong, Y.2    Rogers, R.3    Matunis, M.J.4    Park-Sargell, O.-K.5    Sarge, K.D.6
  • 14
    • 0033571214 scopus 로고    scopus 로고
    • SUMO-1 modification activates the transcriptional response of p53
    • DOI 10.1093/emboj/18.22.6455
    • Rodriguez MS, Desterro JM, Lain S, Midgley CA, Lane DP, Hay RT. SUMO-1 modification activates the transcriptional response of p53. Embo J 1999; 18: 6455-6461 (Pubitemid 29533249)
    • (1999) EMBO Journal , vol.18 , Issue.22 , pp. 6455-6461
    • Rodriguez, M.S.1    Desterro, J.M.P.2    Lain, S.3    Midgley, C.A.4    Lane, D.P.5    Hay, R.T.6
  • 15
    • 3142544806 scopus 로고    scopus 로고
    • Dual role of sumoylation in the nuclear localization and transcriptional activation of NFAT1
    • DOI 10.1074/jbc.M403153200
    • Terui Y, Saad N, Jia S, McKeon F, Yuan J. Dual role of sumoylation in the nuclear localization and transcriptional activation of NFAT1. J Biol Chem 2004; 279: 28257-28265 (Pubitemid 38900103)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28257-28265
    • Teruit, Y.1    Saad, N.2    Jia, S.3    McKeon, F.4    Yuan, J.5
  • 16
    • 0041669469 scopus 로고    scopus 로고
    • Dynamic interplay of the SUMO and ERK pathways in regulating Elk-1 transcriptional activity
    • DOI 10.1016/S1097-2765(03)00265-X
    • Yang SH, Jaffray E, Hay RT, Sharrocks AD. Dynamic interplay of the SUMO and ERK pathways in regulating Elk-1 transcriptional activity. Mol Cell 2003; 12: 63-74. (Pubitemid 36945037)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 63-74
    • Yang, S.-H.1    Jaffray, E.2    Hay, R.T.3    Sharrocks, A.D.4
  • 17
    • 1342271367 scopus 로고    scopus 로고
    • SUMO and transcriptional repression: Dynamic interactions between the MAP kinase and SUMO pathways
    • Yang SH, Jaffray E, Senthinathan B, Hay RT, Sharrocks AD. SUMO and transcriptional repression: dynamic interactions between the MAP kinase and SUMO pathways. Cell Cycle 2003; 2: 528-530
    • (2003) Cell Cycle , vol.2 , pp. 528-530
    • Yang, S.H.1    Jaffray, E.2    Senthinathan, B.3    Hay, R.T.4    Sharrocks, A.D.5
  • 20
    • 2542487192 scopus 로고    scopus 로고
    • Differential effect of Small Ubiquitin-Like Modifier (SUMO)-ylation of the androgen receptor in the control of cooperativity on selective versus canonical response elements
    • DOI 10.1210/me.2003-0313
    • Callewaert L, Verrijdt G, Haelens A, Claessens F. Differential effect of small ubiquitin-like modifier (SUMO)-ylation of the androgen receptor in the control of cooperativity on selective versus canonical response elements. Mol Endocrinol 2004; 18: 1438-1449 (Pubitemid 38692181)
    • (2004) Molecular Endocrinology , vol.18 , Issue.6 , pp. 1438-1449
    • Callewaert, L.1    Verrijdt, G.2    Haelens, A.3    Claessens, F.4
  • 21
    • 0037088588 scopus 로고    scopus 로고
    • Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity
    • DOI 10.1074/jbc.M110453200
    • Bies J, Markus J, Wolff L. Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity. J Biol Chem 2002; 277: 8999-9009. (Pubitemid 34952972)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.11 , pp. 8999-9009
    • Bies, J.1    Markus, J.2    Wolff, L.3
  • 22
    • 0037163074 scopus 로고    scopus 로고
    • Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo
    • Eloranta JJ, Hurst HC. Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo. J Biol Chem 2002; 277: 30798-30804
    • (2002) J Biol Chem , vol.277 , pp. 30798-30804
    • Eloranta, J.J.1    Hurst, H.C.2
  • 24
    • 2542489214 scopus 로고    scopus 로고
    • Regulation of Smad4 sumoylation and transforming growth factor-beta signaling by protein inhibitor of activated STAT1
    • DOI 10.1074/jbc.M401554200
    • Liang M, Melchior F, Feng XH, Lin X. Regulation of Smad4 sumoylation and transforming growth factor-beta signaling by protein inhibitor of activated STAT1. J Biol Chem 2004; 279: 22857-22865 (Pubitemid 38685586)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 22857-22865
    • Liang, M.1    Melchior, F.2    Feng, X.-H.3    Lin, X.4
  • 25
    • 34250352765 scopus 로고    scopus 로고
    • Transforming growth factor-beta-independent regulation of myogenesis by SnoN sumoylation
    • DOI 10.1074/jbc.M610206200
    • Wrighton KH, Liang M, Bryan B, Luo K, Liu M, Feng XH, Lin X. Transforming growth factor-beta-independent regulation of myogenesis by SnoN sumoylation. J Biol Chem 2007; 282: 6517-6524 (Pubitemid 47100903)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6517-6524
    • Wrighton, K.H.1    Liang, M.2    Bryan, B.3    Luo, K.4    Liu, M.5    Feng, X.-H.6    Lin, X.7
  • 26
    • 0033977682 scopus 로고    scopus 로고
    • Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies
    • DOI 10.1128/MCB.20.3.1072-1082.2000
    • Lehembre F, Badenhorst P, Muller S, Travers A, Schweisguth F, Dejean A. Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies. Mol Cell Biol 2000; 20: 1072-1082 (Pubitemid 30044244)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.3 , pp. 1072-1082
    • Lehembre, F.1    Badenhorst, P.2    Muller, S.3    Travers, A.4    Schweisguth, F.5    Dejean, A.6
  • 27
    • 49449086759 scopus 로고    scopus 로고
    • Analysis of expressed sequenced tags from abdominal muscle cDNA library of the pacific white shrimp Litopenaeus vannamei
    • Cesar JRO, Zhao B, Yang J. Analysis of expressed sequenced tags from abdominal muscle cDNA library of the pacific white shrimp Litopenaeus vannamei. Animal 2008; 2:1377-1383
    • (2008) Animal , vol.2 , pp. 1377-1383
    • Cesar, J.R.O.1    Zhao, B.2    Yang, J.3
  • 28
    • 33947708813 scopus 로고    scopus 로고
    • Expression patterns of ubiquitin, heat shock protein 70, alpha-actin and beta-actin over the molt cycle in the abdominal muscle of marine shrimp Litopenaeus vannamei
    • DOI 10.1002/mrd.20605
    • Cesar JRO, Yang J. Expression patterns of ubiquitin, heat shock protein 70, alpha-actin and beta-actin over the molt cycle in the abdominal muscle of marine shrimp Litopenaeus vannamei. Mol Reprod Dev 2007; 74: 554-559 (Pubitemid 46493743)
    • (2007) Molecular Reproduction and Development , vol.74 , Issue.5 , pp. 554-559
    • Cesar, J.R.O.1    Yang, J.2
  • 29
    • 23244457177 scopus 로고    scopus 로고
    • Effects of bovine somatotropin on beta-casein mRNA levels in mammary tissue of lactating cows
    • Yang J, Zhao B, Baracos VE, Kennelly JJ. Effects of bovine somatotropin on beta-casein mRNA levels in mammary tissue of lactating cows. J Dairy Sci. 2005; 88: 2806-2812 (Pubitemid 41096443)
    • (2005) Journal of Dairy Science , vol.88 , Issue.8 , pp. 2806-2812
    • Yang, J.1    Zhao, B.2    Baracos, V.E.3    Kennelly, J.J.4
  • 30
    • 0002743430 scopus 로고
    • Development of a Biotinylated DNA Probe for Detection and Identification of Infectious Hematopoietic Necrosis Virus
    • Deering RE, Arakawa CK, Oshima KH, Ohara PJ, Landolt ML, Winton JR. Development of a Biotinylated DNA Probe for Detection and Identification of Infectious Hematopoietic Necrosis Virus. Dis Aquat Org 1991; 11: 57-65.
    • (1991) Dis Aquat Org , vol.11 , pp. 57-65
    • Deering, R.E.1    Arakawa, C.K.2    Oshima, K.H.3    Ohara, P.J.4    Landolt, M.L.5    Winton, J.R.6
  • 32
    • 0030826334 scopus 로고    scopus 로고
    • Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p
    • DOI 10.1074/jbc.272.43.26799
    • Johnson ES, Blobel G. Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p. J Biol Chem 1997; 272: 26799-26802 (Pubitemid 27452622)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.43 , pp. 26799-26802
    • Johnson, E.S.1    Blobel, G.2
  • 33
    • 0037151769 scopus 로고    scopus 로고
    • Molecular features of human ubiquitin-like SUMO genes and their encoded proteins
    • Su HL, Li SS. Molecular features of human ubiquitin-like SUMO genes and their encoded proteins. Gene 2002; 296: 65-73.
    • (2002) Gene , vol.296 , pp. 65-73
    • Su, H.L.1    Li, S.S.2
  • 35
    • 0031913121 scopus 로고    scopus 로고
    • The ubiquitin-homology gene PIC1: Characterization of mouse (Pic1) and human (UBL1) genes and pseudogenes
    • DOI 10.1006/geno.1997.5091
    • Howe K, Williamson J, Boddy N, Sheer D, Freemont P, Solomon E. The ubiquitin-homology gene PIC1: characterization of mouse (Pic1) and human (UBL1) genes and pseudogenes. Genomics 1998; 47: 92-100. (Pubitemid 28080085)
    • (1998) Genomics , vol.47 , Issue.1 , pp. 92-100
    • Howe, K.1    Williamson, J.2    Boddy, N.3    Sheer, D.4    Freemont, P.5    Solomon, E.6
  • 36
    • 0032080337 scopus 로고    scopus 로고
    • Characterization of a second member of the sentrin family of ubiquitin- Like proteins
    • DOI 10.1074/jbc.273.18.11349
    • Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ETH. Characterization of a second member of the sentrin family of ubiquitin-like proteins. J Biol Chem 1998; 273: 11349-11353 (Pubitemid 28204990)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 11349-11353
    • Kamitani, T.1    Kito, K.2    Nguyen, H.P.3    Fukuda-Kamitani, T.4    Yeh, E.T.H.5
  • 37
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • DOI 10.1074/jbc.275.9.6252
    • Saitoh H, Hinchey J. Functional heterogeneity of small ubiquitin- related protein modifiers SUMO-1 versus SUMO-2/3. J Biol Chem 2000; 275: 6252-6258 (Pubitemid 30129915)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.9 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 38
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay RT. SUMO: A history of modification. Molecular Cell 2005; 18: 1-12.
    • (2005) Molecular Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 39
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 Conjugation in Vivo Requires Both a Consensus Modification Motif and Nuclear Targeting
    • DOI 10.1074/jbc.M009476200
    • Rodriguez MS, Dargemont C, Hay RT. SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J Biol Chem 2001; 276: 12654-12659 (Pubitemid 37385176)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.16 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 41
    • 33750460279 scopus 로고    scopus 로고
    • Muscle development in dendro-branchiate shrimp, with comparison with Artemia
    • Kiernan DA, Hertzler PL. Muscle development in dendro-branchiate shrimp, with comparison with Artemia. Evol & Dev 2006; 8:537-549.
    • (2006) Evol & Dev , vol.8 , pp. 537-549
    • Kiernan, D.A.1    Hertzler, P.L.2
  • 42
    • 33750472584 scopus 로고
    • The abdominal muscular systems of the zoea and mysis stages of shrimp (Crangon vulgaris Fabr) and their bearing on phylogeny
    • Daniel RJ. The abdominal muscular systems of the zoea and mysis stages of shrimp (Crangon vulgaris Fabr) and their bearing on phylogeny. Proc Trans Liverpool Biol Soc 1930; 44: 95-109.
    • (1930) Proc Trans Liverpool Biol Soc , vol.44 , pp. 95-109
    • Daniel, R.J.1
  • 43
    • 0013355273 scopus 로고
    • Morphology of the white shrimp Penaeus setiferus
    • United states Department of the Interior, Fish and Wildlife Service
    • Young JH. Morphology of the white shrimp Penaeus setiferus. United states Department of the Interior, Fish and Wildlife Service. Fishery Bull. 1959; 59: 1-169
    • (1959) Fishery Bull , vol.59 , pp. 1-169
    • Young, J.H.1
  • 44
    • 0024357562 scopus 로고
    • The ski oncogene induces muscle differentiation in quail embryo cells
    • DOI 10.1016/0092-8674(89)90291-2
    • Colmenares C, Stavnezer E. The ski oncogene induces muscle differentiation in quail embryo cells. Cell 1989; 59: 293-303. (Pubitemid 19264375)
    • (1989) Cell , vol.59 , Issue.2 , pp. 293-303
    • Colmenares, C.1    Stavnezer, E.2
  • 45
    • 0027395955 scopus 로고
    • Sequence and biological activity of chicken snoN cDNA clones
    • Boyer PL, Colmenares C, Stavnezer E, Hughes SH. Sequence and biological activity of chicken snoN cDNA clones. Oncogene 1993; 8: 457-466 (Pubitemid 23073762)
    • (1993) Oncogene , vol.8 , Issue.2 , pp. 457-466
    • Boyer, P.L.1    Colmenares, C.2    Stavnezer, E.3    Hughes, S.H.4
  • 46
    • 0021780518 scopus 로고
    • The role of calcium-dependent proteinase in molt-induced claw muscle atrophy
    • Mykles DL, Skinner DM. The role of calcium-dependent proteinase in molt-induced claw muscle atrophy. Prog Clin Biol Res 1985; 180: 141-150
    • (1985) Prog Clin Biol Res , vol.180 , pp. 141-150
    • Mykles, D.L.1    Skinner, D.M.2
  • 47
    • 0027035247 scopus 로고
    • Regulation of muscle gene expression in Crustacea over the moult cycle
    • el Haj AJ, Harrison P, Whiteley NM. Regulation of muscle gene expression in Crustacea over the moult cycle. Symp Soc Exp Biol 1992; 46: 151-165
    • (1992) Symp Soc Exp Biol , vol.46 , pp. 151-165
    • El Haj, A.J.1    Harrison, P.2    Whiteley, N.M.3
  • 48
    • 33750513663 scopus 로고    scopus 로고
    • Morphological and biochemical changes in the muscle of the marine shrimp Litopenaeus vannamei during the molt cycle
    • DOI 10.1016/j.aquaculture.2006.08.003, PII S004484860600603X
    • Cesar JRO, Zhao B, Malcha S, Ako H, Yang J. Morphological and biochemical changes in the muscle of the marine shrimp Litopenaeus vannamei during the molt cycle. Aquaculture, 2005; 261: 688-694 (Pubitemid 44666930)
    • (2006) Aquaculture , vol.261 , Issue.2 , pp. 688-694
    • De Oliveira Cesar, J.R.1    Zhao, B.2    Malecha, S.3    Ako, H.4    Yang, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.