메뉴 건너뛰기




Volumn 34, Issue 6, 1997, Pages 897-911

Cloning and characterization of the calreticulin gene from Ricinus communis L.

Author keywords

Calreticulin; Gene characterization; Ricinus communis L.

Indexed keywords

CALCIUM; CALCIUM BINDING PROTEIN; CALRETICULIN; COMPLEMENTARY DNA; MESSENGER RNA; PLANT RNA; RECOMBINANT PROTEIN; RIBONUCLEOPROTEIN;

EID: 0031214672     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005822327479     Document Type: Article
Times cited : (58)

References (57)
  • 2
    • 0029564658 scopus 로고
    • Interaction of calreticulin with protein disulfide isomerase
    • Baksh S, Burns K, Andrin C, Michalak M: Interaction of calreticulin with protein disulfide isomerase. J Biol Chem 270: 31338-31344 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 31338-31344
    • Baksh, S.1    Burns, K.2    Andrin, C.3    Michalak, M.4
  • 3
    • 0026930761 scopus 로고
    • Intracellular trafficking of secretory proteins
    • Bednarek SY, Raikhel N: Intracellular trafficking of secretory proteins. Plant Mol Biol 20: 133-150 (1992).
    • (1992) Plant Mol Biol , vol.20 , pp. 133-150
    • Bednarek, S.Y.1    Raikhel, N.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72: 248-254 (1976).
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0027530856 scopus 로고
    • Interactions of calreticulin with proteins of the endoplasmic and sarcoplasmic reticulum membranes
    • Burns K, Michalak M: Interactions of calreticulin with proteins of the endoplasmic and sarcoplasmic reticulum membranes. FEBS Lett 318: 181-185 (1993).
    • (1993) FEBS Lett , vol.318 , pp. 181-185
    • Burns, K.1    Michalak, M.2
  • 10
    • 0023605130 scopus 로고
    • Mapping of gene transcripts by nuclease protection assays and cDNA primer extension
    • Calzone FJ, Britten RJ, Davidson EH: Mapping of gene transcripts by nuclease protection assays and cDNA primer extension. Meth Enzymol 152: 611-632 (1987).
    • (1987) Meth Enzymol , vol.152 , pp. 611-632
    • Calzone, F.J.1    Britten, R.J.2    Davidson, E.H.3
  • 11
    • 0020643575 scopus 로고
    • 2+-binding proteins, calsequestrin, calmodulin, troponinC, and S-100, with the cationic carbocyanine dye 'stains all'
    • 2+-binding proteins, calsequestrin, calmodulin, troponinC, and S-100, with the cationic carbocyanine dye 'stains all'. J Biol Chem 258: 11267-11273 (1983).
    • (1983) J Biol Chem , vol.258 , pp. 11267-11273
    • Campbell, K.P.1    MacLennan, D.H.2    Jorgensen, A.O.3
  • 12
    • 0003024799 scopus 로고
    • 2+-ATPase of 120 kilodaltons on the endoplasmic reticulum from carrot (Daucus carota) cells: Properties of the phosphorylated intermediate
    • 2+-ATPase of 120 kilodaltons on the endoplasmic reticulum from carrot (Daucus carota) cells: properties of the phosphorylated intermediate. Plant Physiol 102: 651-661 (1993).
    • (1993) Plant Physiol , vol.102 , pp. 651-661
    • Chen, F.H.1    Ratterman, D.M.2    Sze, H.3
  • 13
    • 0028450064 scopus 로고
    • Identification and characterization of cDNA clones encoding plant calreticulin in barley
    • Chen F, Hayes PM, Mulrooney DM, Pan A: Identification and characterization of cDNA clones encoding plant calreticulin in barley. Plant Cell 6: 835-843 (1994).
    • (1994) Plant Cell , vol.6 , pp. 835-843
    • Chen, F.1    Hayes, P.M.2    Mulrooney, D.M.3    Pan, A.4
  • 14
    • 0030042362 scopus 로고    scopus 로고
    • Molecular characterization of plant endoplasmic reticulum: Identification of protein disulfide isomerase as the major reticuloplasmin
    • Coughlan SJ, Hastings C, Winfrey Jr RJ: Molecular characterization of plant endoplasmic reticulum: identification of protein disulfide isomerase as the major reticuloplasmin. Eur J Biochem 275: 215-224 (1996).
    • (1996) Eur J Biochem , vol.275 , pp. 215-224
    • Coughlan, S.J.1    Hastings, C.2    Winfrey Jr., R.J.3
  • 19
    • 0024819297 scopus 로고
    • Molecular cloning of the high affinity calcium binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
    • Fliegel L, Burns K, MacLennan DH, Reithmeier RAF, Maichalak M: Molecular cloning of the high affinity calcium binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J Biol Chem 264: 21522-21528 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 21522-21528
    • Fliegel, L.1    Burns, K.2    MacLennan, D.H.3    Reithmeier, R.A.F.4    Maichalak, M.5
  • 20
    • 0026040155 scopus 로고
    • Evidence for complex formation between rabbit lung flavin-containing monooxygenase and calreticulin
    • Guan S, Falick AM, Williams DA, Cashman JR: Evidence for complex formation between rabbit lung flavin-containing monooxygenase and calreticulin. Biochemistry 30: 9892-9900 (1991).
    • (1991) Biochemistry , vol.30 , pp. 9892-9900
    • Guan, S.1    Falick, A.M.2    Williams, D.A.3    Cashman, J.R.4
  • 21
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining
    • Heukeshoven J, Dernick R: Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining. Electrophoresis 6: 103-112 (1985).
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 22
    • 51249176890 scopus 로고
    • Assaying chimeric genes in plants: The GUS gene fusion system
    • Jefferson RA: Assaying chimeric genes in plants: the GUS gene fusion system. Plant Mol Biol Rep 5: 387-405 (1987).
    • (1987) Plant Mol Biol Rep , vol.5 , pp. 387-405
    • Jefferson, R.A.1
  • 23
    • 0342444416 scopus 로고
    • GUS fusions: Beta-glucuronidase as a sensitive and versatile gene marker in higher plants
    • Jefferson RA, Kavanagh TA, Bevan MW: GUS fusions: beta-glucuronidase as a sensitive and versatile gene marker in higher plants. EMBO J 6: 3901-3907 (1987).
    • (1987) EMBO J , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 24
    • 0029105589 scopus 로고
    • Binding-protein expression is subject to temporal, developmental, and stress-induced regulation in terminally differentiated soybean organs
    • Kalinski A, Rowley DL, Loer DS, Foley C, Buta G, Herman EM: Binding-protein expression is subject to temporal, developmental, and stress-induced regulation in terminally differentiated soybean organs. Planta 195: 611-621 (1995).
    • (1995) Planta , vol.195 , pp. 611-621
    • Kalinski, A.1    Rowley, D.L.2    Loer, D.S.3    Foley, C.4    Buta, G.5    Herman, E.M.6
  • 25
    • 0023303619 scopus 로고
    • Molecular cloning of the Beta-subunit of human prolyl-4-hydroxylase. This subunit and protein disulfide isomerase are products of the same gene
    • Koivu J, Myllya R, Helaakoski T, Pihlajaniemi T, Tasanen K, Kivirikko KI: Molecular cloning of the Beta-subunit of human prolyl-4-hydroxylase. This subunit and protein disulfide isomerase are products of the same gene. EMBO J 6: 643-649 (1987).
    • (1987) EMBO J , vol.6 , pp. 643-649
    • Koivu, J.1    Myllya, R.2    Helaakoski, T.3    Pihlajaniemi, T.4    Tasanen, K.5    Kivirikko, K.I.6
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227: 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 8544253576 scopus 로고
    • Radioiodination by use of the Bolton-Hunter and related reagents
    • Langone J: Radioiodination by use of the Bolton-Hunter and related reagents. Meth Enzymol 70: 21-247 (1989).
    • (1989) Meth Enzymol , vol.70 , pp. 21-247
    • Langone, J.1
  • 28
    • 0023749218 scopus 로고
    • Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum
    • Macer DRJ, Koch GLE: Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum. J Cell Sci 91: 61-70 (1988).
    • (1988) J Cell Sci , vol.91 , pp. 61-70
    • Macer, D.R.J.1    Koch, G.L.E.2
  • 29
    • 0029670548 scopus 로고    scopus 로고
    • Snapshots of membrane-translocating proteins
    • Maroglio B, Dobberstein B: Snapshots of membrane-translocating proteins. Trends Cell Biol 6: 142-147 (1996).
    • (1996) Trends Cell Biol , vol.6 , pp. 142-147
    • Maroglio, B.1    Dobberstein, B.2
  • 30
    • 1542460575 scopus 로고
    • Qualitative and quantitative changes in mRNA of castor beans during initial stages of germination
    • Martin C, Northcote DA: Qualitative and quantitative changes in mRNA of castor beans during initial stages of germination. Planta 151: 189-197 (1981).
    • (1981) Planta , vol.151 , pp. 189-197
    • Martin, C.1    Northcote, D.A.2
  • 31
    • 0021379023 scopus 로고
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis. J Biochem 95: 511-519 (1984).
    • (1984) J Biochem , vol.95 , pp. 511-519
    • Maruyama, K.1    Mikawa, T.2    Ebashi, S.3
  • 32
    • 0025259121 scopus 로고
    • Limited N-terminal sequence analysis
    • Matsudaira P: Limited N-terminal sequence analysis. Meth Enzymol 182: 602-613 (1990).
    • (1990) Meth Enzymol , vol.182 , pp. 602-613
    • Matsudaira, P.1
  • 33
    • 0026801469 scopus 로고
    • The 5′-flanking region of the human calreticulin gene shares homology with the human GRP78, GRP94, and protein disulfide isomerase promoters
    • McCauliffe DP, Yang Y-S, Wilson J, Sontheimer RD, Capra JD: The 5′-flanking region of the human calreticulin gene shares homology with the human GRP78, GRP94, and protein disulfide isomerase promoters. J Biol Chem 267: 2557-2562 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 2557-2562
    • McCauliffe, D.P.1    Yang, Y.-S.2    Wilson, J.3    Sontheimer, R.D.4    Capra, J.D.5
  • 36
    • 0025834610 scopus 로고
    • Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum
    • Milner RE, baksh S, Shemanko C, Carpenter MR, Smillie L, Vance JE, Opas M, Michalak M: Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum. J Biol Chem 266: 7155-7165 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 7155-7165
    • Milner, R.E.1    Baksh, S.2    Shemanko, C.3    Carpenter, M.R.4    Smillie, L.5    Vance, J.E.6    Opas, M.7    Michalak, M.8
  • 38
    • 0028964421 scopus 로고
    • Calreticulin functions as a molecular chaperone in the biosynthesis of myleloperoxidase
    • Nauseef WM, McCormick SJ, Clark RA: Calreticulin functions as a molecular chaperone in the biosynthesis of myleloperoxidase. J Biol Chem 270: 4741-4747 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 4741-4747
    • Nauseef, W.M.1    McCormick, S.J.2    Clark, R.A.3
  • 41
    • 0030053103 scopus 로고    scopus 로고
    • Calreticulin interacts with newly synthesised human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin
    • Otteken O, Moss B: Calreticulin interacts with newly synthesised human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J Biol Chem 271: 97-103 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 97-103
    • Otteken, O.1    Moss, B.2
  • 42
    • 0025225456 scopus 로고
    • The retention signal for soluble proteins of the endoplasmic reticulum
    • Pelham HRB: The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem Sci 15: 483-486 (1990).
    • (1990) Trends Biochem Sci , vol.15 , pp. 483-486
    • Pelham, H.R.B.1
  • 43
    • 8544278538 scopus 로고    scopus 로고
    • Calreticulin is a lectin like chaperone for glycoproteins in the endoplasmic reticulum
    • Peterson J, Ora A, Helenius A: Calreticulin is a lectin like chaperone for glycoproteins in the endoplasmic reticulum. Mol Biol Cell 6: 1173-1184 (1996).
    • (1996) Mol Biol Cell , vol.6 , pp. 1173-1184
    • Peterson, J.1    Ora, A.2    Helenius, A.3
  • 47
    • 0025840492 scopus 로고
    • Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulphide isomerase and a phosphatidylinositol-specific phospholipase C
    • Shorrosh BS, Dixon RA: Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulphide isomerase and a phosphatidylinositol-specific phospholipase C. Proc Natl Acad Sci USA 88: 10941-10945 (1991).
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10941-10945
    • Shorrosh, B.S.1    Dixon, R.A.2
  • 49
    • 0028606112 scopus 로고
    • Identification of calreticulin as a rubella virus RNA binding protein
    • Singh NK, Atreya CD, Nakhasi HL: Identification of calreticulin as a rubella virus RNA binding protein. Proc Natl Acad Sci USA 91: 12770-12774 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12770-12774
    • Singh, N.K.1    Atreya, C.D.2    Nakhasi, H.L.3
  • 50
    • 0024829021 scopus 로고
    • Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ES/SR protein
    • Smith M, Koch GLE: Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ES/SR protein. EMBO J 8: 3581-3586 (1989).
    • (1989) EMBO J , vol.8 , pp. 3581-3586
    • Smith, M.1    Koch, G.L.E.2
  • 52
    • 0039080152 scopus 로고
    • Do exons code for structural or functional units in proteins?
    • Traut TW: Do exons code for structural or functional units in proteins? Proc Natl Acad Sci USA 85: 2944-2948 (1988).
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2944-2948
    • Traut, T.W.1
  • 53
    • 0001143106 scopus 로고
    • The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport
    • Vitale A, Ceriotti A, Denecke J: The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport. J Exp Bot 44: 1417-1444 (1993).
    • (1993) J Exp Bot , vol.44 , pp. 1417-1444
    • Vitale, A.1    Ceriotti, A.2    Denecke, J.3
  • 54
    • 0023928974 scopus 로고
    • Transcending the inpenetrable: How proteins come to terms with membranes
    • Von Heijne G: Transcending the inpenetrable: how proteins come to terms with membranes. Biochim Biophys Acta 947: 307-333 (1988).
    • (1988) Biochim Biophys Acta , vol.947 , pp. 307-333
    • Von Heijne, G.1
  • 55
    • 0027571389 scopus 로고
    • A pathogen-induced gene of barley encodes a HSP90 homologue showing striking similarity to vertebrate forms resident in the endoplasmic reticulum
    • Walther-Larsen H, Brandt J, Collinge DB, Thordal-Christensen H: A pathogen-induced gene of barley encodes a HSP90 homologue showing striking similarity to vertebrate forms resident in the endoplasmic reticulum. Plant Mol Biol 21: 1097-1108 (1993).
    • (1993) Plant Mol Biol , vol.21 , pp. 1097-1108
    • Walther-Larsen, H.1    Brandt, J.2    Collinge, D.B.3    Thordal-Christensen, H.4
  • 57
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • Wetterau JR, Combs KA, Spinner SN, Joiner BJ: Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J Biol Chem 265: 9800-9807 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 9800-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.