메뉴 건너뛰기




Volumn 18, Issue 3, 2009, Pages 629-636

Dematin exhibits a natively unfolded core domain and an independently folded headpiece domain

Author keywords

Actin binding protein; Band 4.9; Erythrocyte dematin; Headpiece domain; Natively unfolded protein; NMR; PEST sequence

Indexed keywords

ACTIN BINDING PROTEIN; ERYTHROCYTE BAND 4.9 PROTEIN; GLUTAMIC ACID; PROLINE; RECOMBINANT PROTEIN; SERINE; THREONINE;

EID: 61449191746     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.59     Document Type: Article
Times cited : (14)

References (34)
  • 1
    • 0024362222 scopus 로고
    • Purification of erythrocyte dematin (protein 4.9) reveals an endogenous protein kinase that modulates actin-bundling activity
    • Chishti AH, Faquin W, Wu CC, Branton D (1989) Purification of erythrocyte dematin (protein 4.9) reveals an endogenous protein kinase that modulates actin-bundling activity. J Biol Chem 264:8985-8991.
    • (1989) J Biol Chem , vol.264 , pp. 8985-8991
    • Chishti, A.H.1    Faquin, W.2    Wu, C.C.3    Branton, D.4
  • 2
    • 0024552276 scopus 로고
    • The spectrin-actin junction of erythrocyte membrane skeletons
    • Bennett V (1989) The spectrin-actin junction of erythrocyte membrane skeletons. Biochim Biophys Acta 988:107-121.
    • (1989) Biochim Biophys Acta , vol.988 , pp. 107-121
    • Bennett, V.1
  • 4
    • 0030872241 scopus 로고    scopus 로고
    • Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein
    • Roof DJ, Hayes A, Adamian M, Chishti A, Li T (1997) Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein. J Cell Biol 138: 575-588.
    • (1997) J Cell Biol , vol.138 , pp. 575-588
    • Roof, D.J.1    Hayes, A.2    Adamian, M.3    Chishti, A.4    Li, T.5
  • 7
    • 0023992619 scopus 로고
    • A immunoreactive form of erythrocyte protein 4.9 is present in non-erythroid cells
    • Faquin WC, Husain A, Hung J, Branton D (1988) A immunoreactive form of erythrocyte protein 4.9 is present in non-erythroid cells. Eur J Cell. Biol 46:168-175.
    • (1988) Eur J Cell. Biol , vol.46 , pp. 168-175
    • Faquin, W.C.1    Husain, A.2    Hung, J.3    Branton, D.4
  • 9
    • 0029084382 scopus 로고
    • Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily
    • Azim. AC, Knoll JHM, Beggs AH, Chishti AH (1995) Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily. J Biol Chem 270:17407-17413.
    • (1995) J Biol Chem , vol.270 , pp. 17407-17413
    • Azim, A.C.1    Knoll, J.H.M.2    Beggs, A.H.3    Chishti, A.H.4
  • 11
    • 0021989328 scopus 로고
    • Partial purification and characterization of an actin-bundling protein, band 4.9, from human erythrocytes
    • Siegel DL, Branton D (1985) Partial purification and characterization of an actin-bundling protein, band 4.9, from human erythrocytes. J Cell Biol 100:775-785.
    • (1985) J Cell Biol , vol.100 , pp. 775-785
    • Siegel, D.L.1    Branton, D.2
  • 12
    • 0023793618 scopus 로고    scopus 로고
    • Abolition of actinbundling by phosphorylation of human erythrocyte protein 4.9
    • Chishti AH, Levin A, Branton. D (1998) Abolition of actinbundling by phosphorylation of human erythrocyte protein 4.9. Nature 334:718-721.
    • (1998) Nature , vol.334 , pp. 718-721
    • Chishti, A.H.1    Levin, A.2    Branton, D.3
  • 13
    • 1542349982 scopus 로고    scopus 로고
    • The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site
    • Frank BS, Vardar D, Chishti AH, McKnight CJ (2004) The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site. J Biol Chem. 279:7909-7916.
    • (2004) J Biol Chem , vol.279 , pp. 7909-7916
    • Frank, B.S.1    Vardar, D.2    Chishti, A.H.3    McKnight, C.J.4
  • 14
    • 32044451299 scopus 로고    scopus 로고
    • A phosphorylationinduced conformation change in dematin headpiece
    • Jiang ZG, McKnight CJ (2006) A phosphorylationinduced conformation change in dematin headpiece. Structure 14:379-387.
    • (2006) Structure , vol.14 , pp. 379-387
    • Jiang, Z.G.1    McKnight, C.J.2
  • 15
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M, Rogers SW (1996) PEST sequences and regulation by proteolysis. Trends Biochem Sci 21: 267-271.
    • (1996) Trends Biochem Sci , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 16
    • 0036415329 scopus 로고    scopus 로고
    • Removal of DnaK contamination during fusion protein purifications
    • Rial VD, Ceccarelli EA (2002) Removal of DnaK contamination during fusion protein purifications. Protein Expr Purif 25:503-507.
    • (2002) Protein Expr Purif , vol.25 , pp. 503-507
    • Rial, V.D.1    Ceccarelli, E.A.2
  • 17
    • 61449113157 scopus 로고    scopus 로고
    • Doolittle RF. Redundancies in protein sequences. In: Fasman GD Ed. (1989) Prediction of protein structure and the principles of protein conformation. New York: Plenum Press, pp 599-623.
    • Doolittle RF. Redundancies in protein sequences. In: Fasman GD Ed. (1989) Prediction of protein structure and the principles of protein conformation. New York: Plenum Press, pp 599-623.
  • 19
    • 34250849051 scopus 로고    scopus 로고
    • The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence
    • Smimov SL, Isern NG, Jiang ZG, Hoyt DW, McKnight CJ (2007) The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence. Biochemistry 46:7488-7496.
    • (2007) Biochemistry , vol.46 , pp. 7488-7496
    • Smimov, S.L.1    Isern, N.G.2    Jiang, Z.G.3    Hoyt, D.W.4    McKnight, C.J.5
  • 20
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink AL (2005) Natively unfolded proteins. Curr Opin Struct Biol 15:35-41.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 21
    • 0036153571 scopus 로고    scopus 로고
    • What does it means to be natively unfolded?
    • Uversky VN (2002) What does it means to be natively unfolded? Eur J Biochem 269:2-12.
    • (2002) Eur J Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 22
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky VN (2002) Natively unfolded proteins: a point where biology waits for physics. Protein Sci 11:739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 23
    • 22544439366 scopus 로고    scopus 로고
    • Human full-length Securin is a natively unfolded protein
    • Sanchez-Puig N, Veprintsev DB, Fersht AR (2005) Human full-length Securin is a natively unfolded protein. Protein Sci 14:1410-1418.
    • (2005) Protein Sci , vol.14 , pp. 1410-1418
    • Sanchez-Puig, N.1    Veprintsev, D.B.2    Fersht, A.R.3
  • 24
    • 33646835410 scopus 로고    scopus 로고
    • HIV-i Tat is a natively unfolded protein: The solution conformation and dynamics of reduced HIV-1 Tat-(1-72) by NMR spectroscopy
    • Shojania S, O'Neil JD (2006) HIV-i Tat is a natively unfolded protein: the solution conformation and dynamics of reduced HIV-1 Tat-(1-72) by NMR spectroscopy. J Biol Chem 281:8347-8356.
    • (2006) J Biol Chem , vol.281 , pp. 8347-8356
    • Shojania, S.1    O'Neil, J.D.2
  • 25
    • 0025584623 scopus 로고
    • PEST sequences are signals for rapid intracellular proteolysis
    • Rechsteiner M (1990) PEST sequences are signals for rapid intracellular proteolysis. Semin Cell Biol 1:433-440.
    • (1990) Semin Cell Biol , vol.1 , pp. 433-440
    • Rechsteiner, M.1
  • 26
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley J, Lu M, Bracken C (2001) A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 20:71-75.
    • (2001) J Biomol NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 28
    • 24644519821 scopus 로고    scopus 로고
    • High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity
    • Meng J, Vardar D, Wang Y, Guo H, Head JF, McKnight CJ (2005) High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity. Biochemistry 44:11963-11973.
    • (2005) Biochemistry , vol.44 , pp. 11963-11973
    • Meng, J.1    Vardar, D.2    Wang, Y.3    Guo, H.4    Head, J.F.5    McKnight, C.J.6
  • 29
    • 0025727887 scopus 로고
    • Negative staining-carbon film technique: New cellular and molecular applications
    • Harris JR (1991) Negative staining-carbon film technique: new cellular and molecular applications. J Electron Microsc Tech 18:269-276.
    • (1991) J Electron Microsc Tech , vol.18 , pp. 269-276
    • Harris, J.R.1
  • 30
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield N, Pasman GD (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8:4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Pasman, G.D.2
  • 31
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M, Saudek V, Sklenař V (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2:661-665.
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenař, V.3
  • 33
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek G, Vuister G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:227-293.
    • (1995) J Biomol NMR , vol.6 , pp. 227-293
    • Delaglio, F.1    Grzesiek, G.2    Vuister, G.3    Pfeifer, J.4    Bax, A.5
  • 34
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA (1994) NMRView: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4:603-614.
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.