메뉴 건너뛰기




Volumn 22, Issue 1, 2003, Pages 13-23

Control of protein life-span by N-terminal methionine excision

Author keywords

Gene knockout; N end rule; Photosystem; Protein degradation; Stability

Indexed keywords

ACTINONIN; METHIONINE; PEPTIDE DEFORMYLASE; POLYPEPTIDE; PROTEIN SUBUNIT; PROTEOME;

EID: 0037413729     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg007     Document Type: Article
Times cited : (132)

References (65)
  • 1
    • 0036776905 scopus 로고    scopus 로고
    • Cutting edge of chloroplast proteolysis
    • Adam, Z. and Clarke, A.K. (2002) Cutting edge of chloroplast proteolysis. Trends Plant Sci., 7, 451-456.
    • (2002) Trends Plant Sci. , vol.7 , pp. 451-456
    • Adam, Z.1    Clarke, A.K.2
  • 2
    • 0032091047 scopus 로고    scopus 로고
    • Mutation of residue threonine-2 of the D2 polypeptide and its effect on photosystem II function in Chlamydomonas reinhardtii
    • Andronis, C., Kruse, O., Deak, Z., Vass, I., Diner, B.A. and Nixon, P.J. (1998) Mutation of residue threonine-2 of the D2 polypeptide and its effect on photosystem II function in Chlamydomonas reinhardtii. Plant Physiol., 117, 515-524.
    • (1998) Plant Physiol. , vol.117 , pp. 515-524
    • Andronis, C.1    Kruse, O.2    Deak, Z.3    Vass, I.4    Diner, B.A.5    Nixon, P.J.6
  • 4
    • 0027199986 scopus 로고
    • Photoinhibifion of photosystem II. Inactivation, protein damage and turnover
    • Aro, E.M., Virgin, I. and Andersson, B. (1993) Photoinhibifion of photosystem II. Inactivation, protein damage and turnover. Biochim. Biophys. Acta, 1143, 113-134.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 113-134
    • Aro, E.M.1    Virgin, I.2    Andersson, B.3
  • 5
    • 0033770817 scopus 로고    scopus 로고
    • Control of methionine biosynthesis in Escherichia coli by proteolysis
    • Biran, D., Gur, E., Gollan, L. and Ron, E.Z. (2000) Control of methionine biosynthesis in Escherichia coli by proteolysis. Mol. Microbiol., 37, 1436-1443.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1436-1443
    • Biran, D.1    Gur, E.2    Gollan, L.3    Ron, E.Z.4
  • 6
    • 0024283282 scopus 로고
    • Chloroplast transformation in Chlamydomonas with high velocity microprojectiles
    • Boynton, J.E. et al. (1988) Chloroplast transformation in Chlamydomonas with high velocity microprojectiles. Science, 240, 1534-1538.
    • (1988) Science , vol.240 , pp. 1534-1538
    • Boynton, J.E.1
  • 8
    • 0032127904 scopus 로고    scopus 로고
    • N-terminal processing: The methionine aminopeptidase and N α-acetyl transferase families
    • Bradshaw, R.A., Brickey, W.W. and Walker, K.W. (1998) N-terminal processing: the methionine aminopeptidase and N α-acetyl transferase families. Trends Biochem. Sci., 23, 263-267.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 263-267
    • Bradshaw, R.A.1    Brickey, W.W.2    Walker, K.W.3
  • 9
    • 0024347025 scopus 로고
    • Methionine amino-peptidase gene of Escherichia coli is essential for cell growth
    • Chang, S.Y., McGary, E.C. and Chang, S. (1989) Methionine amino-peptidase gene of Escherichia coli is essential for cell growth. J. Bacteriol., 171, 4071-4072.
    • (1989) J. Bacteriol. , vol.171 , pp. 4071-4072
    • Chang, S.Y.1    McGary, E.C.2    Chang, S.3
  • 10
    • 0034673093 scopus 로고    scopus 로고
    • Actinonin, a naturally occurring antibacterial agent, is a potent deformylase inhibitor
    • Chen, D.Z. et al. (2000) Actinonin, a naturally occurring antibacterial agent, is a potent deformylase inhibitor. Biochemistry, 39, 1256-1262.
    • (2000) Biochemistry , vol.39 , pp. 1256-1262
    • Chen, D.Z.1
  • 11
    • 0033865042 scopus 로고    scopus 로고
    • Synthesis, assembly and degradation of thylakoid membrane proteins
    • Choquet, Y. and Vallon, O. (2000) Synthesis, assembly and degradation of thylakoid membrane proteins. Biochimie, 82, 615-634.
    • (2000) Biochimie , vol.82 , pp. 615-634
    • Choquet, Y.1    Vallon, O.2
  • 12
    • 0034725661 scopus 로고    scopus 로고
    • RGS4 is arginylated and degraded by the N-end rule pathway in vitro
    • Davydov, I.V. and Varshavsky, A. (2000) RGS4 is arginylated and degraded by the N-end rule pathway in vitro. J. Biol. Chem., 275, 22931-22941.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22931-22941
    • Davydov, I.V.1    Varshavsky, A.2
  • 13
    • 0035212719 scopus 로고    scopus 로고
    • Functional genomics of plant photosynthesis in the fast lane using Chlamydomonas reinhardtii
    • Dent, R.M., Han, M. and Niyogi, K.K. (2001) Functional genomics of plant photosynthesis in the fast lane using Chlamydomonas reinhardtii. Trends Plant Sci., 6. 364-371.
    • (2001) Trends Plant Sci. , vol.6 , pp. 364-371
    • Dent, R.M.1    Han, M.2    Niyogi, K.K.3
  • 14
    • 0024730745 scopus 로고
    • Posttranslational events leading to the assembly of photosystem II protein complex: A study using photosynthesis mutants from Chlamydomonas reinhardtii
    • de Vitry, C., Olive, J., Drapier, D., Recouvreur, M. and Wollman, F.A. (1989) Posttranslational events leading to the assembly of photosystem II protein complex: a study using photosynthesis mutants from Chlamydomonas reinhardtii. J. Cell Biol., 109, 991-1006.
    • (1989) J. Cell Biol. , vol.109 , pp. 991-1006
    • De Vitry, C.1    Olive, J.2    Drapier, D.3    Recouvreur, M.4    Wollman, F.A.5
  • 15
    • 0026045166 scopus 로고
    • Photosystem II particles from Chlamydomonas reinhardtii
    • de Vitry, C., Diner, B.A. and Popot, J.L. (1991) Photosystem II particles from Chlamydomonas reinhardtii. J. Biol. Chem., 266, 16614-16621.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16614-16621
    • De Vitry, C.1    Diner, B.A.2    Popot, J.L.3
  • 16
    • 0024590280 scopus 로고
    • Disruption of the yeast N-myristoyl transferase gene causes recessive lethality
    • Duronio, R.J., Towler, D.A., Heuckeroth, R.O. and Gordon, J.I. (1989) Disruption of the yeast N-myristoyl transferase gene causes recessive lethality. Science, 243, 796-800.
    • (1989) Science , vol.243 , pp. 796-800
    • Duronio, R.J.1    Towler, D.A.2    Heuckeroth, R.O.3    Gordon, J.I.4
  • 17
    • 0032792264 scopus 로고    scopus 로고
    • Characterization of mutants with alterations of the phosphorylation site in the D2 photosystem II polypeptide of Chlamydomonas reinhardtii
    • Fleischmann, M.M. and Rochaix, J.D. (1999) Characterization of mutants with alterations of the phosphorylation site in the D2 photosystem II polypeptide of Chlamydomonas reinhardtii. Plant Physiol., 119, 1557-1566.
    • (1999) Plant Physiol. , vol.119 , pp. 1557-1566
    • Fleischmann, M.M.1    Rochaix, J.D.2
  • 18
    • 0035543404 scopus 로고    scopus 로고
    • Organellar peptide deformylases: Universality of the N-terminal methionine cleavage mechanism
    • Giglione, C. and Meinnel, T. (2001a) Organellar peptide deformylases: universality of the N-terminal methionine cleavage mechanism. Trends Plant Sci., 6, 566-572.
    • (2001) Trends Plant Sci. , vol.6 , pp. 566-572
    • Giglione, C.1    Meinnel, T.2
  • 19
    • 0002002492 scopus 로고    scopus 로고
    • Peptide deformylase as an emerging target for antiparasitic agents
    • Giglione, C. and Meinnel, T. (2001b) Peptide deformylase as an emerging target for antiparasitic agents. Emerg. Therap. Targets, 5, 41-57.
    • (2001) Emerg. Therap. Targets , vol.5 , pp. 41-57
    • Giglione, C.1    Meinnel, T.2
  • 20
    • 0033936704 scopus 로고    scopus 로고
    • Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents
    • Giglione, C., Pierre, M. and Meinnel, T. (2000a) Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents. Mol. Microbiol., 36, 1197-1205.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1197-1205
    • Giglione, C.1    Pierre, M.2    Meinnel, T.3
  • 21
    • 0034329475 scopus 로고    scopus 로고
    • Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms
    • Giglione, C., Serero, A., Pierre, M., Boisson, B. and Meinnel, T. (2000b) Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms. EMBO J., 19, 5916-5929.
    • (2000) EMBO J. , vol.19 , pp. 5916-5929
    • Giglione, C.1    Serero, A.2    Pierre, M.3    Boisson, B.4    Meinnel, T.5
  • 22
    • 0036051481 scopus 로고    scopus 로고
    • The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry
    • Gomez, S.M., Nishio, J.N., Faull, K.F. and Whitelegge, J.P. (2002) The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry. Mol. Cell Proteomics, 1, 46-59.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 46-59
    • Gomez, S.M.1    Nishio, J.N.2    Faull, K.F.3    Whitelegge, J.P.4
  • 23
    • 0031171961 scopus 로고    scopus 로고
    • Methionine aminopeptidase (type 2) is the common target for angiogenesis AGM-1470 and ovalicin
    • Griffith, E.C., Su, Z., Turk, B.E., Chen, S., Chang, Y.-H., Wu, Z., Biemann, K. and Liu, J. (1997) Methionine aminopeptidase (type 2) is the common target for angiogenesis AGM-1470 and ovalicin. Chem. Biol., 4, 461-471.
    • (1997) Chem. Biol. , vol.4 , pp. 461-471
    • Griffith, E.C.1    Su, Z.2    Turk, B.E.3    Chen, S.4    Chang, Y.-H.5    Wu, Z.6    Biemann, K.7    Liu, J.8
  • 26
  • 27
    • 0001596491 scopus 로고    scopus 로고
    • A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II
    • Haussuhl, K. Andersson, B. and Adamska, I. (2001) A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II. EMBO J., 20, 713-722.
    • (2001) EMBO J. , vol.20 , pp. 713-722
    • Haussuhl, K.1    Andersson, B.2    Adamska, I.3
  • 30
    • 0023927794 scopus 로고
    • Altered turnover of allelic variants of hypoxanthine phosphoribosyltransferase is associated with N-terminal amino acid sequence variation
    • Johnson, G.G., Kronert, W.A., Bernstein, S.I., Chapman, V.M. and Smith, K.D. (1988) Altered turnover of allelic variants of hypoxanthine phosphoribosyltransferase is associated with N-terminal amino acid sequence variation. J. Biol. Chem., 263, 9079-9082.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9079-9082
    • Johnson, G.G.1    Kronert, W.A.2    Bernstein, S.I.3    Chapman, V.M.4    Smith, K.D.5
  • 31
    • 0000518615 scopus 로고    scopus 로고
    • In vivo measurements of photosynthetic activity: Methods
    • Rochaix, J.-D., Goldschmidt-Clermont, M. and Merchant, S. (eds). Kluwer, Dordrecht, The Netherlands
    • Joliot, P., Beal, D. and Delosme, R. (1998) In vivo measurements of photosynthetic activity: methods. In Rochaix, J.-D., Goldschmidt-Clermont, M. and Merchant, S. (eds), The Molecular Biology of Chloroplast and Mitochondria in Chlamydomonas. Kluwer, Dordrecht, The Netherlands, pp. 433-449.
    • (1998) The Molecular Biology of Chloroplast and Mitochondria in Chlamydomonas , pp. 433-449
    • Joliot, P.1    Beal, D.2    Delosme, R.3
  • 32
    • 0035936144 scopus 로고    scopus 로고
    • Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi
    • Katinka, M.D. et al. (2001) Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi. Nature, 414, 450-453.
    • (2001) Nature , vol.414 , pp. 450-453
    • Katinka, M.D.1
  • 33
    • 0028178516 scopus 로고
    • 6/f complexes: An approach using genetic transformation of the green alga Chlamydomonas reinhardtii
    • 6/f complexes: an approach using genetic transformation of the green alga Chlamydomonas reinhardtii. EMBO J., 13, 1019-1027.
    • (1994) EMBO J. , vol.13 , pp. 1019-1027
    • Kuras, R.1    Wollman, F.A.2
  • 36
    • 0029585125 scopus 로고
    • Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases
    • Li, X. and Chang, Y.H. (1995) Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc. Natl Acad. Sci. USA, 92, 12357-12361.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12357-12361
    • Li, X.1    Chang, Y.H.2
  • 37
    • 0034031132 scopus 로고    scopus 로고
    • The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein
    • Lindahl, M., Spetea, C., Hundal, T., Oppenheim, A.B., Adam, Z. and Andersson, B. (2000) The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein. Plant Cell, 12, 419-431.
    • (2000) Plant Cell , vol.12 , pp. 419-431
    • Lindahl, M.1    Spetea, C.2    Hundal, T.3    Oppenheim, A.B.4    Adam, Z.5    Andersson, B.6
  • 38
    • 0032515029 scopus 로고    scopus 로고
    • Structure of human methionine aminopeptidase-2 complexed with fumagillin
    • Liu, S., Widom, J., Kemp, C.W. and Clardy, J. (1998) Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science, 282, 1324-1327.
    • (1998) Science , vol.282 , pp. 1324-1327
    • Liu, S.1    Widom, J.2    Kemp, C.W.3    Clardy, J.4
  • 39
    • 0001404141 scopus 로고
    • Fumagillin (H-3), a new antibiotic with amebicidal properties
    • McCowen, M.C., Callender, M.E. and Lawlis, J., Jr (1951) Fumagillin (H-3), a new antibiotic with amebicidal properties. Science. 113, 202-203.
    • (1951) Science , vol.113 , pp. 202-203
    • McCowen, M.C.1    Callender, M.E.2    Lawlis J., Jr.3
  • 41
    • 0001541578 scopus 로고
    • Isolation and characterization of mutants in plant cell culture
    • Maliga, P. (1984) Isolation and characterization of mutants in plant cell culture. Annu. Rev. Plant Physiol., 35, 519-542.
    • (1984) Annu. Rev. Plant Physiol. , vol.35 , pp. 519-542
    • Maliga, P.1
  • 42
    • 0034177339 scopus 로고    scopus 로고
    • Peptide deformylase of eukaryotic protists: A target for new antiparasitic agents?
    • Meinnel, T. (2000) Peptide deformylase of eukaryotic protists: a target for new antiparasitic agents? Parasitol. Today, 16, 165-168.
    • (2000) Parasitol. Today , vol.16 , pp. 165-168
    • Meinnel, T.1
  • 43
    • 0027971916 scopus 로고
    • Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase
    • Meinnel, T. and Blanquet, S. (1994) Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase. J. Bacteriol., 176, 7387-7390.
    • (1994) J. Bacteriol. , vol.176 , pp. 7387-7390
    • Meinnel, T.1    Blanquet, S.2
  • 44
    • 0027882514 scopus 로고
    • Methionine as translation start signal: A review of the enzymes of the pathway in Escherichia coli
    • Meinnel, T., Mechulam, Y. and Blanquet, S. (1993) Methionine as translation start signal: a review of the enzymes of the pathway in Escherichia coli. Biochimie, 75, 1061-1075.
    • (1993) Biochimie , vol.75 , pp. 1061-1075
    • Meinnel, T.1    Mechulam, Y.2    Blanquet, S.3
  • 45
    • 0024729628 scopus 로고
    • pepM is an essential gene in Salmonella typhimurium
    • Miller, C.G., Kukral, A.M., Miller, J.L. and Movva, N.R. (1989) pepM is an essential gene in Salmonella typhimurium. J. Bacteriol., 171, 5215-5217.
    • (1989) J. Bacteriol. , vol.171 , pp. 5215-5217
    • Miller, C.G.1    Kukral, A.M.2    Miller, J.L.3    Movva, N.R.4
  • 47
    • 0026751110 scopus 로고
    • The 'second-codon rule' and autophosphorylation govern the stability and activity of Mos during the meiotic cell cycle in Xenopus oocytes
    • Nishizawa, M., Okazaki, K., Furuno, N., Watanabe, N. and Sagata, N. (1992) The 'second-codon rule' and autophosphorylation govern the stability and activity of Mos during the meiotic cell cycle in Xenopus oocytes. EMBO J. 11, 2433-2446.
    • (1992) EMBO J. , vol.11 , pp. 2433-2446
    • Nishizawa, M.1    Okazaki, K.2    Furuno, N.3    Watanabe, N.4    Sagata, N.5
  • 48
    • 0034669118 scopus 로고    scopus 로고
    • Phosphorylation and N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2
    • Nusspaumer, G., Remacha, M. and Ballesta, J.P. (2000) Phosphorylation and N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2. EMBO J., 19, 6075-6084.
    • (2000) EMBO J. , vol.19 , pp. 6075-6084
    • Nusspaumer, G.1    Remacha, M.2    Ballesta, J.P.3
  • 49
    • 0019494798 scopus 로고
    • A nuclear mutant of Chlamydomonas reinhardtii defective in photosynthetic photo-phosphorylation. Characterization of the algal coupling factor ATPase
    • Piccioni, R.G., Bennoun, P. and Chua, N.H. (1981) A nuclear mutant of Chlamydomonas reinhardtii defective in photosynthetic photo-phosphorylation. Characterization of the algal coupling factor ATPase. Eur. J. Biochem., 117, 93-102.
    • (1981) Eur. J. Biochem. , vol.117 , pp. 93-102
    • Piccioni, R.G.1    Bennoun, P.2    Chua, N.H.3
  • 50
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra, R.J., Thompson, W.A. and Kriedemann, P.E. (1989) Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim. Biophys. Acta, 975, 384-394.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 51
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H. and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem., 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    Von Jagow, G.2
  • 52
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schagger, H., Cramer, W.A. and von Jagow, G. (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem., 217, 220-230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 53
    • 0035824874 scopus 로고    scopus 로고
    • Distinctive features of the two classes of eukaryotic peptide deformylases
    • Serero, A., Giglione, C. and Meinnel, T. (2001a) Distinctive features of the two classes of eukaryotic peptide deformylases. J. Mol. Biol., 314, 695-708.
    • (2001) J. Mol. Biol. , vol.314 , pp. 695-708
    • Serero, A.1    Giglione, C.2    Meinnel, T.3
  • 54
    • 0002301759 scopus 로고    scopus 로고
    • Seeking new targets for antiparasitic agents
    • Serero, A., Giglione, C. and Meinnel, T. (2001b) Seeking new targets for antiparasitic agents. Trends Parasitol., 17, 7-8.
    • (2001) Trends Parasitol. , vol.17 , pp. 7-8
    • Serero, A.1    Giglione, C.2    Meinnel, T.3
  • 55
    • 0030924753 scopus 로고    scopus 로고
    • The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2
    • Sin, N., Meng, L., Wang, M.Q., Wen, J.J., Bornmann, W.G. and Crews, C.M. (1997) The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2. Proc. Natl Acad. Sci. USA, 94, 6099-6103.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6099-6103
    • Sin, N.1    Meng, L.2    Wang, M.Q.3    Wen, J.J.4    Bornmann, W.G.5    Crews, C.M.6
  • 56
    • 0032766060 scopus 로고    scopus 로고
    • Processing of the N termini of nascent polypeptide chains requires deformylation prior to methionine removal
    • Solbiati, J., Chapman-Smith, A., Miller, J.L., Miller, C.G. and Cronan, J.E., Jr (1999) Processing of the N termini of nascent polypeptide chains requires deformylation prior to methionine removal. J. Mol. Biol., 290, 607-614.
    • (1999) J. Mol. Biol. , vol.290 , pp. 607-614
    • Solbiati, J.1    Chapman-Smith, A.2    Miller, J.L.3    Miller, C.G.4    Cronan J.E., Jr.5
  • 57
    • 0037077261 scopus 로고    scopus 로고
    • Stabilization of the biotinoyl domain of Escherichia coli acetyl-CoA carboxylase by interactions between the attached biotin and the protruding 'thumb'structure
    • Solbiati, J., Chapman-Smith, A. and Cronan, J.E., Jr (2002) Stabilization of the biotinoyl domain of Escherichia coli acetyl-CoA carboxylase by interactions between the attached biotin and the protruding 'thumb'structure. J. Biol. Chem., 277, 21604-21609.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21604-21609
    • Solbiati, J.1    Chapman-Smith, A.2    Cronan J.E., Jr.3
  • 59
    • 0030910218 scopus 로고    scopus 로고
    • Synthesis and assembly of the D1 protein into photosystem II: Processing of the C-terminus and identification of the initial assembly partners and complexes during photosystem II repair
    • van Wijk, K.J., Roobol-Boza, M., Kettunen, R. Andersson, B. and Aro, E.M. (1997) Synthesis and assembly of the D1 protein into photosystem II: processing of the C-terminus and identification of the initial assembly partners and complexes during photosystem II repair. Biochemistry, 36. 6178-6186.
    • (1997) Biochemistry , vol.36 , pp. 6178-6186
    • Van Wijk, K.J.1    Roobol-Boza, M.2    Kettunen, R.3    Andersson, B.4    Aro, E.M.5
  • 60
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A. (1996) The N-end rule: functions, mysteries, uses. Proc. Natl Acad. Sci. USA, 93, 12142-12149.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 61
    • 0035831456 scopus 로고    scopus 로고
    • Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana
    • Vener, A.V., Harms, A., Sussman, M.R. and Vierstra, R.D. (2001) Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana. J. Biol. Chem., 276, 6959-6966.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6959-6966
    • Vener, A.V.1    Harms, A.2    Sussman, M.R.3    Vierstra, R.D.4
  • 63
    • 0032910388 scopus 로고    scopus 로고
    • The biogenesis and assembly of photosynthetic proteins in thylakoid membranes
    • Wollman, F.A., Minai, L. and Nechushtai, R. (1999) The biogenesis and assembly of photosynthetic proteins in thylakoid membranes. Biochim. Biophys. Acta, 1411, 21-85.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 21-85
    • Wollman, F.A.1    Minai, L.2    Nechushtai, R.3
  • 64
    • 0033523114 scopus 로고    scopus 로고
    • Cotranslational assembly of the D1 protein into photosystem II
    • Zhang, L., Paakkarinen, V., van Wijk, K.J. and Aro, E.M. (1999) Cotranslational assembly of the D1 protein into photosystem II. J. Biol. Chem., 274, 16062-16067.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16062-16067
    • Zhang, L.1    Paakkarinen, V.2    Van Wijk, K.J.3    Aro, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.