메뉴 건너뛰기




Volumn 5, Issue 8, 2006, Pages 1378-1387

Eukaryotic release factor 1 phosphorylation by CK2 protein kinase is dynamic but has little effect on the efficiency of translation termination in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE II; EUKARYOTIC RELEASE FACTOR 1, S CEREVISIAE; MESSENGER RNA; PEPTIDE CHAIN RELEASE FACTOR 3; PEPTIDE-CHAIN-RELEASE FACTOR 3; PHOSPHOPROTEIN PHOSPHATASE; PPQ1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSLATION TERMINATION FACTOR;

EID: 33747339238     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00073-06     Document Type: Article
Times cited : (16)

References (44)
  • 1
    • 8544253956 scopus 로고    scopus 로고
    • A faux 3′-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay
    • Amrani, N., R. Ganesan, S. Kervestin, D. A. Mangus, S. Ghosh, and A. Jacobson. 2004. A faux 3′-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay. Nature 432:112-118.
    • (2004) Nature , vol.432 , pp. 112-118
    • Amrani, N.1    Ganesan, R.2    Kervestin, S.3    Mangus, D.A.4    Ghosh, S.5    Jacobson, A.6
  • 2
    • 0030466725 scopus 로고    scopus 로고
    • The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1
    • Andjelkovic, N., S. Zolnierowicz, C. Van Hoof, J. Goris, and B. A. Hemmings. 1996. The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1. EMBO J. 15:7156-7167.
    • (1996) EMBO J. , vol.15 , pp. 7156-7167
    • Andjelkovic, N.1    Zolnierowicz, S.2    Van Hoof, C.3    Goris, J.4    Hemmings, B.A.5
  • 4
    • 0242541806 scopus 로고    scopus 로고
    • Genetic interactions among ZDS1.2, CDC37, and protein kinase CK2 in Saccharomyces cerevisiae
    • Bandhakavi, S., R. O. McCann, D. E. Hanna, and C. V. Glover. 2003. Genetic interactions among ZDS1.2, CDC37, and protein kinase CK2 in Saccharomyces cerevisiae. FEBS Lett. 554:295-300.
    • (2003) FEBS Lett. , vol.554 , pp. 295-300
    • Bandhakavi, S.1    McCann, R.O.2    Hanna, D.E.3    Glover, C.V.4
  • 5
    • 0033827056 scopus 로고    scopus 로고
    • Terminating eukaryote translation: Domain 1 of release factor eRF1 functions in stop codon recognition
    • Bertram, G., H. A. Bell, D. W. Ritchie, G. Fullerton, and I. Stansfield. 2000. Terminating eukaryote translation: domain 1 of release factor eRF1 functions in stop codon recognition. RNA 6:1236-1247.
    • (2000) RNA , vol.6 , pp. 1236-1247
    • Bertram, G.1    Bell, H.A.2    Ritchie, D.W.3    Fullerton, G.4    Stansfield, I.5
  • 6
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-Fluoro-orotic acid resistance
    • Boeke, J. D., F. LaCroute, and G. R. Fink. 1984. A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet. 197:345-346.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    LaCroute, F.2    Fink, G.R.3
  • 7
    • 0026607164 scopus 로고
    • Casein kinase II phosphorylates the eukaryote-specific C-terminal domain of topoisomerase II in vivo
    • Cardenas, M. E., Q. Dang, C. V. Glover, and S. M. Gasser. 1992. Casein kinase II phosphorylates the eukaryote-specific C-terminal domain of topoisomerase II in vivo. EMBO J. 11:1785-1796.
    • (1992) EMBO J. , vol.11 , pp. 1785-1796
    • Cardenas, M.E.1    Dang, Q.2    Glover, C.V.3    Gasser, S.M.4
  • 8
    • 0025003542 scopus 로고
    • Functional properties of phosphorylated elongation factor 2
    • Carlberg, U., A. Nilsson, and O. Nygard. 1990. Functional properties of phosphorylated elongation factor 2. Eur. J. Biochem. 191:639-645.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 639-645
    • Carlberg, U.1    Nilsson, A.2    Nygard, O.3
  • 9
    • 0032518567 scopus 로고    scopus 로고
    • Insulin stimulation of phosphorylation of elongation factor 1 (eEF-1) enhances elongation activity
    • Chang, Y. W., and J. A. Traugh. 1998. Insulin stimulation of phosphorylation of elongation factor 1 (eEF-1) enhances elongation activity. Eur. J. Biochem. 251:201-207.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 201-207
    • Chang, Y.W.1    Traugh, J.A.2
  • 10
    • 0034826629 scopus 로고    scopus 로고
    • The polypeptide chain release factor eRF1 specifically contacts the s(4)UGA stop codon located in the A site of eukaryotic ribosomes
    • Chavatte, L., L. Frolova, L. Kisselev, and A. Favre. 2001. The polypeptide chain release factor eRF1 specifically contacts the s(4)UGA stop codon located in the A site of eukaryotic ribosomes. Eur. J. Biochem. 268:2896-2904.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2896-2904
    • Chavatte, L.1    Frolova, L.2    Kisselev, L.3    Favre, A.4
  • 11
    • 0027139838 scopus 로고
    • PPQ, a novel protein phosphatase containing a Ser + Asn-rich amino-terminal domain, is involved in the regulation of protein synthesis
    • Chen, M. X., Y. H. Chen, and P. T. Cohen. 1993. PPQ, a novel protein phosphatase containing a Ser + Asn-rich amino-terminal domain, is involved in the regulation of protein synthesis. Eur. J. Biochem. 218:689-699.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 689-699
    • Chen, M.X.1    Chen, Y.H.2    Cohen, P.T.3
  • 13
    • 0031768437 scopus 로고    scopus 로고
    • Accumulation of mRNA coding for the ctf 13p kinetochore subunit of Saccharomyces cerevisiae depends on the same factors that promote rapid decay of nonsense mRNAs
    • Dahlseid, J. N., J. Puziss, R. L. Shirley, A. L. Atkin, P. Hieter, and M. R. Culbertson. 1998. Accumulation of mRNA coding for the ctf 13p kinetochore subunit of Saccharomyces cerevisiae depends on the same factors that promote rapid decay of nonsense mRNAs. Genetics 150:1019-1035.
    • (1998) Genetics , vol.150 , pp. 1019-1035
    • Dahlseid, J.N.1    Puziss, J.2    Shirley, R.L.3    Atkin, A.L.4    Hieter, P.5    Culbertson, M.R.6
  • 14
    • 0033016754 scopus 로고    scopus 로고
    • C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids
    • Ebihara, K., and Y. Nakamura. 1999. C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids. RNA 5:739-750.
    • (1999) RNA , vol.5 , pp. 739-750
    • Ebihara, K.1    Nakamura, Y.2
  • 15
    • 0032937983 scopus 로고    scopus 로고
    • The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae
    • Eurwilaichitr, L., F. M. Graves, I. Stansfield, and M. F. Tuite. 1999. The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae. Mol. Microbiol. 32:485-496.
    • (1999) Mol. Microbiol. , vol.32 , pp. 485-496
    • Eurwilaichitr, L.1    Graves, F.M.2    Stansfield, I.3    Tuite, M.F.4
  • 16
    • 0028122964 scopus 로고
    • Casein kinase II mediates multiple phosphorylation of Saccharomyces cerevisiae eIF-2α (encoded by SUI2), which is required for optimal eIF-2 function in S. cerevisiae
    • Feng, L., H. Yoon, and T. F. Donahue. 1994. Casein kinase II mediates multiple phosphorylation of Saccharomyces cerevisiae eIF-2α (encoded by SUI2), which is required for optimal eIF-2 function in S. cerevisiae. Mol. Cell. Biol. 14:5139-5153.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5139-5153
    • Feng, L.1    Yoon, H.2    Donahue, T.F.3
  • 17
    • 19244364778 scopus 로고    scopus 로고
    • Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome-dependent guanosine triphosphatase
    • Frolova, L., X. Le Goff, G. Zhouravleva, E. Davydova, M. Philippe, and L. Kisselev. 1996. Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome-dependent guanosine triphosphatase. RNA 2:334-341.
    • (1996) RNA , vol.2 , pp. 334-341
    • Frolova, L.1    Le Goff, X.2    Zhouravleva, G.3    Davydova, E.4    Philippe, M.5    Kisselev, L.6
  • 18
    • 0035787713 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in Saccharomyces cerevisiae: A quality control mechanism that degrades transcripts harboring premature termination codons
    • Gonzalez, C. I., W. Wang, and S. W. Peltz. 2001. Nonsense-mediated mRNA decay in Saccharomyces cerevisiae: a quality control mechanism that degrades transcripts harboring premature termination codons. Cold Spring Harb. Symp. Quant. Biol. 66:321-328.
    • (2001) Cold Spring Harb. Symp. Quant. Biol. , vol.66 , pp. 321-328
    • Gonzalez, C.I.1    Wang, W.2    Peltz, S.W.3
  • 19
    • 0031922812 scopus 로고    scopus 로고
    • A dual-luciferase reporter system for studying receding signals
    • Grentzmann, G., J. A. Ingram, P. J. Kelly, R. F. Gesteland, and J. F. Atkins. 1998. A dual-luciferase reporter system for studying receding signals. RNA 4:479-486.
    • (1998) RNA , vol.4 , pp. 479-486
    • Grentzmann, G.1    Ingram, J.A.2    Kelly, P.J.3    Gesteland, R.F.4    Atkins, J.F.5
  • 20
    • 26944487335 scopus 로고    scopus 로고
    • Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology
    • Gross, S. R., and T. G. Kinzy. 2005. Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology. Nat. Struct. Mol. Biol. 12:772-778.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 772-778
    • Gross, S.R.1    Kinzy, T.G.2
  • 21
    • 0028805890 scopus 로고
    • Casein kinase II is required for cell cycle progression during G1 and G2/M in Saccharomyces cerevisiae
    • Hanna, D. E., A. Rethinaswamy, and C. V. Glover. 1995. Casein kinase II is required for cell cycle progression during G1 and G2/M in Saccharomyces cerevisiae. J. Biol. Chem. 270:25905-25914.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25905-25914
    • Hanna, D.E.1    Rethinaswamy, A.2    Glover, C.V.3
  • 25
    • 1642447080 scopus 로고    scopus 로고
    • Leaky termination at premature stop codons antagonizes nonsense-mediated mRNA decay in S. cerevisiae
    • Keeling, K. M., J. Lanier, M. Du, J. Salas-Marco, L. Gao, A. Kaenjak-Angeletti, and D. M. Bedwell. 2004. Leaky termination at premature stop codons antagonizes nonsense-mediated mRNA decay in S. cerevisiae. RNA 10:691-703.
    • (2004) RNA , vol.10 , pp. 691-703
    • Keeling, K.M.1    Lanier, J.2    Du, M.3    Salas-Marco, J.4    Gao, L.5    Kaenjak-Angeletti, A.6    Bedwell, D.M.7
  • 26
    • 0028988306 scopus 로고
    • Protein kinase C delta-specific phosphorylation of the elongation factor eEF-alpha and an eEF-1 alpha peptide at threonine 431
    • Kielbassa, K., H. J. Muller, H. E. Meyer, F. Marks, and M. Gschwendt. 1995. Protein kinase C delta-specific phosphorylation of the elongation factor eEF-alpha and an eEF-1 alpha peptide at threonine 431. J. Biol. Chem. 270:6156-6162.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6156-6162
    • Kielbassa, K.1    Muller, H.J.2    Meyer, H.E.3    Marks, F.4    Gschwendt, M.5
  • 27
    • 0028800891 scopus 로고
    • Cloning of the Candida glabrata TRP1 and HIS3 genes, and construction of their disruptant strains by sequential integrative transformation
    • Kitada, K., E. Yamaguchi, and M. Arisawa. 1995. Cloning of the Candida glabrata TRP1 and HIS3 genes, and construction of their disruptant strains by sequential integrative transformation. Gene 165:203-206.
    • (1995) Gene , vol.165 , pp. 203-206
    • Kitada, K.1    Yamaguchi, E.2    Arisawa, M.3
  • 30
    • 0037472524 scopus 로고    scopus 로고
    • Casein kinase II phosphorylates translation initiation factor 5 (eIF5) in Saccharomyces cerevisiae
    • Maiti, T., A. Bandyopadhyay, and U. Maitra. 2003. Casein kinase II phosphorylates translation initiation factor 5 (eIF5) in Saccharomyces cerevisiae. Yeast 20:97-108.
    • (2003) Yeast , vol.20 , pp. 97-108
    • Maiti, T.1    Bandyopadhyay, A.2    Maitra, U.3
  • 31
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio, F., and L. A. Pinna. 2003. One-thousand-and-one substrates of protein kinase CK2? FASEB J. 17:349-368.
    • (2003) FASEB J. , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 32
    • 0035049593 scopus 로고    scopus 로고
    • Overexpression of translation elongation factor 1A affects the organization and function of the actin cytoskeleton in yeast
    • Munshi, R., K. A. Kandl, A. Carr-Schmid, J. L. Whitacre, A. E. Adams, and T. G. Kinzy. 2001. Overexpression of translation elongation factor 1A affects the organization and function of the actin cytoskeleton in yeast. Genetics 157:1425-1436.
    • (2001) Genetics , vol.157 , pp. 1425-1436
    • Munshi, R.1    Kandl, K.A.2    Carr-Schmid, A.3    Whitacre, J.L.4    Adams, A.E.5    Kinzy, T.G.6
  • 33
    • 0034669118 scopus 로고    scopus 로고
    • Phosphorylation and N-terminal region of yeast ribosomal protein Pl mediate its degradation, which is prevented by protein P2
    • Nusspaumer, G., M. Remacha, and J. P. Ballesta. 2000. Phosphorylation and N-terminal region of yeast ribosomal protein Pl 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
  • 34
    • 0030907757 scopus 로고    scopus 로고
    • Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: Implications for prion-dependent regulation
    • Paushkin, S. V., V. V. Kushnirov, V. N. Smirnov, and M. D. Ter-Avanesyan. 1997. Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation. Mol. Cell. Biol. 17:2798-2805.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2798-2805
    • Paushkin, S.V.1    Kushnirov, V.V.2    Smirnov, V.N.3    Ter-Avanesyan, M.D.4
  • 36
    • 0032564302 scopus 로고    scopus 로고
    • Phosphorylation of ribosomal protein P0 is not essential for ribosome function but can affect translation
    • Rodriguez-Gabriel, M. A., M. Remacha, and J. P. Ballesta. 1998. Phosphorylation of ribosomal protein P0 is not essential for ribosome function but can affect translation. Biochemistry 37:16620-16626.
    • (1998) Biochemistry , vol.37 , pp. 16620-16626
    • Rodriguez-Gabriel, M.A.1    Remacha, M.2    Ballesta, J.P.3
  • 37
    • 4344677977 scopus 로고    scopus 로고
    • GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination
    • Salas-Marco, J., and D. M. Bedwell. 2004. GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination. Mol. Cell. Biol. 24:7769-7778.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7769-7778
    • Salas-Marco, J.1    Bedwell, D.M.2
  • 38
    • 0025362399 scopus 로고
    • A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae
    • Schmitt, M. E., T. A. Brown, and B. L. Trumpower. 1990. A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res. 18:3091-3092.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3091-3092
    • Schmitt, M.E.1    Brown, T.A.2    Trumpower, B.L.3
  • 39
    • 0037311233 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factors and regulators
    • Sonenberg, N., and T. E. Dever. 2003. Eukaryotic translation initiation factors and regulators. Curr. Opin. Struct. Biol. 13:56-63.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 56-63
    • Sonenberg, N.1    Dever, T.E.2
  • 40
    • 0023304198 scopus 로고
    • Allosuppressors that enhance the efficiency of omnipotent suppressors in Saccharomyces cerevisiae
    • Song, J. M., and S. W. Liebman. 1987. Allosuppressors that enhance the efficiency of omnipotent suppressors in Saccharomyces cerevisiae. Genetics 115:451-460.
    • (1987) Genetics , vol.115 , pp. 451-460
    • Song, J.M.1    Liebman, S.W.2
  • 41
    • 0030957794 scopus 로고    scopus 로고
    • A conditional-lethal translation termination defect in a sup45 mutant of the yeast Saccharomyces cerevisiae
    • Stansfield, I., V. V. Kushnirov, K. M. Jones, and M. F. Tuite. 1997. A conditional-lethal translation termination defect in a sup45 mutant of the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 245:557-563.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 557-563
    • Stansfield, I.1    Kushnirov, V.V.2    Jones, K.M.3    Tuite, M.F.4
  • 42
    • 0027960808 scopus 로고
    • The yeast translational allosuppressor, SAL6: A new member of the PP1-like phosphatase family with a long serine-rich N-terminal extension
    • Vincent, A., G. Newnam, and S. W. Liebman. 1994. The yeast translational allosuppressor, SAL6: a new member of the PP1-like phosphatase family with a long serine-rich N-terminal extension. Genetics 138:597-608.
    • (1994) Genetics , vol.138 , pp. 597-608
    • Vincent, A.1    Newnam, G.2    Liebman, S.W.3
  • 43
    • 84873787842 scopus 로고
    • A critical evaluation of the nitrogen assimilation tests commonly used in classification of yeasts
    • Wickerham, L. J. 1946. A critical evaluation of the nitrogen assimilation tests commonly used in classification of yeasts. J. Bacteriol. 52:293-301.
    • (1946) J. Bacteriol. , vol.52 , pp. 293-301
    • Wickerham, L.J.1
  • 44
    • 0030976507 scopus 로고    scopus 로고
    • Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr3
    • Wilson, L. K., N. Dhillon, J. Thorner, and G. S. Martin. 1997. Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr3. J. Biol. Chem. 272:12961-12967.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12961-12967
    • Wilson, L.K.1    Dhillon, N.2    Thorner, J.3    Martin, G.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.