메뉴 건너뛰기




Volumn 37, Issue 18, 2009, Pages 6116-6125

Stm1p alters the ribosome association of eukaryotic elongation factor 3 and affects translation elongation

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR 3; HYGROMYCIN; MUTANT PROTEIN; PAROMOMYCIN; PROTEIN STM1P; SACCHAROMYCES CEREVISIAE PROTEIN; UNCLASSIFIED DRUG;

EID: 70350700748     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp645     Document Type: Article
Times cited : (24)

References (47)
  • 1
    • 0027053633 scopus 로고
    • Molecular analysis of POP2 gene, a gene required for glucose-derepression of gene expression in Saccharomyces cerevisiae
    • Sakai,A., Chibazakura,T., Shimizu,Y. and Hishinuma,F. (1992) Molecular analysis of POP2 gene, a gene required for glucose-derepression of gene expression in Saccharomyces cerevisiae. Nucleic Acids Res., 20, 6227-6233.
    • (1992) Nucleic Acids Res , vol.20 , pp. 6227-6233
    • Sakai, A.1    Chibazakura, T.2    Shimizu, Y.3    Hishinuma, F.4
  • 2
    • 0027967851 scopus 로고
    • A new yeast gene, HTR1, required for growth at high temperature, is needed for recovery from mating pheromone-induced G1 arrest
    • Kikuchi,Y., Oka,Y., Kobayashi,M., Uesono,Y., Toh-e,A. and Kikuchi,A. (1994) A new yeast gene, HTR1, required for growth at high temperature, is needed for recovery from mating pheromone-induced G1 arrest. Mol. Gen. Genet., 245, 107-116.
    • (1994) Mol. Gen. Genet , vol.245 , pp. 107-116
    • Kikuchi, Y.1    Oka, Y.2    Kobayashi, M.3    Uesono, Y.4    Toh-e, A.5    Kikuchi, A.6
  • 3
    • 0029152117 scopus 로고
    • A high dose of the STM1 gene suppresses the temperature sensitivity of the tom1 and htr1 mutants in Saccharomyces cerevisiae
    • Utsugi,T., Toh-e,A. and Kikuchi,Y. (1995) A high dose of the STM1 gene suppresses the temperature sensitivity of the tom1 and htr1 mutants in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1263, 285-288.
    • (1995) Biochim. Biophys. Acta , vol.1263 , pp. 285-288
    • Utsugi, T.1    Toh-e, A.2    Kikuchi, Y.3
  • 4
    • 0031886351 scopus 로고    scopus 로고
    • Dhh1p, a putative RNA helicase, associates with the general transcription factors Pop2p and Ccr4p from Saccharomyces cerevisiae
    • Hata,H., Mitsui,H., Liu,H., Bai,Y., Denis,C.L., Shimizu,Y. and Sakai,A. (1998) Dhh1p, a putative RNA helicase, associates with the general transcription factors Pop2p and Ccr4p from Saccharomyces cerevisiae. Genetics, 148, 571-579.
    • (1998) Genetics , vol.148 , pp. 571-579
    • Hata, H.1    Mitsui, H.2    Liu, H.3    Bai, Y.4    Denis, C.L.5    Shimizu, Y.6    Sakai, A.7
  • 6
    • 0035217080 scopus 로고    scopus 로고
    • Apoptosis in yeast: A new model for aging research
    • Fröhlich,K.U. and Madeo,F. (2001) Apoptosis in yeast: A new model for aging research. Exp. Gerontol., 37, 27-31.
    • (2001) Exp. Gerontol , vol.37 , pp. 27-31
    • Fröhlich, K.U.1    Madeo, F.2
  • 7
    • 0036042588 scopus 로고    scopus 로고
    • STM1, a gene which encodes a guanine quadruplex binding protein, interacts with CDC13 in Saccharomyces cerevisiae
    • Hayashi,N. and Murakami,S. (2002) STM1, a gene which encodes a guanine quadruplex binding protein, interacts with CDC13 in Saccharomyces cerevisiae. Mol. Genet. Genomics, 267, 806-813.
    • (2002) Mol. Genet. Genomics , vol.267 , pp. 806-813
    • Hayashi, N.1    Murakami, S.2
  • 8
    • 2642531102 scopus 로고    scopus 로고
    • Stm1p, a G4 quadruplex and purine motif triplex nucleic acid-binding protein, interacts with ribosomes and subtelomeric Y' DNA in Saccharomyces cerevisiae
    • Van Dyke,M.W., Nelson,L.D., Weilbaecher,R.G. and Mehta,D.V. (2004) Stm1p, a G4 quadruplex and purine motif triplex nucleic acid-binding protein, interacts with ribosomes and subtelomeric Y' DNA in Saccharomyces cerevisiae. J. Biol. Chem., 279, 24323-24333.
    • (2004) J. Biol. Chem , vol.279 , pp. 24323-24333
    • Van Dyke, M.W.1    Nelson, L.D.2    Weilbaecher, R.G.3    Mehta, D.V.4
  • 9
    • 33646106577 scopus 로고    scopus 로고
    • Stm1p, a ribosome-associated protein, is important for protein synthesis in Saccharomyces cerevisiae under nutritional stress conditions
    • Van Dyke,N., Baby,J. and Van Dyke,M.W. (2006) Stm1p, a ribosome-associated protein, is important for protein synthesis in Saccharomyces cerevisiae under nutritional stress conditions. J. Mol. Biol., 358, 1023-1031.
    • (2006) J. Mol. Biol , vol.358 , pp. 1023-1031
    • Van Dyke, N.1    Baby, J.2    Van Dyke, M.W.3
  • 10
    • 34250614765 scopus 로고    scopus 로고
    • CAF1 plays an important role in mRNA deadenylation separate from its contact to CCR4
    • Ohn,T., Chiang,Y.C., Lee,D.J., Yao,G., Zhang,C. and Denis,C.L. (2007) CAF1 plays an important role in mRNA deadenylation separate from its contact to CCR4. Nucleic Acids Res., 35, 3002-3015.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3002-3015
    • Ohn, T.1    Chiang, Y.C.2    Lee, D.J.3    Yao, G.4    Zhang, C.5    Denis, C.L.6
  • 11
    • 61549115905 scopus 로고    scopus 로고
    • Stm1 modulates mRNA decay and Dhh1 function in Saccharomyces cerevisiae
    • Balagopal,V. and Parker,R. (2009) Stm1 modulates mRNA decay and Dhh1 function in Saccharomyces cerevisiae. Genetics, 181, 93-103.
    • (2009) Genetics , vol.181 , pp. 93-103
    • Balagopal, V.1    Parker, R.2
  • 12
    • 0028912841 scopus 로고
    • A yeast gene product, G4p2, with a specific affinity for quadruplex nucleic acids
    • Frantz,J.D. and Gilbert,W. (1995) A yeast gene product, G4p2, with a specific affinity for quadruplex nucleic acids. J. Biol. Chem., 270, 9413-9419.
    • (1995) J. Biol. Chem , vol.270 , pp. 9413-9419
    • Frantz, J.D.1    Gilbert, W.2
  • 13
    • 0034102424 scopus 로고    scopus 로고
    • The yeast STM1 gene encodes a purine-motif triple-helical DNA binding protein
    • Nelson,L.D., Musso,M. and Van Dyke,M.W. (2000) The yeast STM1 gene encodes a purine-motif triple-helical DNA binding protein. J. Biol. Chem., 275, 5573-5581.
    • (2000) J. Biol. Chem , vol.275 , pp. 5573-5581
    • Nelson, L.D.1    Musso, M.2    Van Dyke, M.W.3
  • 14
    • 0002024553 scopus 로고    scopus 로고
    • Sonenberg,N. and Hershey,J.W.B, eds, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp
    • Merrick,W.C. and Nyborg,J. (2000) In Sonenberg,N. and Hershey,J.W.B. (eds), Translational Control of Gene Expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 89-126.
    • (2000) Translational Control of Gene Expression , pp. 89-126
    • Merrick, W.C.1    Nyborg, J.2
  • 15
    • 0017342290 scopus 로고
    • Dissimilarity in protein chain elongation factor requirements between yeast and rat liver ribosomes
    • Skogerson,L. and Engelhardt,D. (1977) Dissimilarity in protein chain elongation factor requirements between yeast and rat liver ribosomes. J. Biol. Chem., 252, 1471-1475.
    • (1977) J. Biol. Chem , vol.252 , pp. 1471-1475
    • Skogerson, L.1    Engelhardt, D.2
  • 16
    • 0019843254 scopus 로고
    • Protein synthesis in yeast. I. Purification and properties of elongation factor 3 from Saccharomyces cerevisiae
    • Dasmahapatra,B. and Chakraburtty,K. (1981) Protein synthesis in yeast. I. Purification and properties of elongation factor 3 from Saccharomyces cerevisiae. J. Biol. Chem., 256, 9999-10004.
    • (1981) J. Biol. Chem , vol.256 , pp. 9999-10004
    • Dasmahapatra, B.1    Chakraburtty, K.2
  • 17
    • 0027182421 scopus 로고
    • Translation elongation factor 3: A fungus-specific translation factor?
    • Belfield,G.P. and Tuite,M.F. (1993) Translation elongation factor 3: A fungus-specific translation factor? Mol. Microbiol., 9, 411-418.
    • (1993) Mol. Microbiol , vol.9 , pp. 411-418
    • Belfield, G.P.1    Tuite, M.F.2
  • 18
    • 0023644923 scopus 로고
    • Isolation of the yeast gene encoding elongation factor 3 for protein synthesis
    • Qin,S.L., Moldave,K. and McLaughlin,C.S. (1987) Isolation of the yeast gene encoding elongation factor 3 for protein synthesis. J. Biol. Chem., 262, 7802-7807.
    • (1987) J. Biol. Chem , vol.262 , pp. 7802-7807
    • Qin, S.L.1    Moldave, K.2    McLaughlin, C.S.3
  • 19
    • 0025140815 scopus 로고
    • Isolation and characterization of the structural gene encoding elongation factor 3
    • Sandbaken,M., Lupisella,J.A., DiDomenico,B. and Chakraburtty,K. (1990) Isolation and characterization of the structural gene encoding elongation factor 3. Biochim. Biophys. Acta, 1050, 230-234.
    • (1990) Biochim. Biophys. Acta , vol.1050 , pp. 230-234
    • Sandbaken, M.1    Lupisella, J.A.2    DiDomenico, B.3    Chakraburtty, K.4
  • 20
    • 0022851642 scopus 로고
    • Intrinsic ATPase activity of yeast peptide chain elongation factor 3 (EF-3) and its direct interaction with various nucleotides
    • Miyazaki,M., Uritani,M. and Kagiyama,H. (1986) Intrinsic ATPase activity of yeast peptide chain elongation factor 3 (EF-3) and its direct interaction with various nucleotides. Nucleic Acids Symp. Ser., 17, 171-174.
    • (1986) Nucleic Acids Symp. Ser , vol.17 , pp. 171-174
    • Miyazaki, M.1    Uritani, M.2    Kagiyama, H.3
  • 21
    • 0024083552 scopus 로고
    • The yeast peptide elongation factor 3 (EF-3) carries an active site for ATP hydrolysis which can interact with various nucleoside triphosphates in the absence of ribosomes
    • Miyazaki,M., Uritani,M. and Kagiyama,H. (1988) The yeast peptide elongation factor 3 (EF-3) carries an active site for ATP hydrolysis which can interact with various nucleoside triphosphates in the absence of ribosomes. J. Biochem., 104, 445-450.
    • (1988) J. Biochem , vol.104 , pp. 445-450
    • Miyazaki, M.1    Uritani, M.2    Kagiyama, H.3
  • 22
    • 0024437753 scopus 로고
    • Role of yeast elongation factor 3 in the elongation cycle
    • Kamath,A. and Chakraburtty,K. (1989) Role of yeast elongation factor 3 in the elongation cycle. J. Biol. Chem., 264, 15423-15428.
    • (1989) J. Biol. Chem , vol.264 , pp. 15423-15428
    • Kamath, A.1    Chakraburtty, K.2
  • 23
    • 0029154909 scopus 로고
    • The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor
    • Triana-Alonso,F.J., Chakraburtty,K. and Nierhaus,K.H. (1995) The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor. J. Biol. Chem., 270, 20473-20478.
    • (1995) J. Biol. Chem , vol.270 , pp. 20473-20478
    • Triana-Alonso, F.J.1    Chakraburtty, K.2    Nierhaus, K.H.3
  • 24
    • 0030891728 scopus 로고    scopus 로고
    • Functional subdomains of yeast elongation factor 3. Localization of ribosome-binding domain
    • Kambampati,R. and Chakraburtty,K. (1997) Functional subdomains of yeast elongation factor 3. Localization of ribosome-binding domain. J. Biol. Chem., 272, 6377-6381.
    • (1997) J. Biol. Chem , vol.272 , pp. 6377-6381
    • Kambampati, R.1    Chakraburtty, K.2
  • 25
    • 0037470057 scopus 로고    scopus 로고
    • Functional interactions between yeast translation elongation factor (eEF) 1A and eEF3
    • Anand,M., Chakraburtty,K., Marton,M.J., Hinnebusch,A.G. and Kinzy,T.G. (2003) Functional interactions between yeast translation elongation factor (eEF) 1A and eEF3. J. Biol. Chem., 278, 6985-6991.
    • (2003) J. Biol. Chem , vol.278 , pp. 6985-6991
    • Anand, M.1    Chakraburtty, K.2    Marton, M.J.3    Hinnebusch, A.G.4    Kinzy, T.G.5
  • 26
    • 33845926808 scopus 로고    scopus 로고
    • Domain and nucleotide dependence of the interaction between Saccharomyces cerevisiae translation elongation factors 3 and 1A
    • Anand,M., Balar,B., Ulloque,R., Gross,S.R. and Kinzy,T.G. (2006) Domain and nucleotide dependence of the interaction between Saccharomyces cerevisiae translation elongation factors 3 and 1A. J. Biol. Chem. 281, 32318-32326.
    • (2006) J. Biol. Chem , vol.281 , pp. 32318-32326
    • Anand, M.1    Balar, B.2    Ulloque, R.3    Gross, S.R.4    Kinzy, T.G.5
  • 28
    • 0030881688 scopus 로고    scopus 로고
    • Three Ever Shorter Telomere (EST) genes are dispensable for in vitro yeast telomerase activity
    • Lingner,J., Cech,T.R., Hughes,T.R. and Lundblad,V. (1997) Three Ever Shorter Telomere (EST) genes are dispensable for in vitro yeast telomerase activity. Proc. Natl Acad. Sci. USA, 94, 11190-11195.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11190-11195
    • Lingner, J.1    Cech, T.R.2    Hughes, T.R.3    Lundblad, V.4
  • 30
    • 0031000833 scopus 로고    scopus 로고
    • Ribosomal protein L32 of Saccharomyces cerevisiae influences both the splicing of its own transcript and the processing of rRNA
    • Vilardell,J. and Warner,J. (1997) Ribosomal protein L32 of Saccharomyces cerevisiae influences both the splicing of its own transcript and the processing of rRNA. Mol. Cell Biol., 17, 1959-1965.
    • (1997) Mol. Cell Biol , vol.17 , pp. 1959-1965
    • Vilardell, J.1    Warner, J.2
  • 31
    • 0033569767 scopus 로고    scopus 로고
    • Mutations in a GTP-binding motif of eukaryotic elongation factor 1A reduce both translational fidelity and the requirement for nucleotide exchange
    • Carr-Schmid,A., Durko,N., Cavallius,J., Merrick,W.C. and Kinzy,T.G. (1999) Mutations in a GTP-binding motif of eukaryotic elongation factor 1A reduce both translational fidelity and the requirement for nucleotide exchange. J. Biol. Chem., 274, 30297-30302.
    • (1999) J. Biol. Chem , vol.274 , pp. 30297-30302
    • Carr-Schmid, A.1    Durko, N.2    Cavallius, J.3    Merrick, W.C.4    Kinzy, T.G.5
  • 32
    • 41149135521 scopus 로고    scopus 로고
    • rRNA mutants in the yeast peptidyltransferase center reveal allosteric information networks and mechanism of drug resistance
    • Rakauskaite,R. and Dinman,J.D. (2008) rRNA mutants in the yeast peptidyltransferase center reveal allosteric information networks and mechanism of drug resistance. Nucleic Acids Res., 36, 1497-1507.
    • (2008) Nucleic Acids Res , vol.36 , pp. 1497-1507
    • Rakauskaite, R.1    Dinman, J.D.2
  • 33
    • 0035838497 scopus 로고    scopus 로고
    • Yeast ribosomal protein deletion mutants possess altered peptidyltransferase activity and different sensitivity to cycloheximide
    • Dresios,J., Panopoulos,P., Frantziou,C.P. and Synetos,D. (2001) Yeast ribosomal protein deletion mutants possess altered peptidyltransferase activity and different sensitivity to cycloheximide. Biochemistry, 40, 8101-8108.
    • (2001) Biochemistry , vol.40 , pp. 8101-8108
    • Dresios, J.1    Panopoulos, P.2    Frantziou, C.P.3    Synetos, D.4
  • 34
    • 0034704217 scopus 로고    scopus 로고
    • The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit
    • Brodersen,D.E., Clemons,W.M., Carter,A.P., Morgan-Warren,R.J., Wimberly,B.T. and Ramakrishnan,V. (2000) The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit. Cell, 103, 1143-1154.
    • (2000) Cell , vol.103 , pp. 1143-1154
    • Brodersen, D.E.1    Clemons, W.M.2    Carter, A.P.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 35
    • 0034886697 scopus 로고    scopus 로고
    • Crystal structure of paromomycin docked into the eubacterial ribosomal decoding A site
    • Vicens,Q. and Westhof,E. (2001) Crystal structure of paromomycin docked into the eubacterial ribosomal decoding A site. Structure, 9 647-658.
    • (2001) Structure , vol.9 , pp. 647-658
    • Vicens, Q.1    Westhof, E.2
  • 36
    • 0003086056 scopus 로고
    • Regulation of elongation rate
    • Traschel,H, ed, CRC Press, Boca Raton, FL, pp
    • Spirin,A.S. and Ryazanov,A.G. (1991) Regulation of elongation rate. In Traschel,H. (ed.), Translation in Eukaryotes. CRC Press, Boca Raton, FL, pp. 325-350.
    • (1991) Translation in Eukaryotes , pp. 325-350
    • Spirin, A.S.1    Ryazanov, A.G.2
  • 38
    • 65549167195 scopus 로고    scopus 로고
    • Hypusine-containing protein eIF5A promotes translation elongation
    • Saini,P., Eyler,D.E., Green,R. and Dever,T.E. (2009) Hypusine-containing protein eIF5A promotes translation elongation. Nature, 459, 118-121.
    • (2009) Nature , vol.459 , pp. 118-121
    • Saini, P.1    Eyler, D.E.2    Green, R.3    Dever, T.E.4
  • 39
    • 36248983727 scopus 로고    scopus 로고
    • Roles of the negatively charged N-terminal extension of Saccharomyces cerevisiae ribosomal protein S5 revealed by characterization of a yeast strain containing human ribosomal protein S5
    • Galkin,O., Bentley,A.A., Gupta,S., Compton,B., Mazumder,B., Kinzy,T.G., Merrick,W.C., Hatzoglou,M., Pestova,T.V., Hellen,C.U.T. et al. (2007) Roles of the negatively charged N-terminal extension of Saccharomyces cerevisiae ribosomal protein S5 revealed by characterization of a yeast strain containing human ribosomal protein S5. RNA, 13, 2116-2128.
    • (2007) RNA , vol.13 , pp. 2116-2128
    • Galkin, O.1    Bentley, A.A.2    Gupta, S.3    Compton, B.4    Mazumder, B.5    Kinzy, T.G.6    Merrick, W.C.7    Hatzoglou, M.8    Pestova, T.V.9    Hellen, C.U.T.10
  • 41
    • 0040837015 scopus 로고    scopus 로고
    • Identification of elongation factor 2 as the essential protein targeted by sordarins in Candida albicans
    • Dominguez,J.M. and Martin,J.J. (1998) Identification of elongation factor 2 as the essential protein targeted by sordarins in Candida albicans. Antimicrob. Agents Chemother., 42, 2279-2283.
    • (1998) Antimicrob. Agents Chemother , vol.42 , pp. 2279-2283
    • Dominguez, J.M.1    Martin, J.J.2
  • 42
    • 0029166173 scopus 로고
    • Mutations in the elongation factor 2 gene which confer resistance to diphtheria toxin and Pseudomonas exotoxin A. Genetic and biochemical analyses
    • Foley,B.T., Moehring,J.M. and Moehring,T.J. (1995) Mutations in the elongation factor 2 gene which confer resistance to diphtheria toxin and Pseudomonas exotoxin A. Genetic and biochemical analyses. J. Biol. Chem., 270, 23218-23225.
    • (1995) J. Biol. Chem , vol.270 , pp. 23218-23225
    • Foley, B.T.1    Moehring, J.M.2    Moehring, T.J.3
  • 43
    • 0032488918 scopus 로고    scopus 로고
    • Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis
    • Justice,M.C., Hsu,M.J., Tse,B., Ku,T., Balkovec,J., Schmatz,D. and Nielsen,J. (1998) Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis. J. Biol. Chem., 273, 3148-3151.
    • (1998) J. Biol. Chem , vol.273 , pp. 3148-3151
    • Justice, M.C.1    Hsu, M.J.2    Tse, B.3    Ku, T.4    Balkovec, J.5    Schmatz, D.6    Nielsen, J.7
  • 44
    • 0038433302 scopus 로고    scopus 로고
    • An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation
    • Savelsbergh,A., Katunin,V.I., Mohr,D., Peske,F., Rodnina,M.V. and Wintermeyer,W. (2003) An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation. Mol. Cell, 11 1517-1523.
    • (2003) Mol. Cell , vol.11 , pp. 1517-1523
    • Savelsbergh, A.1    Katunin, V.I.2    Mohr, D.3    Peske, F.4    Rodnina, M.V.5    Wintermeyer, W.6
  • 45
    • 20444393817 scopus 로고    scopus 로고
    • Guanine-nucleotide exchange on ribosome-bound elongation factor G initiates the translocation of tRNAs
    • Zavialov,A.V., Hauryliuk,V.V. and Ehrenberg,M. (2005) Guanine-nucleotide exchange on ribosome-bound elongation factor G initiates the translocation of tRNAs. J. Biol., 4, 9-14.
    • (2005) J. Biol , vol.4 , pp. 9-14
    • Zavialov, A.V.1    Hauryliuk, V.V.2    Ehrenberg, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.