Experts and Doctors on peptide elongation factors in Denmark

Summary

Locale: Denmark
Topic: peptide elongation factors

Top Publications

  1. Muller S, Sandal T, Kamp Hansen P, Dalbøge H. Comparison of expression systems in the yeasts Saccharomyces cerevisiae, Hansenula polymorpha, Klyveromyces lactis, Schizosaccharomyces pombe and Yarrowia lipolytica. Cloning of two novel promoters from Yarrowia lipolytica. Yeast. 1998;14:1267-83 pubmed
    ..Based on the present tests of the new promoters. Y. lipolytica appears as a highly attractive alternative to S. cerevisiae as a host organism for expression cloning. ..
  2. Nilsson J, Nissen P. Elongation factors on the ribosome. Curr Opin Struct Biol. 2005;15:349-54 pubmed
    ..A model emerges of the specific routes of conformational changes mediated by tRNA and the ribosome that trigger the GTPase activity of the elongation factors on the ribosome. ..
  3. Steffensen L, Pedersen P. Heterologous expression of membrane and soluble proteins derepresses GCN4 mRNA translation in the yeast Saccharomyces cerevisiae. Eukaryot Cell. 2006;5:248-61 pubmed
    ..The increase in Gcn4p density in response to heterologous expression did not induce transcription from the HIS4 promoter, a traditional Gcn4p target. ..
  4. Andersen C, Anand M, Boesen T, Van L, Kinzy T, Andersen G. Purification and crystallization of the yeast translation elongation factor eEF3. Acta Crystallogr D Biol Crystallogr. 2004;60:1304-7 pubmed
    ..3 A. A density-modified map derived from low-resolution SIRAS phases allows model building. ..
  5. Nyborg J, Liljas A. Protein biosynthesis: structural studies of the elongation cycle. FEBS Lett. 1998;430:95-9 pubmed
    ..In addition, electron cryomicroscopy studies of ribosomes with tRNA as well as the ternary complex bound are beginning to give a solid structural basis for the functional description of elongation. ..
  6. Mansilla F, Friis I, Jadidi M, Nielsen K, Clark B, Knudsen C. Mapping the human translation elongation factor eEF1H complex using the yeast two-hybrid system. Biochem J. 2002;365:669-76 pubmed
    ..These units can dimerize via eEF1B beta. Our model is compared with other models, and structural as well as functional aspects of the model are discussed. ..
  7. Frydenberg J, Poulsen K, Petersen A, Lund A, Olesen O. Isolation and characterization of the gene encoding EF-1 alpha O, an elongation factor 1-alpha expressed during early development of Xenopus laevis. Gene. 1991;109:185-92 pubmed
    ..The first intron contains G + C-rich elements which exist both isolated and as part of longer inverted repeats. Furthermore, one octamer and four Sp1-binding sites are found in this intron. ..
  8. Karring H, Bjornsson A, Thirup S, Clark B, Knudsen C. Functional effects of deleting the coiled-coil motif in Escherichia coli elongation factor Ts. Eur J Biochem. 2003;270:4294-305 pubmed
    ..The present results also indicate that the deletion alters the competition between EF-Ts and kirromycin for the binding to EF-Tu. ..
  9. Kristensen P, Lund A, Clark B, Cavallius J, Merrick W. Purification and characterisation of a tissue specific elongation factor 1 alpha (EF-1 alpha 2) from rabbit muscle. Biochem Biophys Res Commun. 1998;245:810-4 pubmed

More Information

Publications27

  1. Coppard N, Poulsen K, Madsen H, Frydenberg J, Clark B. 42Sp48 in previtellogenic Xenopus oocytes is structurally homologous to EF-1 alpha and may be a stage-specific elongation factor. J Cell Biol. 1991;112:237-43 pubmed
    ..coli, for which the three-dimensional structure including that of the GTP binding sites have been determined, supports this hypothesis. ..
  2. Madsen H, Poulsen K, Dahl O, Clark B, Hjorth J. Retropseudogenes constitute the major part of the human elongation factor 1 alpha gene family. Nucleic Acids Res. 1990;18:1513-6 pubmed
    ..The others appeared to be retropseudogenes. EF-1 alpha retropseudogenes were also found to be abundant in the mammalian species mouse and pig, while the chicken contained only one presumably active EF-1 alpha gene. ..
  3. Vogel U, Jensen K. NusA is required for ribosomal antitermination and for modulation of the transcription elongation rate of both antiterminated RNA and mRNA. J Biol Chem. 1997;272:12265-71 pubmed
    ..These results suggest that NusA is the component of the transcription elongation complex required for inhibition of mRNA elongation by ppGpp. ..
  4. Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark B, et al. Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science. 1995;270:1464-72 pubmed
    ..The overall shape of the ternary complex is similar to that of the translocation factor, EF-G-GDP, and this suggests a novel mechanism involving "molecular mimicry" in the translational apparatus. ..
  5. Huang L, Vanstone M, Hartley T, Osmond M, Barrowman N, Allanson J, et al. Mandibulofacial Dysostosis with Microcephaly: Mutation and Database Update. Hum Mutat. 2016;37:148-54 pubmed publisher
    ..All reported EFTUD2 mutations can be found in the EFTUD2 mutation database (http://databases.lovd.nl/shared/genes/EFTUD2). ..
  6. Kidmose R, Vasiliev N, Chetverin A, Andersen G, Knudsen C. Structure of the Qbeta replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins. Proc Natl Acad Sci U S A. 2010;107:10884-9 pubmed publisher
    ..The evolution of resistance by the host appears to be impaired because of the interactions of the beta-subunit with parts of EF-Tu essential in recognition of aminoacyl-tRNA...
  7. Andersen C, Becker T, Blau M, Anand M, Halic M, Balar B, et al. Structure of eEF3 and the mechanism of transfer RNA release from the E-site. Nature. 2006;443:663-8 pubmed
    ..eEF3 uses an entirely new factor binding site near the ribosomal E-site, with the chromodomain likely to stabilize the ribosomal L1 stalk in an open conformation, thus allowing tRNA release. ..
  8. Andersen J, Jensen K, Poulsen P. Role of transcription pausing in the control of the pyrE attenuator in Escherichia coli. Mol Microbiol. 1991;5:327-33 pubmed
  9. Jeppesen M, Navratil T, Spremulli L, Nyborg J. Crystal structure of the bovine mitochondrial elongation factor Tu.Ts complex. J Biol Chem. 2005;280:5071-81 pubmed
    ..The structure of the EF-Tumt.Tsmt complex provides new insights into the nucleotide exchange mechanism and provides a framework for explaining much of the mutational data obtained for this complex. ..
  10. Sørensen H, Sperling Petersen H, Mortensen K. A favorable solubility partner for the recombinant expression of streptavidin. Protein Expr Purif. 2003;32:252-9 pubmed
    ..coli. ..
  11. Karring H, Mathu S, van Duin J, Clark B, Kraal B, Knudsen C. Qbeta-phage resistance by deletion of the coiled-coil motif in elongation factor Ts. J Biol Chem. 2004;279:1878-84 pubmed
    ..We propose that the role of EF-Ts in the Qbeta-polymerase complex is to control and trap EF-Tu in a stable conformation with affinity for RNA templates while unable to bind aminoacyl-tRNA. ..
  12. Andersen G, Nissen P, Nyborg J. Elongation factors in protein biosynthesis. Trends Biochem Sci. 2003;28:434-41 pubmed
    ..Very recent structures of the yeast translocation factor and its complex with the antifungal drug sordarin reveal an unexpected conformational flexibility that might be crucial to the mechanism of translocation. ..
  13. Karring H, Andersen G, Thirup S, Nyborg J, Spremulli L, Clark B. Isolation, crystallisation, and preliminary X-ray analysis of the bovine mitochondrial EF-Tu:GDP and EF-Tu:EF-Ts complexes. Biochim Biophys Acta. 2002;1601:172-7 pubmed
    ..78 A, c=128.89 A and beta=96.978 degrees. The crystals of the homologous mitochondrial EF-Tu:EF-Ts complex diffract to 4 A and belong to space group C2 with cell parameters a=157.7 A, b=151.9 A, c=156.9 A, and beta=108.96 degrees. ..
  14. Knudsen S, Frydenberg J, Clark B, Leffers H. Tissue-dependent variation in the expression of elongation factor-1 alpha isoforms: isolation and characterisation of a cDNA encoding a novel variant of human elongation-factor 1 alpha. Eur J Biochem. 1993;215:549-54 pubmed
    ..EF-1 alpha was expressed in brain, placenta, lung, liver, kidney, pancreas and in all the cell lines that we have analysed but barely detectable in heart and skeletal muscle. ..
  15. Nyborg J, Kjeldgaard M. Elongation in bacterial protein biosynthesis. Curr Opin Biotechnol. 1996;7:369-75 pubmed
    ..GTP and of the complex EF-Tu.EF-Ts have been determined. Within the same period, new cryo-electron microscopy reconstructions of ribosome particles have been obtained. ..
  16. Lund A, Knudsen S, Vissing H, Clark B, Tommerup N. Assignment of human elongation factor 1alpha genes: EEF1A maps to chromosome 6q14 and EEF1A2 to 20q13.3. Genomics. 1996;36:359-61 pubmed
    ..3 by FISH. In addition, the 11 strongest cross-hybridizing loci (EEF1AL2-EEF1AL13) were mapped by FISH to 12p12, 9q34, 7p15-p21, 19q13, 3q26-q27, 7q33-q35, 1p13-p22, 2q12-q14, 5p12-q11, 1q31-q32, and Xq21. ..
  17. Kahns S, Lund A, Kristensen P, Knudsen C, Clark B, Cavallius J, et al. The elongation factor 1 A-2 isoform from rabbit: cloning of the cDNA and characterization of the protein. Nucleic Acids Res. 1998;26:1884-90 pubmed
    ..In contrast, the GDP dissociation rate constant is approximately 7 times higher for eEF1A-1 than for eEF1A-2. The nucleotide preference ratio (GDP/GTP) for eEF1A-1 was 0.82, while the preference ratio for eEF1A-2 was 1.50. ..
  18. Bøgestrand S, Wiborg O, Thirup S, Nyborg J. Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli. FEBS Lett. 1995;368:49-54 pubmed
    ..The diffraction pattern shows a pronounced pseudo-C2 symmetry at low resolution. This pseudo symmetry increases when the crystals are irradiated with X-rays for a few hours. ..