Valine114 Replacements In The Archaeal Elongation Factor 1a Enhanced Its Ability To Interact With Aminoacyl-Trna And Kirromycin(274 views visite) Masullo M, Cantiello P, Paola B, Fiengo A, Vitagliano L, Zagari A, Arcari P
Dipto. di Scienze Farmacobiologiche, Univ. di Catanzaro Magna Graecia, Roccelletta di Borgia, 1-88021 Catanzaro, Italy Dipto. Biochimica e Biotecnol. Med., Universita di Napoli Federico II, CEINGE Biotecnologie Avanzate Scarl, via S. Pansini 5, 1-80131 Napoli, Italy Ist. di Biostrutture e Bioimmagini, CNR, Departimento di Chimica Biologica, Via Mezzocannone 6, 1-80134 Napoli, Italy
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Valine114 Replacements In The Archaeal Elongation Factor 1a Enhanced Its Ability To Interact With Aminoacyl-Trna And Kirromycin
Valine 114 in the D109AAILVVA sequence of elongation factor 1α from the archaeon Sulfolobus solfataricus (SsEF-1α) was substituted with an acidic (V114E), basic (V114K), or cavity-forming (V114A) residue, and the effects on the biochemical properties of the factor were investigated. This sequence is well-conserved among most of eukaryal and eubacterial counterparts, and in the three-dimensional structure of SsEF-1α, V114 is located in a hydrophobic pocket near the first GDP-binding consensus sequence G13XXXXGK[T,S] [Vitagliano, L., Masullo, M., Sica, F., Zagari, A., and Bocchini, V. (2001) EMBO J. 20, 5305-5311]. These mutants displayed functions absent in the wild-type factor. In fact, although they exhibited a rate in poly(Phe) incorporation almost identical to that of SsEF-1α V114K, and V114A exhibited an affinity for GDP and GTP higher and a capability to bind heterologous aa-tRNA stronger than that elicited by SsEF-1α but similar to that of eubacterial EF-Tu. V114E instead displayed not only a weaker binding capability for aa-tRNA but also a lower affinity for GDP. The intrinsic GTPase activity of V114E was drastically reduced compared to those of SsEF-1α, V114K, and V114A. Interestingly, the decreased intrinsic GTPase activity of V114E was partially restored by kirromycin, an effect already observed for the G13A mutant of SsEF-1α [Masullo, M., Cantiello, P., de Paola, B., Catanzano, F., Arcari, P., and Bocchini, V. (2002) Biochemistry 41, 628-633]. Finally, the V114A substitution showed only a marginal effect on both the thermostability and thermophilicity of SsEF-1α, whereas V114K and V114E replacements strongly destabilized the molecule.
Valine114 Replacements In The Archaeal Elongation Factor 1a Enhanced Its Ability To Interact With Aminoacyl-Trna And Kirromycin
Kim YH, Shin SW, Pellicano R, Fagoonee S, Choi IJ, Kim YI, Park B, Choi JM, Kim SG, Choi J, Park JY, Oh S, Yang HJ, Lim JH, Im JP, Kim JS, Jung HC, Ponzetto A, Figura N, Malfertheiner P, Choi IJ, Kook MC, Kim YI, Cho SJ, Lee JY, Kim CG, Park B, Nam BH, Bae SE, Choi KD, Choe J, Kim SO, Na HK, Choi JY, Ahn JY, Jung KW, Lee J, Kim DH, Chang HS, Song HJ, Lee GH, Jung HY, Seta T, Takahashi Y, Noguchi Y, Shikata S, Sakai T, Sakai K, Yamashita Y, Nakayama T, Leja M, Park JY, Murillo R, Liepniece-karele I, Isajevs S, Kikuste I, Rudzite D, Krike P, Parshutin S, Polaka I, Kirsners A, Santare D, Folkmanis V, Daugule I, Plummer M, Herrero R, Tsukamoto T, Nakagawa M, Kiriyama Y, Toyoda T, Cao X, Corral JE, Mera R, Dye CW, Morgan DR, Lee YC, Lin JT, Garcia Martin R, Matia Cubillo A, Lee SH, Park JM, Han YM, Ko WJ, Hahm KB, Leontiadis GI, Ford AC, Ichinose M, Sugano K, Jeong M, Park JM, Han YM, Park KY, Lee DH, Yoo JH, Cho JY, Hahm KB, Bang CS, Baik GH, Shin IS, Kim JB, Suk KT, Yoon JH, Kim YS, Kim DJ * Helicobacter pylori Eradication for Prevention of Metachronous Recurrence after Endoscopic Resection of Early Gastric Cancer(204 visite) N Engl J Med (ISSN: 0028-4793, 0028-4793linking, 1533-4406electronic), 2015 Jun; 30642104201566393291: 749-756. Impact Factor:59.558 DettagliEsporta in BibTeXEsporta in EndNote
283 Records (281 escludendo Abstract e Conferenze). Impact factor totale: 1107.873 (1099.792 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 1112.714 (1104.087 escludendo Abstract e Conferenze).
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