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Page 1
[Elongation Factor P: New Mechanisms of Function and an Evolutionary Diversity of Translation Regulation].
Golubev AA, Validov SZ, Usachev KS, Yusupov MM. Golubev AA, et al. Mol Biol (Mosk). 2019 Jul-Aug;53(4):561-573. doi: 10.1134/S0026898419040037. Mol Biol (Mosk). 2019. PMID: 31397432 Free article. Review. Russian.
The protein synthesis in cells occurs in ribosomes, with the involvement of protein translational factors. One of these translational factors is the elongation factor P (EF-P). EF-P is a three-domain protein that binds between the P and E sites of the …
The protein synthesis in cells occurs in ribosomes, with the involvement of protein translational factors. One of these translational …
Translation elongation factor 3: a fungus-specific translation factor?
Belfield GP, Tuite MF. Belfield GP, et al. Mol Microbiol. 1993 Aug;9(3):411-8. doi: 10.1111/j.1365-2958.1993.tb01702.x. Mol Microbiol. 1993. PMID: 8412690 Review.
Fungi appear to be unique in their requirement for a third soluble translation elongation factor. This factor, designated elongation factor 3 (EF-3), was first described in the yeast Saccharomyces cerevisiae and has subsequently been identified …
Fungi appear to be unique in their requirement for a third soluble translation elongation factor. This factor, designat …
Cellular ADP-ribosylation of elongation factor 2.
Iglewski WJ. Iglewski WJ. Mol Cell Biochem. 1994 Sep;138(1-2):131-3. doi: 10.1007/BF00928454. Mol Cell Biochem. 1994. PMID: 7898455 Review.
The enzyme transfers ADP-ribose from NAD to elongation factor 2, inactivating the factor and thus inhibiting in vitro protein synthesis. ...The endogenously ADP-ribosylated EF-2 has been detected by a variety of methods including two-dimensional electrophores …
The enzyme transfers ADP-ribose from NAD to elongation factor 2, inactivating the factor and thus inhibiting in vitro p …
Posttranslational modification of Elongation Factor P from Staphylococcus aureus.
Golubev A, Negroni L, Krasnovid F, Validov S, Yusupova G, Yusupov M, Usachev K. Golubev A, et al. FEBS Open Bio. 2020 Jul;10(7):1342-1347. doi: 10.1002/2211-5463.12901. Epub 2020 Jun 16. FEBS Open Bio. 2020. PMID: 32436337 Free PMC article.
Antibiotic-resistant Staphylococcus aureus is becoming a major burden on health care systems in many countries, necessitating the identification of new targets for antibiotic development. Elongation Factor P (EF-P) is a highly conserved elongation protein …
Antibiotic-resistant Staphylococcus aureus is becoming a major burden on health care systems in many countries, necessitating the identifica …
Eukaryotic translation elongation factor 1 alpha: structure, expression, functions, and possible role in aminoacyl-tRNA channeling.
Negrutskii BS, El'skaya AV. Negrutskii BS, et al. Prog Nucleic Acid Res Mol Biol. 1998;60:47-78. doi: 10.1016/s0079-6603(08)60889-2. Prog Nucleic Acid Res Mol Biol. 1998. PMID: 9594571 Review.
This review offers a comprehensive analysis of eukaryotic translation elongation factor 1 (eEF-1 alpha) in comparison with its bacterial counterpart EF-Tu. Altogether, the data presented indicate some variances in the elongation process in prokaryotes and euk …
This review offers a comprehensive analysis of eukaryotic translation elongation factor 1 (eEF-1 alpha) in comparison with its …
The interaction between RNA polymerase and the elongation factor NusA.
Yang X, Lewis PJ. Yang X, et al. RNA Biol. 2010 May-Jun;7(3):272-5. doi: 10.4161/rna.7.3.12021. Epub 2010 May 7. RNA Biol. 2010. PMID: 20458190 Free article. Review.
The synthesis of RNA is highly regulated at all stages by transcription factors. As an essential transcription elongation factor, NusA has been studied biochemically for more than 30 years. ...The resulting model of RNA polymerase in complex with NusA has she …
The synthesis of RNA is highly regulated at all stages by transcription factors. As an essential transcription elongation f
Structural insights of the elongation factor EF-Tu complexes in protein translation of Mycobacterium tuberculosis.
Zhan B, Gao Y, Gao W, Li Y, Li Z, Qi Q, Lan X, Shen H, Gan J, Zhao G, Li J. Zhan B, et al. Commun Biol. 2022 Oct 3;5(1):1052. doi: 10.1038/s42003-022-04019-y. Commun Biol. 2022. PMID: 36192483 Free PMC article.
Tuberculosis (TB) caused by Mycobacterium tuberculosis (Mtb) is the second-deadliest infectious disease worldwide. Emerging evidence shows that the elongation factor EF-Tu could be an excellent target for treating Mtb infection. Here, we report the crystal structure …
Tuberculosis (TB) caused by Mycobacterium tuberculosis (Mtb) is the second-deadliest infectious disease worldwide. Emerging evidence shows t …
A novel function for eukaryotic elongation factor 3: Inhibition of stop codon readthrough in yeast.
Kobayashi S, Kaji A, Kaji H. Kobayashi S, et al. Arch Biochem Biophys. 2023 May 15;740:109580. doi: 10.1016/j.abb.2023.109580. Epub 2023 Mar 21. Arch Biochem Biophys. 2023. PMID: 36948349
Eukaryotic elongation factor 3 (eEF3) is one of the essential yeast ribosome-associated ATP-binding cassette type F (ABCF) ATPases. ...When eEF3 was partially removed from the crude extract, the product from the downstream ORF was increased by the readthrough of a U …
Eukaryotic elongation factor 3 (eEF3) is one of the essential yeast ribosome-associated ATP-binding cassette type F (ABCF) ATP …
Structure and Function of an Elongation Factor P Subfamily in Actinobacteria.
Pinheiro B, Scheidler CM, Kielkowski P, Schmid M, Forné I, Ye S, Reiling N, Takano E, Imhof A, Sieber SA, Schneider S, Jung K. Pinheiro B, et al. Cell Rep. 2020 Mar 31;30(13):4332-4342.e5. doi: 10.1016/j.celrep.2020.03.009. Cell Rep. 2020. PMID: 32234471 Free article.
Translation of consecutive proline motifs causes ribosome stalling and requires rescue via the action of a specific translation elongation factor, EF-P in bacteria and archaeal/eukaryotic a/eIF5A. In Eukarya, Archaea, and all bacteria investigated so far, the functi …
Translation of consecutive proline motifs causes ribosome stalling and requires rescue via the action of a specific translation elongatio
23,600 results
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