Zaloguj się

Gotowe bibliografie tematyczne / TRNAfMet

Spis treści

Artykuły w czasopismach

Gotowa bibliografia na temat „TRNAfMet”

Autor: Grafiati

Data publikacji: 6 września 2023

Utwórz poprawne odniesienie w stylach APA, MLA, Chicago, Harvard i wielu innych

Wybierz rodzaj źródła:

Zobacz listy aktualnych artykułów, książek, rozpraw, streszczeń i innych źródeł naukowych na temat „TRNAfMet”.

Przycisk „Dodaj do bibliografii” jest dostępny obok każdej pracy w bibliografii. Użyj go – a my automatycznie utworzymy odniesienie bibliograficzne do wybranej pracy w stylu cytowania, którego potrzebujesz: APA, MLA, Harvard, Chicago, Vancouver itp.

Możesz również pobrać pełny tekst publikacji naukowej w formacie „.pdf” i przeczytać adnotację do pracy online, jeśli odpowiednie parametry są dostępne w metadanych.

Artykuły w czasopismach na temat "TRNAfMet"

1

Steiner-Mosonyi, Marta, Carole Creuzenet, Robert A. B. Keates, Benjamin R. Strub, and Dev Mangroo. "ThePseudomonas aeruginosaInitiation Factor IF-2 Is Responsible for Formylation-independent Protein Initiation inP. aeruginosa." Journal of Biological Chemistry 279, no. 50 (2004): 52262–69. http://dx.doi.org/10.1074/jbc.m408086200.

Pełny tekst źródła

Streszczenie:

Formylation of the initiator methionyl-tRNA (Met-tRNAfMet) was generally thought to be essential for initiation of protein synthesis in all eubacteria based on studies conducted primarily inEscherichia coli. However, this view of eubacterial protein initiation has changed because some bacteria have been demonstrated to have the capacity to initiate protein synthesis with the unformylated Met-tRNAfMet. Here we show that thePseudomonas aeruginosainitiation factor IF-2 is required for formylation-independent protein initiation inP. aeruginosa, the first bacterium shown to have the ability to initiate protein synthesis with both the initiator formyl-methionyl-tRNA (fMet-tRNAfMet) and Met-tRNAfMet. TheE. coliIF-2, which participates exclusively in formylation-dependent protein initiation inE. coli, was unable to facilitate utilization of Met-tRNAfMetin initiation inP. aeruginosa. However, theE. coliIF-2 was made to function in formylation-independent protein initiation inP. aeruginosaby decreasing the positive charge potential of the cleft that binds the amino end of the amino acid attached to the tRNA. Furthermore increasing the positive charge potential of this cleft in theP. aeruginosaIF-2 prevented the protein from participating in formylation-independent protein initiation. Thus, this is the first demonstration of a eubacterial IF-2 with an inherent capacity to facilitate utilization of Met-tRNAfMetin protein initiation, discounting the dogma that eubacterial IF-2 can only allow the use of fMet-tRNAfMetin protein initiation. Furthermore these findings give important clues to the basis for discriminating the initiator Met-tRNA by IF-2 and for the evolution of alternative mechanisms for discrimination.

Style APA, Harvard, Vancouver, ISO itp.

2

Li, Yan, William B. Holmes, Dean R. Appling, and Uttam L. RajBhandary. "Initiation of Protein Synthesis in Saccharomyces cerevisiae Mitochondria without Formylation of the Initiator tRNA." Journal of Bacteriology 182, no. 10 (2000): 2886–92. http://dx.doi.org/10.1128/jb.182.10.2886-2892.2000.

Pełny tekst źródła

Streszczenie:

ABSTRACT Protein synthesis in eukaryotic organelles such as mitochondria and chloroplasts is widely believed to require a formylated initiator methionyl tRNA (fMet-tRNAfMet) for initiation. Here we show that initiation of protein synthesis in yeast mitochondria can occur without formylation of the initiator methionyl-tRNA (Met-tRNAfMet). The formylation reaction is catalyzed by methionyl-tRNA formyltransferase (MTF) located in mitochondria and usesN 10-formyltetrahydrofolate (10-formyl-THF) as the formyl donor. We have studied yeast mutants carrying chromosomal disruptions of the genes encoding the mitochondrial C1-tetrahydrofolate (C1-THF) synthase (MIS1), necessary for synthesis of 10-formyl-THF, and the methionyl-tRNA formyltransferase (open reading frame YBL013W; designated FMT1). A direct analysis of mitochondrial tRNAs using gel electrophoresis systems that can separate fMet-tRNAfMet, Met-tRNAfMet, and tRNAfMet shows that there is no formylation in vivo of the mitochondrial initiator Met-tRNA in these strains. In contrast, the initiator Met-tRNA is formylated in the respective “wild-type” parental strains. In spite of the absence of fMet-tRNAfMet, the mutant strains exhibited normal mitochondrial protein synthesis and function, as evidenced by normal growth on nonfermentable carbon sources in rich media and normal frequencies of generation ofpetite colonies. The only growth phenotype observed was a longer lag time during growth on nonfermentable carbon sources in minimal media for the mis1 deletion strain but not for thefmt1 deletion strain.

Style APA, Harvard, Vancouver, ISO itp.

3

Fratte, Sonia Delle, Chiara Piubelli, and Enrico Domenici. "Development of a High-Throughput Scintillation Proximity Assay for the Identification of C-Domain Translational Initiation Factor 2 Inhibitors." Journal of Biomolecular Screening 7, no. 6 (2002): 541–46. http://dx.doi.org/10.1177/1087057102238628.

Pełny tekst źródła

Streszczenie:

Translational initiation factor 2 (IF2) is the largest of the 3 factors required for translation initiation in prokaryotes and has been shown to be essential in Escherichia coli. It stimulates the binding of fMet-tRNAfMet to the 30S ribosomal subunit in the presence of GTP. The selectivity is achieved through specific recognition of the tRNAfMet blocked α-amino group. IF2 is composed of 3 structural domains: N-domain, whose function is not known; G-domain, which contains the GTP/GDP binding site and the GTPase catalytic center; and C-domain, which recognizes and binds fMet-tRNAfMet. Its activity is strictly bacteria specific and highly conserved among prokaryotes. So far, antibiotics targeting IF2 function are not known, and this makes it an ideal target for new drugs with mechanisms of resistance not yet developed. A few assays have been developed in the past, which allow the detection of IF2 activity either directly or indirectly. In both instances, the assays are based on radioactive detection and do not allow for high throughput because of the need for separation or solvent extraction steps. The authors describe a novel biochemical assay for IF2 that exploits the molecular recognition of fMet-tRNAfMet by the C-domain. The assay is based on the incubation of biotinyl-IF2 with fMet-tRNAfMet and the subsequent capture of the radiolabeled complex by streptavidin-coated beads, exploiting the scintillation proximity assay (SPA) technology. The assay has been designed in an automatable, homogeneous, miniaturized fashion suitable for high-throughput screening and is rapid, sensitive, and robust to dimethyl sulfoxide (DMSO) up to 10% v/v. The assay, used to screen a limited chemical collection of about 5000 compounds and a subset of compounds originated by a 2-D substructural search, has shown to be able to detect potential IF2 inhibitors.

Style APA, Harvard, Vancouver, ISO itp.

4

Schmitt, Emmanuelle, Michel Panvert, Sylvain Blanquet, and Yves Mechulam. "Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet." EMBO Journal 17, no. 23 (1998): 6819–26. http://dx.doi.org/10.1093/emboj/17.23.6819.

Pełny tekst źródła

Style APA, Harvard, Vancouver, ISO itp.

5

Polishchuk, L. V. "Nucleotide sequences of tRNA-methonine genes of Streptomyces globisporus 1912-2, identified in silico." Visnik ukrains'kogo tovaristva genetikiv i selekcioneriv 14, no. 1 (2016): 58–62. http://dx.doi.org/10.7124/visnyk.utgis.14.1.545.

Pełny tekst źródła

Streszczenie:

Aim of this work was to identify nucleotide sequences of tRNAMet of S. globisporus 1912-2. Methods. Resources of server NCBI (programs BLAST: blast, discontiguous megablast and databases: “Genome”, “Nucleotide”) were used for in silico analysis of library of S. grlobisporus 1912-2 contigs. Results. Nucleotide sequences of 4 genes of tRNAMet of S. globisporus 1912-2 were determined in silico. Molecules of tRNA of the II type were translated from tRNAMet gene (Contig No 21 (936–1008 bp)) and the molecules of tRNAfMet genes (Contigs No 299 (1713–1787 bp), No 255 (5941–6015 bp)). Conclusions. 4 genes of transfer RNAs-methionine were identified in silico in S. globisporus 1912-2 genome. Two genes from them coded tRNAfMet molecules. The nucleotide sequences of all tRNAMet genes were identified.Keywords: gene, tRNA, methionine, nucleotide sequence, Streptomyces.

Style APA, Harvard, Vancouver, ISO itp.

6

Nomura, Teruaki, Nobuyuki Fujita, and Akira Ishihama. "Promoter selectivity ofEscherichia coliRNA polymerase: alteration by fMet-tRNAfMet." Nucleic Acids Research 14, no. 17 (1986): 6857–70. http://dx.doi.org/10.1093/nar/14.17.6857.

Pełny tekst źródła

Style APA, Harvard, Vancouver, ISO itp.

7

Rodnina, M. V., Y. P. Semenkov, and W. Wintermeyer. "Purification of fMET-tRNAfMET by Fast Protein Liquid Chromatography." Analytical Biochemistry 219, no. 2 (1994): 380–81. http://dx.doi.org/10.1006/abio.1994.1282.

Pełny tekst źródła

Style APA, Harvard, Vancouver, ISO itp.

8

Ferguson, Blair Q., and David C. H. Yang. "Topographic modeling of free and methionyl-tRNA synthetase-bound tRNAfMet by singlet-singlet energy transfer: bending of the 3'-terminal arm in tRNAfMet." Biochemistry 25, no. 21 (1986): 6572–78. http://dx.doi.org/10.1021/bi00369a035.

Pełny tekst źródła

Style APA, Harvard, Vancouver, ISO itp.

9

Duroc, Yann, Carmela Giglione, and Thierry Meinnel. "Mutations in Three Distinct Loci Cause Resistance to Peptide Deformylase Inhibitors in Bacillus subtilis." Antimicrobial Agents and Chemotherapy 53, no. 4 (2009): 1673–78. http://dx.doi.org/10.1128/aac.01340-08.

Pełny tekst źródła

Streszczenie:

ABSTRACT Bacillus subtilis mutants with resistance against peptide deformylase inhibitors were isolated. All showed a bypass of the pathway through mutations in three genes required for formylation of Met-tRNAfMet, fmt, folD, and glyA. glyA corresponds to a yet uncharacterized locus inducing resistance. The bypass of formylation caused robust fitness reduction but was not accompanied by alterations of the transcription profile. A subtle adaptation of the enzymes of the intermediary metabolism was observed.

Style APA, Harvard, Vancouver, ISO itp.

10

Guenneugues, Marc, Enrico Caserta, Letizia Brandi, et al. "Mapping the fMet-tRNAfMet binding site of initiation factor IF2." EMBO Journal 19, no. 19 (2000): 5233–40. http://dx.doi.org/10.1093/emboj/19.19.5233.

Pełny tekst źródła

Style APA, Harvard, Vancouver, ISO itp.

Więcej źródeł

Oferujemy zniżki na wszystkie plany premium dla autorów, których prace zostały uwzględnione w tematycznych zestawieniach literatury. Skontaktuj się z nami, aby uzyskać unikalny kod promocyjny!