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Did you mean rtrmfo (1 results)?
TrmFO, a Fibronectin-Binding Adhesin of Mycoplasma bovis.
Guo Y, Zhu H, Wang J, Huang J, Khan FA, Zhang J, Guo A, Chen X. Guo Y, et al. Int J Mol Sci. 2017 Aug 9;18(8):1732. doi: 10.3390/ijms18081732. Int J Mol Sci. 2017. PMID: 28792486 Free PMC article.
The present study was designed to characterize the Fn-binding ability of methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (TrmFO) and its role in M. bovis cytoadherence. The trmFO (MBOV_RS00785) gene was cloned and expressed in E. coli BL21, and polyclon …
The present study was designed to characterize the Fn-binding ability of methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (Tr
The presence of adhesion factors NOX, alpha-enolase, TrmFO, P27, and VpmaX in Mycoplasma bovis wild isolates in Japan.
Shitamori F, Uemura R, Kanda T, Sueyoshi M. Shitamori F, et al. Open Vet J. 2022 Nov-Dec;12(6):782-786. doi: 10.5455/OVJ.2022.v12.i6.1. Epub 2022 Nov 3. Open Vet J. 2022. PMID: 36650870 Free PMC article.
In recent years, five new adhesins, NOX, alpha-enolase, TrmFO, P27, and VpmaX, have been reported in M. bovis strains from pneumonia cases. However, the presence of these adhesins in wild isolates has not been established. ...Specific polymerase chain reaction reactions we …
In recent years, five new adhesins, NOX, alpha-enolase, TrmFO, P27, and VpmaX, have been reported in M. bovis strains from pneumonia …
Ultrafast photoinduced flavin dynamics in the unusual active site of the tRNA methyltransferase TrmFO.
Dozova N , Lacombat F , Bou-Nader C , Hamdane D , Plaza P . Dozova N , et al. Phys Chem Chem Phys. 2019 Apr 24;21(17):8743-8756. doi: 10.1039/c8cp06072j. Phys Chem Chem Phys. 2019. PMID: 30968076
The bacterial FAD and folate-dependent tRNA methyltransferase TrmFO has the unique property of stabilizing its FAD coenzyme by an unusual H-bond-assisted pi-pi stacking interaction, involving a conserved tyrosine (Y346 in Bacillus subtilis TrmFO, BsTrmFO), the isoal …
The bacterial FAD and folate-dependent tRNA methyltransferase TrmFO has the unique property of stabilizing its FAD coenzyme by an unu …
Photochemical processes in flavo-enzymes as a probe for active site dynamics: TrmFO of Thermus thermophilus.
Zhuang B, Nag L, Sournia P, Croitoru A, Ramodiharilafy R, Lambry JC, Myllykallio H, Aleksandrov A, Liebl U, Vos MH. Zhuang B, et al. Photochem Photobiol Sci. 2021 May;20(5):663-670. doi: 10.1007/s43630-021-00052-8. Epub 2021 May 11. Photochem Photobiol Sci. 2021. PMID: 33977512
In the C51A variant of the bacterial RNA-transforming flavoenzyme TrmFO from the bacterium Thermus thermophilus, fluorescence is very short-lived (~ 1 ps), and close-by Tyr343 is known to act as the main quencher, as confirmed here by the very similar dynamics observed in …
In the C51A variant of the bacterial RNA-transforming flavoenzyme TrmFO from the bacterium Thermus thermophilus, fluorescence is very …
Consumption of N5, N10-methylenetetrahydrofolate in Thermus thermophilus under nutrient-poor condition.
Yamagami R, Miyake R, Fukumoto A, Nakashima M, Hori H. Yamagami R, et al. J Biochem. 2018 Aug 1;164(2):141-152. doi: 10.1093/jb/mvy037. J Biochem. 2018. PMID: 29538705
TrmFO catalyzes the formation of 5-methyluridine at position 54 in tRNA and uses N5, N10-methylenetetrahydrofolate (CH2THF) as the methyl group donor. ...Moreover, in vitro experiments showed that TrmFO interfered with ThyX through consumption of CH2THF. Addition of
TrmFO catalyzes the formation of 5-methyluridine at position 54 in tRNA and uses N5, N10-methylenetetrahydrofolate (CH2THF) as the me
The tRNA recognition mechanism of folate/FAD-dependent tRNA methyltransferase (TrmFO).
Yamagami R, Yamashita K, Nishimasu H, Tomikawa C, Ochi A, Iwashita C, Hirata A, Ishitani R, Nureki O, Hori H. Yamagami R, et al. J Biol Chem. 2012 Dec 14;287(51):42480-94. doi: 10.1074/jbc.M112.390112. Epub 2012 Oct 24. J Biol Chem. 2012. PMID: 23095745 Free PMC article.
In Gram-positive and some Gram-negative eubacteria, m(5)U54 is produced by folate/FAD-dependent tRNA (m(5)U54) methyltransferase (TrmFO). TrmFO utilizes N(5),N(10)-methylenetetrahydrofolate (CH(2)THF) as a methyl donor. ...The positive determinants for TrmFO
In Gram-positive and some Gram-negative eubacteria, m(5)U54 is produced by folate/FAD-dependent tRNA (m(5)U54) methyltransferase (TrmFO
Crystallization and preliminary X-ray crystallographic characterization of TrmFO, a folate-dependent tRNA methyltransferase from Thermotoga maritima.
Cicmil N. Cicmil N. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Mar 1;64(Pt 3):193-5. doi: 10.1107/S1744309108003825. Epub 2008 Feb 23. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008. PMID: 18323606 Free PMC article.
TrmFO, previously classified as GID, is a methyltransferase that catalyzes the formation of 5-methyluridine or ribothymidine (T) at position 54 in tRNA in some Gram-positive bacteria. To date, TrmFO is the only characterized tRNA methyltransferase that does not use
TrmFO, previously classified as GID, is a methyltransferase that catalyzes the formation of 5-methyluridine or ribothymidine (T) at p
In vitro detection of the enzymatic activity of folate-dependent tRNA (Uracil-54,-C5)-methyltransferase: evolutionary implications.
Urbonavicius J, Brochier-Armanet C, Skouloubris S, Myllykallio H, Grosjean H. Urbonavicius J, et al. Methods Enzymol. 2007;425:103-19. doi: 10.1016/S0076-6879(07)25004-9. Methods Enzymol. 2007. PMID: 17673080 Review.
Inspection of presently available sequenced genomes reveals that trmFO gene is present in most Firmicutes, in all alpha- and delta-Proteobacteria (except Rickettsiales in which the trmFO gene is missing), Deinococci, Cyanobacteria, Fusobacteria, Thermotogales, Acido …
Inspection of presently available sequenced genomes reveals that trmFO gene is present in most Firmicutes, in all alpha- and delta-Pr …
Identification of the TyrOH( +) Radical Cation in the Flavoenzyme TrmFO.
Nag L, Sournia P, Myllykallio H, Liebl U, Vos MH. Nag L, et al. J Am Chem Soc. 2017 Aug 23;139(33):11500-11505. doi: 10.1021/jacs.7b04586. Epub 2017 Aug 8. J Am Chem Soc. 2017. PMID: 28745052
With a genetically modified form of the flavoenzyme TrmFO as a suitable model system and using ultrafast fluorescence and absorption spectroscopy, we characterize its protonated precursor TyrOH( +), and we show this species to have a distinct visible absorption band and a …
With a genetically modified form of the flavoenzyme TrmFO as a suitable model system and using ultrafast fluorescence and absorption …
27 results