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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
additional information
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
the recombinant protein exhibits the same specificity as the native enzyme. It forms only m5C and only at position 967. C1407, which is also 5-methylcytosine in natural 16S RNA, is not methylated. In vitro, the enzyme only recognizes free 16S RNA. 30S ribosomal subunits are not a substrate
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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additional information
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substrate recognition mechanism, overview
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additional information
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substrate recognition mechanism, overview
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
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evolution
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Fmu/RsmB/RrmB homologues exist not only in bacteria but also in archaea and eukarya and constitute a large orthologous group in the RNA:m5C methyltransferase family. The sequence of the N-terminal domain is negligibly conserved between the bacterial and archaeal subfamilies
evolution
Fmu/RsmB/RrmB homologues exist not only in bacteria but also in archaea and eukarya and constitute a large orthologous group in the RNA:m5C methyltransferase family. The sequence of the N-terminal domain is negligibly conserved between the bacterial and archaeal subfamilies
malfunction
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deletion of rsmB in a C-terminal S9 tail deletion strain of Escherichia coli causes significantly increased -1 frameshifting at 37°C
malfunction
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enzyme deficiency does not impact initiation from most codons
malfunction
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deletion of rsmB in a C-terminal S9 tail deletion strain of Escherichia coli causes significantly increased -1 frameshifting at 37°C
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metabolism
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two methyltransferases, RsmB and RsmF, are responsible for all four 5-methylcytidine modifications in 16S rRNA of Thermus thermophilus, overview. RsmB produces m5C967, while RsmF methylates C1400, C1404, and C1407 in a 30S subunit substrate, but only C1400 and C1404 when naked 16S rRNA is the substrate
metabolism
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two methyltransferases, RsmB and RsmF, are responsible for all four 5-methylcytidine modifications in 16S rRNA of Thermus thermophilus, overview. RsmB produces m5C967, while RsmF methylates C1400, C1404, and C1407 in a 30S subunit substrate, but only C1400 and C1404 when naked 16S rRNA is the substrate
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additional information
next to the S-adenosyl-L-methionine-binding site is a positively charged cleft, formed between the N- and C-terminal domains, which is conserved in the archaeal PH0851 homologues and seems to be suitable for binding the RNA substrate
additional information
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next to the S-adenosyl-L-methionine-binding site is a positively charged cleft, formed between the N- and C-terminal domains, which is conserved in the archaeal PH0851 homologues and seems to be suitable for binding the RNA substrate
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monomer
two domains and one linker: an N-terminal domain formed by residues 1-145, a C-terminal domain formed by residues 185-448, and an alpha-helical linker formed by residues 146-184
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x * 47000, SDS-PAGE
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x * 47140, calculated from sequence
additional information
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next to the S-adenosyl-L-methionine-binding site is a positively charged cleft, formed between the N- and C-terminal domains, that seems to be suitable for binding the RNA substrate. The N-terminal domains of Pyrococcus horikoshii PH0851 and Escherichia coli Fmu/RsmB/RrmB are both alpha-helical and adopt a similar topology, sequence and structure comparison, overview
additional information
next to the S-adenosyl-L-methionine-binding site is a positively charged cleft, formed between the N- and C-terminal domains, which is conserved in the archaeal PH0851 homologues and seems to be suitable for binding the RNA substrate. The N-terminal domains of Pyrococcus horikoshii PH0851 and Escherichia coli Fmu/RsmB/RrmB are both alpha-helical and adopt a similar topology, sequence and structure comparison, overview
additional information
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next to the S-adenosyl-L-methionine-binding site is a positively charged cleft, formed between the N- and C-terminal domains, which is conserved in the archaeal PH0851 homologues and seems to be suitable for binding the RNA substrate. The N-terminal domains of Pyrococcus horikoshii PH0851 and Escherichia coli Fmu/RsmB/RrmB are both alpha-helical and adopt a similar topology, sequence and structure comparison, overview
additional information
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comparison of Thermus thermophilus RsmB and RsmF protein sequences, secondary and tertiary structure, differences in substrate binding, overview
additional information
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comparison of Thermus thermophilus RsmB and RsmF protein sequences, secondary and tertiary structure, differences in substrate binding, overview
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hanging-drop vapor diffusion method, crystal structure of Escherichia coli Fmu, determined at 1.65 A resolution for the apoenzyme and 2.1 A resolution in complex with S-adenosyl-L-methionine
purified wild-type and SeMet-labeled PH0851 complexed with S-adenosyl-L-methionine-analogue sinefungin, hanging drop vapour diffusion method, mixing of protein solution, containing 1.7 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, 400 mM NaCl, and 1 mM sinefungin, with reservoir solution, containing 80 mM HEPES-Na buffer, pH 7.0, 1.15 M sodium citrate, and 7-15% w/v 1,6-hexanediol, in a 4:1 ratio, 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.55-3.0 A resolution, molecular replacement
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Tscherne, J.S.; Nurse, K.; Popienick, P.; Michel, H.; Sochacki, M.; Ofengand, J.
Purification, cloning, and characterization of the 16S RNA m5C967 methyltransferase from Escherichia coli
Biochemistry
38
1884-1892
1999
Escherichia coli (P36929)
brenda
Gu, X.R.; Gustafsson, C.; Ku, J.; Yu, M.; Santi, D.V.
Identification of the 16S rRNA m5C967 methyltransferase from Escherichia coli
Biochemistry
38
4053-4057
1999
Escherichia coli (P36929), Escherichia coli
brenda
Foster, P.G.; Nunes, C.R.; Greene, P.; Moustakas, D.; Stroud, R.M.
The first structure of an RNA m5C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate
Structure
11
1609-1620
2003
Escherichia coli (P36929), Escherichia coli
brenda
Hikida, Y.; Kuratani, M.; Bessho, Y.; Sekine, S.I.; Yokoyama, S.
Structure of an archaeal homologue of the bacterial Fmu/RsmB/RrmB rRNA cytosine 5-methyltransferase
Acta Crystallogr. Sect. D
66
1301-1307
2010
Escherichia coli, Pyrococcus horikoshii (O58581), Pyrococcus horikoshii
brenda
Demirci, H.; Larsen, L.H.; Hansen, T.; Rasmussen, A.; Cadambi, A.; Gregory, S.T.; Kirpekar, F.; Jogl, G.
Multi-site-specific 16S rRNA methyltransferase RsmF from Thermus thermophilus
RNA
16
1584-1596
2010
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Arora, S.; Bhamidimarri, S.P.; Weber, M.H.; Varshney, U.
Role of the ribosomal P-site elements of m2G966, m5C967, and the S9 C-terminal tail in maintenance of the reading frame during translational elongation in Escherichia coli
J. Bacteriol.
195
3524-3530
2013
Escherichia coli, Escherichia coli BW25113
brenda
Arora, S.; Bhamidimarri, S.P.; Bhattacharyya, M.; Govindan, A.; Weber, M.H.; Vishveshwara, S.; Varshney, U.
Distinctive contributions of the ribosomal P-site elements m2G966, m5C967 and the C-terminal tail of the S9 protein in the fidelity of initiation of translation in Escherichia coli
Nucleic Acids Res.
41
4963-4975
2013
Escherichia coli
brenda
Prokhorova, I.V.; Osterman, I.A.; Burakovsky, D.E.; Serebryakova, M.V.; Galyamina, M.A.; Pobeguts, O.V.; Altukhov, I.; Kovalchuk, S.; Alexeev, D.G.; Govorun, V.M.; Bogdanov, A.A.; Sergiev, P.V.; Dontsova, O.A.
Modified nucleotides m2G966/m5C967 of Escherichia coli 16S rRNA are required for attenuation of tryptophan operon
Sci. Rep.
3
3236
2013
Escherichia coli, Escherichia coli BW25113
brenda