The enzyme methylates 23S rRNA in vitro, assembled 50S subunits are not a substrate . The enzyme specifically methylates guanine2445 at N2 in 23S rRNA.
The enzyme methylates 23S rRNA in vitro, assembled 50S subunits are not a substrate [1]. The enzyme specifically methylates guanine2445 at N2 in 23S rRNA.
N2-methylguanosine2445 of the 23S rRNA is located in a cluster of modified nucleotides concentrated at the peptidyl transferase center of the ribosome. It is likely that the G2445 modification is necessary for prevention of nonfunctional secondary or tertiary structure formation at the peptidyl transferase center
recombinant YcbY protein is able to methylate 23S rRNA purified from the ycbY knock-out strain in vitro, assembled 50S subunits are not a substrate for the methylase
duplex formation of H74 is not required for the m2G2445 formation. The 29-mer single-stranded transcript 6, which consists of residues C2422 to A2450, can form m2G2445 efficiently
the bifunctional methyltransferase YcbY, i.e. RlmKL, adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA, recognition of dual rRNA targets by YcbY
the bifunctional methyltransferase YcbY, i.e. RlmKL, adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA, recognition of dual rRNA targets by YcbY
helix 80 and the 12 nt ss region are critical sites necessary for m2G2445 and m7G2069 formation. Transcript 7, which lacks helix 80 and the 12 nt single-strand region, is not methylated at either position
N2-methylguanosine2445 of the 23S rRNA is located in a cluster of modified nucleotides concentrated at the peptidyl transferase center of the ribosome. It is likely that the G2445 modification is necessary for prevention of nonfunctional secondary or tertiary structure formation at the peptidyl transferase center
the bifunctional methyltransferase YcbY, i.e. RlmKL, adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA, recognition of dual rRNA targets by YcbY
the bifunctional methyltransferase YcbY, i.e. RlmKL, adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA, recognition of dual rRNA targets by YcbY
the enzyme is a member of the COG1092 family, evolutionary implications of the apparent emergence of Escherichia coli YcbY from the fusion of Streptococcus mutans Smu472 and Smu776 orthologues are considered
cooperative methylation of helix 74 by RlmKL plays a key role in the efficient assembly of the 50S subunit, RlmKL enzyme is an example of a methyltransferase catalyzing two mechanistically different types of RNA modification. RlmKL has an unwinding activity of Helix 74, facilitating cooperative methylations of m7G2069 and m2G2445 during biogenesis of 50S subunit. Methyltransferase RlmL, encoded by rlmL/ycbY, catalyzes S-adenosyl-L-methionine-dependent m2G2445 formation
insertions in both uup and ycbY confer a Uup- phenotype. It is concluded that ycbY and uup constitute a single operon and that the failure of the ycbY insertion to complement mutations in uup is because of a polarity effect associated with the former
knock-out of the ycbY gene leads to loss of modification at G2445 and growth retardation. Growth competition with the parental wild-type strain leads to a gradual decrease in the knock-out strain cells proportion in the media
it is likely that the G2445 modification is necessary for prevention of nonfunctional secondary or tertiary structure formation at the peptidyl transferase center
the N-terminal region of YcbY adds the m2G2445 modification, while the C-terminal region of YcbY is responsible for the m7G2069 methylation on the opposite side of the same helix, H74. YcbY enzyme is an example of a methyltransferase catalyzing two mechanistically different types of RNA modification
structure comparisosns with Streptococcus mutans proteins Smu472 and Smu776, the active site and their folding patterns respectively resemble each other, overview
structure comparisosns with Streptococcus mutans proteins Smu472 and Smu776, the active site and their folding patterns respectively resemble each other, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged RlmL, hanging drop vapour diffusion method, mixing of 0.002 ml of 20 mg/ml protein in 20 mM Tris-HCl, pH 8.0, S-adenosyl-L-homocysteine-saturated, and 200 mM NaCl, with 0.002 ml of reservoir solution containing 0.1 M HEPES, pH 7.0, and 12% w/v PEG 8000, and with 0.001 ml of 30%(w/v) n-octanoylsucrose solution, addition of 2 mM S-adenosyl-L-methionine, equilibration against 0.5 ml of reservoir solution, method optimization, X-ray diffraction structure determination and analysis at 2.2 A resolution