Structure of the bifunctional methyltransferase YcbY (RlmKL) that adds the m 7G2069 and m 2G2445 modifications in Escherichia coli 23S rRNA
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Structure of the bifunctional methyltransferase YcbY (RlmKL) that adds the m 7G2069 and m 2G2445 modifications in Escherichia coli 23S rRNA. / Wang, Kai Tuo; Desmolaize, Benoit; Nan, Jie; Zhang, Xiao Wei; Li, Lan Fen; Douthwaite, Stephen; Su, Xiao Dong.
In: Nucleic Acids Research, Vol. 40, No. 11, 01.06.2012, p. 5138-5148.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Structure of the bifunctional methyltransferase YcbY (RlmKL) that adds the m 7G2069 and m 2G2445 modifications in Escherichia coli 23S rRNA
AU - Wang, Kai Tuo
AU - Desmolaize, Benoit
AU - Nan, Jie
AU - Zhang, Xiao Wei
AU - Li, Lan Fen
AU - Douthwaite, Stephen
AU - Su, Xiao Dong
PY - 2012/6/1
Y1 - 2012/6/1
N2 - The 23S rRNA nucleotide m 2G2445 is highly conserved in bacteria, and in Escherichia coli this modification is added by the enzyme YcbY. With lengths of around 700 amino acids, YcbY orthologs are the largest rRNA methyltransferases identified in Gram-negative bacteria, and they appear to be fusions from two separate proteins found in Gram-positives. The crystal structures described here show that both the N-and C-terminal halves of E. coli YcbY have a methyltransferase active site and their folding patterns respectively resemble the Streptococcus mutans proteins Smu472 and Smu776. Mass spectrometric analyses of 23S rRNAs showed that the N-terminal region of YcbY and Smu472 are functionally equivalent and add the m 2G2445 modification, while the C-terminal region of YcbY is responsible for the m 7G2069 methylation on the opposite side of the same helix (H74). Smu776 does not target G2069, and this nucleotide remains unmodified in Gram-positive rRNAs. The E.coli YcbY enzyme is the first example of a methyltransferase catalyzing two mechanistically different types of RNA modification, and has been renamed as the Ribosomal large subunit methyltransferase, RlmKL. Our structural and functional data provide insights into how this bifunctional enzyme evolved.
AB - The 23S rRNA nucleotide m 2G2445 is highly conserved in bacteria, and in Escherichia coli this modification is added by the enzyme YcbY. With lengths of around 700 amino acids, YcbY orthologs are the largest rRNA methyltransferases identified in Gram-negative bacteria, and they appear to be fusions from two separate proteins found in Gram-positives. The crystal structures described here show that both the N-and C-terminal halves of E. coli YcbY have a methyltransferase active site and their folding patterns respectively resemble the Streptococcus mutans proteins Smu472 and Smu776. Mass spectrometric analyses of 23S rRNAs showed that the N-terminal region of YcbY and Smu472 are functionally equivalent and add the m 2G2445 modification, while the C-terminal region of YcbY is responsible for the m 7G2069 methylation on the opposite side of the same helix (H74). Smu776 does not target G2069, and this nucleotide remains unmodified in Gram-positive rRNAs. The E.coli YcbY enzyme is the first example of a methyltransferase catalyzing two mechanistically different types of RNA modification, and has been renamed as the Ribosomal large subunit methyltransferase, RlmKL. Our structural and functional data provide insights into how this bifunctional enzyme evolved.
UR - http://www.scopus.com/inward/record.url?scp=84862156291&partnerID=8YFLogxK
U2 - 10.1093/nar/gks160
DO - 10.1093/nar/gks160
M3 - Journal article
C2 - 22362734
AN - SCOPUS:84862156291
VL - 40
SP - 5138
EP - 5148
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 0305-1048
IS - 11
ER -
ID: 234874897