Open AccessStructural insights into substrate selectivity of ribosomal RNA methyltransferase RlmCD
Author(s) -
Yiyang Jiang,
Fudong Li,
Jihui Wu,
Yunyu Shi,
Qingguo Gong
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0185226
Subject(s) - methyltransferase , 23s ribosomal rna , ribosomal rna , rna , transferase , biochemistry , ribosome , biology , linker , escherichia coli , chemistry , 5.8s ribosomal rna , enzyme , methylation , gene , computer science , operating system
RlmCD has recently been identified as the S-adenosyl methionine (SAM)-dependent methyltransferase responsible for the formation of m 5 U at U747 and U1939 of 23S ribosomal RNA in Streptococcus pneumoniae . In this research, we determine the high-resolution crystal structures of apo-form RlmCD and its complex with SAH. Using an in-vitro methyltransferase assay, we reveal the crucial residues for its catalytic functions. Furthermore, structural comparison between RlmCD and its structural homologue RumA, which only catalyzes the m 5 U1939 in Escherichia coli , implicates that a unique long linker in the central domain of RlmCD is the key factor in determining its substrate selectivity. Its significance in the enzyme activity of RlmCD is further confirmed by in-vitro methyltransferase assay.