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Structure of an archaeal homologue of the bacterial Fmu/RsmB/RrmB rRNA cytosine 5-methyltransferase by Yasushi Hikida; Mitsuo Kuratani; Yoshitaka Bessho; Shun-ichi Sekine; Shigeyuki Yokoyama is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Structure of an archaeal homologue of the bacterial Fmu/RsmB/RrmB rRNA cytosine 5-methyltransferase about?

One of the modified nucleosides that frequently occurs in rRNAs and tRNAs is 5-methylcytidine (m 5 C). Escherichia coli Fmu/RsmB/RrmB is an S-adenosyl-l-methionine (AdoMet)dependent methyltransferase that forms m 5 C967 in 16S rRNA. Fmu/RsmB/RrmB homologues exist not only in bacteria but also in archaea and eukarya and constitute a large orthologous group in the RNA:m 5 C methyltransferase family. In the present study, the crystal structure of a homologue of E. coli Fmu/RsmB/RrmB from the archaeon Pyrococcus horikoshii (PH0851) complexed with an AdoMet analogue was determined at 2.55 A ̊resolution. The structure and sequence of the C-terminal catalytic domain are highly conserved compared with those of E. coli Fmu/RsmB/RrmB. In contrast, the sequence of the N-terminal domain is negligibly conserved between the bacterial and archaeal subfamilies. Nevertheless, the N-terminal domains of PH0851 and E. coli Fmu/RsmB/ RrmB are both -helical and adopt a similar topology. Next to the AdoMet-binding site, a positively charged cleft is formed between the N-and C-terminal domains. This cleft is conserved in the archaeal PH0851 homologues and seems to be suitable for binding the RNA substrat

Who reads Structure of an archaeal homologue of the bacterial Fmu/RsmB/RrmB rRNA cytosine 5-methyltransferase?

Author

Yasushi Hikida; Mitsuo Kuratani; Yoshitaka Bessho; Shun-ichi Sekine; Shigeyuki Yokoyama

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)