Nucleic Acids Research Advance Access originally published online on March 27, 2007
Nucleic Acids Research 2007 35(7):2295-2301; doi:10.1093/nar/gkm104
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Nucleic Acids Research, 2007, Vol. 35, No. 7 2295-2301
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Survey and Summary |
Ribosomal RNA guanine-(N2)-methyltransferases and their targets
Department of Chemistry and A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119992, Russia
*To whom correspondence should be addressed. +7-495-9395418; +7-495-9393181; Email: dontsova{at}genebee.msu.su
Received January 23, 2007. Revised February 6, 2007. Accepted February 6, 2007.
Five nearly universal methylated guanine-(N2) residues are present in bacterial rRNA in the ribosome. To date four out of five ribosomal RNA guanine-(N2)-methyltransferases are described. RsmC(YjjT) methylates G1207 of the 16S rRNA. RlmG(YgjO) and RlmL(YcbY) are responsible for the 23S rRNA m2G1835 and m2G2445 formation, correspondingly. RsmD(YhhF) is necessary for methylation of G966 residue of 16S rRNA. Structure of Escherichia coli RsmD(YhhF) methyltransferase and the structure of the Methanococcus jannaschii RsmC ortholog were determined. All ribosomal guanine-(N2)-methyltransferases have similar AdoMet-binding sites. In relation to the ribosomal substrate recognition, two enzymes that recognize assembled subunits are relatively small single domain proteins and two enzymes that recognize naked rRNA are larger proteins containing separate methyltransferase- and RNA-binding domains. The model for recognition of specific target nucleotide is proposed. The hypothetical role of the m2G residues in rRNA is discussed.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  A. Czerwoniec, S. Dunin-Horkawicz, E. Purta, K. H. Kaminska, J. M. Kasprzak, J. M. Bujnicki, H. Grosjean, and K. Rother MODOMICS: a database of RNA modification pathways. 2008 update Nucleic Acids Res., January 1, 2009; 37(suppl_1): D118 - D121. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Ero, L. Peil, A. Liiv, and J. Remme Identification of pseudouridine methyltransferase in Escherichia coli RNA, October 1, 2008; 14(10): 2223 - 2233. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. Purta, K. H. Kaminska, J. M. Kasprzak, J. M. Bujnicki, and S. Douthwaite YbeA is the m3{Psi} methyltransferase RlmH that targets nucleotide 1915 in 23S rRNA RNA, October 1, 2008; 14(10): 2234 - 2244. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. S. Pallan, C. Kreutz, S. Bosio, R. Micura, and M. Egli Effects of N2,N2 -dimethylguanosine on RNA structure and stability: Crystal structure of an RNA duplex with tandem m2 2G:A pairs RNA, October 1, 2008; 14(10): 2125 - 2135. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Demirci, S. T. Gregory, A. E. Dahlberg, and G. Jogl Crystal Structure of the Thermus thermophilus 16 S rRNA Methyltransferase RsmC in Complex with Cofactor and Substrate Guanosine J. Biol. Chem., September 26, 2008; 283(39): 26548 - 26556. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Sunita, E. Purta, M. Durawa, K. L. Tkaczuk, J. Swaathi, J. M. Bujnicki, and J. Sivaraman Functional specialization of domains tandemly duplicated within 16S rRNA methyltransferase RsmC Nucleic Acids Res., July 26, 2007; 35(13): 4264 - 4274. [Abstract] [Full Text] [PDF]
|
|