Nucleic Acids Research Advance Access originally published online on March 11, 2009
Nucleic Acids Research 2009 37(10):3134-3142; doi:10.1093/nar/gkp119
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Nucleic Acids Research, 2009, Vol. 37, No. 10 3134-3142
© 2009 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.
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A recurrent magnesium-binding motif provides a framework for the ribosomal peptidyl transferase center
School of Chemistry and Biochemistry, Parker H. Petit Institute of Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA 30332-0400, USA
*To whom correspondence should be addressed. Tel: +1 404 894 9752; Fax: +1 404 894 7452; Email: loren.williams{at}chemistry.gatech.edu
Received October 23, 2008. Revised February 7, 2009. Accepted February 11, 2009.
The ribosome is an ancient macromolecular machine responsible for the synthesis of all proteins in all living organisms. Here we demonstrate that the ribosomal peptidyl transferase center (PTC) is supported by a framework of magnesium microclusters (Mg2+-µc's). Common features of Mg2+-µc's include two paired Mg2+ ions that are chelated by a common bridging phosphate group in the form Mg
–(O1P-P-O2P)–Mg
. This bridging phosphate is part of a 10-membered chelation ring in the form Mg
–(OP-P-O5'-C5'-C4'-C3'-O3'-P-OP)–Mg
. The two phosphate groups of this 10-membered ring are contributed by adjacent residues along the RNA backbone. Both Mg2+ ions are octahedrally coordinated, but are substantially dehydrated by interactions with additional RNA phosphate groups. The Mg2+-µc's in the LSU (large subunit) appear to be highly conserved over evolution, since they are unchanged in bacteria (Thermus thermophilus, PDB entry 2J01) and archaea (Haloarcula marismortui, PDB entry 1JJ2
[PDB]
). The 2D elements of the 23S rRNA that are linked by Mg2+-µc's are conserved between the rRNAs of bacteria, archaea and eukarya and in mitochondrial rRNA, and in a proposed minimal 23S-rRNA. We observe Mg2+-µc's in other rRNAs including the bacterial 16S rRNA, and the P4–P6 domain of the tetrahymena Group I intron ribozyme. It appears that Mg2+-µc's are a primeval motif, with pivotal roles in RNA folding, function and evolution.
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