Nucleic Acids Research, Vol 27, Issue 2 381-388, Copyright © 1999 by Oxford University Press
DE Draper and LP Reynaldo
Structures of a number of ribosomal proteins have now been determined by
crystallography and NMR, though the complete structure of a ribosomal
protein-rRNA complex has yet to be solved. However, some ribosomal protein
structures show strong similarity to well-known families of DNA or RNA
binding proteins for which structures in complex with cognate nucleic acids
are available. Comparison of the known nucleic acid binding mechanisms of
these non-ribosomal proteins with the most highly conserved surfaces of
similar ribosomal proteins suggests ways in which the ribosomal proteins
may be binding RNA. Three binding motifs, found in four ribosomal proteins
so far, are considered here: homeodomain-like alpha-helical proteins (L11),
OB fold proteins (S1 and S17) and RNP consensus proteins (S6). These
comparisons suggest that ribosomal proteins combine a small number of
fundamental strategies to develop highly specific RNA recognition sites.
REVIEWS
RNA binding strategies of ribosomal proteins
Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA. draper@jhunix.hcf.jhu.edu
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