RNA binding strategies of ribosomal proteins.
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.
Draper
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Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA. draper@jhunix.hcf.jhu.edu
Reynaldo
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D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D018398:Homeodomain Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012335:RNA, Ribosomal / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000737:chemistry; D012269:Ribosomal Proteins / Q000737:chemistry / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D018398:Homeodomain Proteins; D012335:RNA, Ribosomal; D012261:Ribonucleoproteins; D012269:Ribosomal Proteins