RNA binding strategies of ribosomal proteins

被引:98
作者
Draper, DE [1 ]
Reynaldo, LP [1 ]
机构
[1] Johns Hopkins Univ, Dept Chem, Baltimore, MD 21218 USA
关键词
D O I
10.1093/nar/27.2.381
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 cc-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.
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页码:381 / 388
页数:8
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