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Alternate RRNA Secondary Structures As Regulators of Translation

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Date 2011 Jan 11
PMID 21217697
Citations 29
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Abstract

Structural dynamics of large molecular assemblies are intricately linked to function. For ribosomes, macromolecular changes occur especially during mRNA translation and involve participation of ribosomal RNA. Without suitable probes specific to RNA secondary structure, however, elucidation of more subtle dynamic ribosome structure-function relationships, especially in vivo, remains challenging. Here we report that the Z-DNA- and Z-RNA-binding domain Zα, derived from the human RNA editing enzyme ADAR1-L, binds with high stability to specific rRNA segments of Escherichia coli and human ribosomes. Zα impaired in Z-RNA recognition does not associate with ribosomes. Notably, Zα(ADAR1)-ribosome interaction blocks translation in vitro and in vivo, with substantial physiological consequences. Our study shows that ribosomes can be targeted by a protein that specifically recognizes an alternate rRNA secondary structure, and suggests a new mechanism of translational regulation on the ribosome.

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References
1.
Schade M, Turner C, Lowenhaupt K, Rich A, Herbert A . Structure-function analysis of the Z-DNA-binding domain Zalpha of dsRNA adenosine deaminase type I reveals similarity to the (alpha + beta) family of helix-turn-helix proteins. EMBO J. 1999; 18(2):470-9. PMC: 1171140. DOI: 10.1093/emboj/18.2.470. View

2.
Jan E, Sarnow P . Factorless ribosome assembly on the internal ribosome entry site of cricket paralysis virus. J Mol Biol. 2002; 324(5):889-902. DOI: 10.1016/s0022-2836(02)01099-9. View

3.
Droge P . Protein tracking-induced supercoiling of DNA: a tool to regulate DNA transactions in vivo?. Bioessays. 1994; 16(2):91-9. DOI: 10.1002/bies.950160205. View

4.
Williams B . PKR; a sentinel kinase for cellular stress. Oncogene. 1999; 18(45):6112-20. DOI: 10.1038/sj.onc.1203127. View

5.
Maas S, Gerber A, Rich A . Identification and characterization of a human tRNA-specific adenosine deaminase related to the ADAR family of pre-mRNA editing enzymes. Proc Natl Acad Sci U S A. 1999; 96(16):8895-900. PMC: 17704. DOI: 10.1073/pnas.96.16.8895. View