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A minihelix-loop RNA acts as a trans-aminoacylation catalyst

Published online by Cambridge University Press:  06 July 2001

NICK LEE  and
HIROAKI SUGA
NICK LEE
Affiliation:
Department of Chemistry, State University of New York at Buffalo, Buffalo, New York 14260-3000, USA
HIROAKI SUGA
Affiliation:
Department of Chemistry, State University of New York at Buffalo, Buffalo, New York 14260-3000, USA
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Abstract

We previously reported a bifunctional ribozyme that catalyzes self-aminoacylation and subsequent acyl-transfer to a tRNA. The ribozyme selectively recognizes a biotinyl-glutamine substrate, and charges the tRNA molecule in trans. Structurally, there are two catalytic domains, referred to as glutamine-recognition (QR) and acyl-transferase (ATRib). We report here the essential catalytic core of the QR domain as determined by extensive biochemical probing, mutation, and structural minimization. The minimal core of the QR domain is a 29-nt helix-loop RNA, which is also able to glutaminylate ATRib in trans. Its amino acid binding site is embedded in an 11-nt cluster that is adjacent to the loop that interacts with the ATRib domain. Our study shows that a minihelix-loop RNA can act as a trans-aminoacylation catalyst, which lends support for the critical role of minihelix-loops in the early evolution of the aminoacylation system.

Keywords

aminoacyl-tRNA synthesisin vitro selectionnucleotide analog interference mappingribozyme
Type
Research Article
Information
RNA , Volume 7 , Issue 7 , July 2001 , pp. 1043 - 1051
Copyright
2001 RNA Society

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