Report

Identification and modeling of a phosphatase-like domain in a tRNA 2′-O-ribosyl phosphate transferase Rit1p

Volume 10, Issue 20   October 15, 2011
Pages 3566 - 3570
http://dx.doi.org/10.4161/cc.10.20.17857
Keywords: Fold-recognition, Rit1p, bioinformatics, homology modeling, tRNA modification
Authors: Anna Czerwoniec and Janusz M. Bujnicki

View affiliations

Abstract:
Cytoplasmic initiator tRNAs from plants and fungi are excluded from participating in translational elongation by the presence of a unique 2'-phosphoribosyl modification of purine 64, introduced posttranscriptionally by the enzyme Rit1p. Members of the Rit1p family show no obvious similarity to other proteins or domains, there is no structural information available to guide experimental analyses, and the mechanism of action of this enzyme remains a mystery. Using protein fold recognition, we identified a phosphatase-like domain in the C-terminal part of Rit1p. A comparative model of the C-terminal domain was constructed and used to predict the function of conserved residues and to propose the mechanism of action of Rit1p. The model will facilitate experimental analyses of Rit1p and its interactions with the initiator tRNA substrate.

Received: May 19, 2011; Accepted: August 23, 2011

Preview:



Advertisements