Identification and modeling of a phosphatase-like domain in a tRNA 2'-O-ribosyl phosphate transferase Rit1p.
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.
Bioinformatics Laboratory, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Poznan, Poland. aczerwo@amu.edu.pl
Anna
A
Czerwoniec
Janusz M
JM
Bujnicki
D000595:Amino Acid Sequence; D001483:Base Sequence; D019295:Computational Biology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010430:Pentosyltransferases / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D016415:Sequence Alignment
D029701:Saccharomyces cerevisiae Proteins; D010430:Pentosyltransferases; C090456:RIT1 protein, S cerevisiae