Control of transfer RNA maturation by phosphorylation of the human La antigen on serine 366

Robert V A Intine, Amy L. Sakulich, Shashi B. Koduru, Ying Huang, Erik Pierstorff, John L Goodier, Lon Phan, Richard J. Maraia

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Abstract

Conversion of a nascent precursor tRNA to a mature-functional species is a multipartite process that involves the sequential actions of several processing and modifying enzymes. La is the first protein to interact with pre-tRNAs in eukaryotes. An opal suppressor tRNA served as a functional probe to examine the activities of yeast and human (h)La proteins in this process in fission yeast. An RNA recognition motif and Walker motif in the metazoan-specific C-terminal domain (CTD) of hLa maintain pre-tRNA in an unprocessed state by blocking the 5'-processing site, impeding an early step in the pathway. Faithful phosphorylation of hLa on serine 366 reverses this block and promotes tRNA maturation. The results suggest that regulation of tRNA maturation at the level of RNase P cleavage may occur via phosphorylation of serine 366 of hLa.

Original languageEnglish (US)
Pages (from-to)339-348
Number of pages10
JournalMolecular Cell
Volume6
Issue number2
Publication statusPublished - 2000
Externally publishedYes

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ASJC Scopus subject areas

  • Molecular Biology

Cite this

Intine, R. V. A., Sakulich, A. L., Koduru, S. B., Huang, Y., Pierstorff, E., Goodier, J. L., ... Maraia, R. J. (2000). Control of transfer RNA maturation by phosphorylation of the human La antigen on serine 366. Molecular Cell, 6(2), 339-348.