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

doi:10.1016/S1097-2765(00)00034-4

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

Research output: Contribution to journal › Article › peer-review

74 Scopus citations

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 language	English (US)
Pages (from-to)	339-348
Number of pages	10
Journal	Molecular cell
Volume	6
Issue number	2
DOIs	https://doi.org/10.1016/S1097-2765(00)00034-4
State	Published - Aug 2000
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/S1097-2765(00)00034-4

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title = "Control of transfer RNA maturation by phosphorylation of the human La antigen on serine 366",

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.",

author = "Intine, {Robert V.A.} and Sakulich, {Amy L.} and Koduru, {Shashi B.} and Ying Huang and Erik Pierstorff and Goodier, {John L.} and Lon Phan and Maraia, {Richard J.}",

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T1 - Control of transfer RNA maturation by phosphorylation of the human La antigen on serine 366

AU - Intine, Robert V.A.

AU - Sakulich, Amy L.

AU - Koduru, Shashi B.

AU - Huang, Ying

AU - Pierstorff, Erik

AU - Goodier, John L.

AU - Phan, Lon

AU - Maraia, Richard J.

PY - 2000/8

Y1 - 2000/8

N2 - 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.

AB - 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.

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JO - Molecular cell

JF - Molecular cell

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

Abstract

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