Saccharomyces cerevisiae RAI1 (YGL246c) is homologous to human DOM3Z and encodes a protein that binds the nuclear exoribonuclease Rat1p

Yang Xue, Xinxue Bai, In suk Lee, George Kallstrom, Jennifer Ho, Justin Brown, Audrey Stevens, Arlen W. Johnson

Research output: Contribution to journalArticle

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Abstract

The RAT1 gene of Saccharomyces cerevisiae encodes a 5'→3' exoribonuclease which plays an essential role in yeast RNA degradation and/or processing in the nucleus. We have cloned a previously uncharacterized gene (YGL246c) that we refer to as RAI1 (Rat1p interacting protein 1). RAI1 is homologous to Caenorhabditis elegans DOM-3 and human DOM3Z. Deletion of RAI1 confers a growth defect which can be complemented by an additional copy of RAT1 on a centromeric vector or by directing Xrn1p, the cytoplasmic homolog of Rat1p, to the nucleus through the addition of a nuclear targeting sequence. Deletion of RAI1 is synthetically lethal with the rat1-1(ts) mutation and shows genetic interaction with a deletion of SKI2 but not XR1. Polysome analysis of an rail deletion mutant indicated a defect in 60S biogenesis which was nearly fully reversed by high-copy RAT1. Northern blot analysis of rRNAs revealed that rail is required for normal 5.8S processing. In the absence of RAI1, 5.8S(L) was the predominant form of 5.8S and there was an accumulation of 3'-extended forms but not 5'-extended species of 5.8S. In addition, a 27S pre-rRNA species accumulated in the rail mutant. Thus, deletion of RAI1 affects both 5' and 3' processing reactions of 5.8S rRNA. Consistent with the in vivo data suggesting that RAI1 enhances RAT1 function, purified Rai1p stabilized the in vitro exoribonuclease activity of Rat1p.

Original languageEnglish
Pages (from-to)4006-4015
Number of pages10
JournalMolecular and Cellular Biology
Volume20
Issue number11
DOIs
Publication statusPublished - 2000 Jun 1

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Exoribonucleases
Nuclear Proteins
Saccharomyces cerevisiae
Proteins
2,5-Dimethoxy-4-Methylamphetamine
Polyribosomes
RNA Precursors
RNA Stability
Caenorhabditis elegans
Northern Blotting
Genes
Yeasts
Mutation

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Xue, Yang ; Bai, Xinxue ; Lee, In suk ; Kallstrom, George ; Ho, Jennifer ; Brown, Justin ; Stevens, Audrey ; Johnson, Arlen W. / Saccharomyces cerevisiae RAI1 (YGL246c) is homologous to human DOM3Z and encodes a protein that binds the nuclear exoribonuclease Rat1p. In: Molecular and Cellular Biology. 2000 ; Vol. 20, No. 11. pp. 4006-4015.
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abstract = "The RAT1 gene of Saccharomyces cerevisiae encodes a 5'→3' exoribonuclease which plays an essential role in yeast RNA degradation and/or processing in the nucleus. We have cloned a previously uncharacterized gene (YGL246c) that we refer to as RAI1 (Rat1p interacting protein 1). RAI1 is homologous to Caenorhabditis elegans DOM-3 and human DOM3Z. Deletion of RAI1 confers a growth defect which can be complemented by an additional copy of RAT1 on a centromeric vector or by directing Xrn1p, the cytoplasmic homolog of Rat1p, to the nucleus through the addition of a nuclear targeting sequence. Deletion of RAI1 is synthetically lethal with the rat1-1(ts) mutation and shows genetic interaction with a deletion of SKI2 but not XR1. Polysome analysis of an rail deletion mutant indicated a defect in 60S biogenesis which was nearly fully reversed by high-copy RAT1. Northern blot analysis of rRNAs revealed that rail is required for normal 5.8S processing. In the absence of RAI1, 5.8S(L) was the predominant form of 5.8S and there was an accumulation of 3'-extended forms but not 5'-extended species of 5.8S. In addition, a 27S pre-rRNA species accumulated in the rail mutant. Thus, deletion of RAI1 affects both 5' and 3' processing reactions of 5.8S rRNA. Consistent with the in vivo data suggesting that RAI1 enhances RAT1 function, purified Rai1p stabilized the in vitro exoribonuclease activity of Rat1p.",
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Saccharomyces cerevisiae RAI1 (YGL246c) is homologous to human DOM3Z and encodes a protein that binds the nuclear exoribonuclease Rat1p. / Xue, Yang; Bai, Xinxue; Lee, In suk; Kallstrom, George; Ho, Jennifer; Brown, Justin; Stevens, Audrey; Johnson, Arlen W.

In: Molecular and Cellular Biology, Vol. 20, No. 11, 01.06.2000, p. 4006-4015.

Research output: Contribution to journalArticle

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AU - Xue, Yang

AU - Bai, Xinxue

AU - Lee, In suk

AU - Kallstrom, George

AU - Ho, Jennifer

AU - Brown, Justin

AU - Stevens, Audrey

AU - Johnson, Arlen W.

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N2 - The RAT1 gene of Saccharomyces cerevisiae encodes a 5'→3' exoribonuclease which plays an essential role in yeast RNA degradation and/or processing in the nucleus. We have cloned a previously uncharacterized gene (YGL246c) that we refer to as RAI1 (Rat1p interacting protein 1). RAI1 is homologous to Caenorhabditis elegans DOM-3 and human DOM3Z. Deletion of RAI1 confers a growth defect which can be complemented by an additional copy of RAT1 on a centromeric vector or by directing Xrn1p, the cytoplasmic homolog of Rat1p, to the nucleus through the addition of a nuclear targeting sequence. Deletion of RAI1 is synthetically lethal with the rat1-1(ts) mutation and shows genetic interaction with a deletion of SKI2 but not XR1. Polysome analysis of an rail deletion mutant indicated a defect in 60S biogenesis which was nearly fully reversed by high-copy RAT1. Northern blot analysis of rRNAs revealed that rail is required for normal 5.8S processing. In the absence of RAI1, 5.8S(L) was the predominant form of 5.8S and there was an accumulation of 3'-extended forms but not 5'-extended species of 5.8S. In addition, a 27S pre-rRNA species accumulated in the rail mutant. Thus, deletion of RAI1 affects both 5' and 3' processing reactions of 5.8S rRNA. Consistent with the in vivo data suggesting that RAI1 enhances RAT1 function, purified Rai1p stabilized the in vitro exoribonuclease activity of Rat1p.

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