FEBS Letters
Volume 584, Issue 15 , Pages 3299-3304, 4 August 2010

Deletion of Swm2p selectively impairs trimethylation of snRNAs by trimethylguanosine synthase (Tgs1p)

Edited by Ulrike Kutay

Biochemistry Center (BZH), University of Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany

Received 25 March 2010; received in revised form 30 June 2010; accepted 2 July 2010. published online 09 July 2010.

Abstract 

The 5′ cap trimethylation of small nuclear (snRNAs) and several nucleolar RNAs (snoRNAs) by trimethylguanosine synthase 1 (Tgs1p) is required for efficient pre-mRNA splicing. The previously uncharacterised protein Swm2p interacted with Tgs1p in yeast two-hybrid screens. In the present study we show that Swm2p interacts with the N-terminus of Tgs1p and its deletion impairs pre-mRNA splicing and pre-rRNA processing. The trimethylation of spliceosomal snRNAs and the U3 snoRNA, but not other snoRNAs, was abolished in the absence of Swm2p, indicating that Swm2p is required for a substrate-specific activity of Tgs1p.

Structured summary

MINT-7949608: p53 (uniprotkb:P02340) physically interacts (MI:0915) with large T-antigen (uniprotkb:P03070) by two-hybrid (MI:0018)

MINT-7949574: swm2 (uniprotkb:P40342) physically interacts (MI:0915) with swm2 (uniprotkb:P40342) by pull down (MI:0096)

MINT-7949556: swm2 (uniprotkb:P40342) physically interacts (MI:0915) with TGS1 (uniprotkb:Q12052) by pull down (MI:0096)

MINT-7949587: swm2 (uniprotkb:P40342) physically interacts (MI:0915) with tgs1 (uniprotkb:Q12052) by two-hybrid (MI:0018)

MINT-7949641: nop1 (uniprotkb:P15646) colocalizes (MI:0403) with TGS1 (uniprotkb:Q12052) by fluorescence microscopy (MI:0416)

MINT-7949627: swm2 (uniprotkb:P40342) and nop1 (uniprotkb:P15646) colocalize (MI:0403) by fluorescence microscopy (MI:0416)

MINT-7949540: swm2 (uniprotkb:P40342) physically interacts (MI:0915) with TGS1 (uniprotkb:Q12052) by tandem affinity purification (MI:0676)

Keywords: Trimethylation, snRNA, snoRNA, Yeast, TGS1, SWM2

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PII: S0014-5793(10)00555-7

doi:10.1016/j.febslet.2010.07.001

FEBS Letters
Volume 584, Issue 15 , Pages 3299-3304, 4 August 2010

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