ArticleMolecular and cellular biology2000
Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that is able to bind S-adenosyl-L-methionine in vitro.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed.
- Loss of Conserved rRNA Modifications in the Peptidyl Transferase Center Leads to Diminished Protein Synthesis and Cell Growth in Budding Yeast.International journal of molecular sciences · 2024Article
- A single 2'-O-methylation of ribosomal RNA gates assembly of a functional ribosome.Nature structural & molecular biology · 2023Article
- The catalytic activity of the translation termination factor methyltransferase Mtq2-Trm112 complex is required for large ribosomal subunit biogenesis.Nucleic acids research · 2020Article
- Review
- Article
- Landmarks in the Evolution of (t)-RNAs from the Origin of Life up to Their Present Role in Human Cognition.Life (Basel, Switzerland) · 2015Review
- Article
- FTSJ2, a heat shock-inducible mitochondrial protein, suppresses cell invasion and migration.PloS one · 2014Article
- Structure of Aeropyrum pernix fibrillarin in complex with natively bound S-adenosyl-L-methionine at 1.7 Å resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Deletion of C2orf34, PREPL and SLC3A1 causes atypical hypotonia-cystinuria syndrome.BMJ case reports · 2009Article
- Trm11p and Trm112p are both required for the formation of 2-methylguanosine at position 10 in yeast tRNA.Molecular and cellular biology · 2005Article
- Substrate binding analysis of the 23S rRNA methyltransferase RrmJ.Journal of bacteriology · 2004Article
- Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-binding protein cause nonsyndromic X-linked mental retardation.American journal of human genetics · 2004Article
- Npa1p, a component of very early pre-60S ribosomal particles, associates with a subset of small nucleolar RNPs required for peptidyl transferase center modification.Molecular and cellular biology · 2004Article
- Purified box C/D snoRNPs are able to reproduce site-specific 2'-O-methylation of target RNA in vitro.Molecular and cellular biology · 2002Article
- Trm7p catalyses the formation of two 2'-O-methylriboses in yeast tRNA anticodon loop.The EMBO journal · 2002Article
- Comparative genomics and evolution of proteins involved in RNA metabolism.Nucleic acids research · 2002Article
- MRM2 encodes a novel yeast mitochondrial 21S rRNA methyltransferase.The EMBO journal · 2002Article
- Conventional and nonconventional roles of the nucleolus.International review of cytology · 2002Review
- The box C/D motif directs snoRNA 5'-cap hypermethylation.Nucleic acids research · 2000Article
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3 authors.
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Abstract
We present here the characterization of SPB1, an essential yeast gene that is required for ribosome synthesis. A cold-sensitive allele for that gene (referred to here as spb1-1) had been previously isolated as a suppressor of a mutation affecting the poly(A)-binding protein gene (PAB1) and a thermosensitive allele (referred to here as spb1-2) was isolated in a search for essential genes required for gene silencing in Saccharomyces cerevisiae. The two mutants are able to suppress the deletion of PAB1, and they both present a strong reduction in their 60S ribosomal subunit content. In an spb1-2 strain grown at the restrictive temperature, processing of the 27S pre-rRNA into mature 25S rRNA and 5.8S is completely abolished and production of mature 18S is reduced, while the abnormal 23S species is accumulated. Spb1p is a 96.5-kDa protein that is localized to the nucleolus. Coimmunoprecipitation experiments show that Spb1p is associated in vivo with the nucleolar proteins Nop1p and Nop5/58p. Protein sequence analysis reveals that Spb1p possesses a putative S-adenosyl-L-methionine (AdoMet)-binding domain, which is common to the AdoMet-dependent methyltransferases. We show here that Spb1p is able to bind [(3)H]AdoMet in vitro, suggesting that it is a novel methylase, whose possible substrates will be discussed.
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