PMID- 10648622
OWN - NLM
STAT- MEDLINE
DCOM- 20000215
LR  - 20190508
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 20
IP  - 4
DP  - 2000 Feb
TI  - Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that is able 
      to bind S-adenosyl-L-methionine in vitro.
PG  - 1370-81
AB  - 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.
FAU - Pintard, L
AU  - Pintard L
AD  - Centre de Recherche de Biochimie Macromoleculaire du CNRS, 34293 Montpellier,
      France.
FAU - Kressler, D
AU  - Kressler D
FAU - Lapeyre, B
AU  - Lapeyre B
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (DNA Primers)
RN  - 0 (Fungal Proteins)
RN  - 0 (NOP1 protein, S cerevisiae)
RN  - 0 (NOP58 protein, S cerevisiae)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Poly(A)-Binding Proteins)
RN  - 0 (RNA, Fungal)
RN  - 0 (RNA, Ribosomal)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Ribonucleoproteins)
RN  - 0 (Ribonucleoproteins, Small Nucleolar)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 7LP2MPO46S (S-Adenosylmethionine)
RN  - EC 2.1.1.- (Methyltransferases)
RN  - EC 2.1.1.- (SPB1 protein, S cerevisiae)
SB  - IM
MH  - Alleles
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Conserved Sequence
MH  - DNA Primers/genetics
MH  - Evolution, Molecular
MH  - Fungal Proteins/genetics/*metabolism
MH  - Gene Deletion
MH  - Genes, Fungal
MH  - Genetic Complementation Test
MH  - *Methyltransferases
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Nuclear Proteins/genetics/*metabolism
MH  - Poly(A)-Binding Proteins
MH  - Protein Binding
MH  - RNA Processing, Post-Transcriptional
MH  - RNA, Fungal/biosynthesis
MH  - RNA, Ribosomal/biosynthesis
MH  - RNA-Binding Proteins/genetics/metabolism
MH  - Ribonucleoproteins/*metabolism
MH  - *Ribonucleoproteins, Small Nucleolar
MH  - S-Adenosylmethionine/*metabolism
MH  - Saccharomyces cerevisiae/genetics/*metabolism
MH  - *Saccharomyces cerevisiae Proteins
MH  - Sequence Homology, Amino Acid
MH  - Suppression, Genetic
MH  - Temperature
PMC - PMC85287
EDAT- 2000/01/29 09:00
MHDA- 2000/04/01 09:00
CRDT- 2000/01/29 09:00
PHST- 2000/01/29 09:00 [pubmed]
PHST- 2000/04/01 09:00 [medline]
PHST- 2000/01/29 09:00 [entrez]
AID - 10.1128/mcb.20.4.1370-1381.2000 [doi]
PST - ppublish
SO  - Mol Cell Biol. 2000 Feb;20(4):1370-81. doi: 10.1128/mcb.20.4.1370-1381.2000.