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PMID: 2666845 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Synthesis of ribosomes in Saccharomyces cerevisiae.

Microbiological reviews ·Vol. 53 ·No. 2 ·1989-06-00 ·Pages 256-71

Warner JR

Abstract

The assembly of a eucaryotic ribosome requires the synthesis of four ribosomal ribonucleic acid (RNA) molecules and more than 75 ribosomal proteins. It utilizes all three RNA polymerases; it requires the cooperation of the nucleus and the cytoplasm, the processing of RNA, and the specific interaction of RNA and protein molecules. It is carried out efficiently and is exquisitely sensitive to the needs of the cell. Our current understanding of this process in the genetically tractable yeast Saccharomyces cerevisiae is reviewed. The ribosomal RNA genes are arranged in a tandem array of 100 to 200 copies. This tandem array has led to unique ways of carrying out a number of functions. Replication is asymmetric and does not initiate from every autonomously replicating sequence. Recombination is suppressed. Transcription of the major ribosomal RNA appears to involve coupling between adjacent transcription units, which are separated by the 5S RNA transcription unit. Genes for many ribosomal proteins have been cloned and sequenced. Few are linked; most are duplicated; most have an intron. There is extensive homology between yeast ribosomal proteins and those of other species. Most, but not all, of the ribosomal protein genes have one or two sites that are essential for their transcription and that bind a common transcription factor. This factor binds also to many other places in the genome, including the telomeres. There is coordinated transcription of the ribosomal protein genes under a variety of conditions. However, the cell seems to possess no mechanism for regulating the transcription of individual ribosomal protein genes in response either to a deficiency or an excess of a particular ribosomal protein. A deficiency causes slow growth. Any excess ribosomal protein is degraded very rapidly, with a half-life of 1 to 5 min. Unlike most types of cells, yeast cells appear not to regulate the translation of ribosomal proteins. However, in the case of ribosomal protein L32, the protein itself causes a feedback inhibition of the splicing of the transcript of its own gene. The synthesis of ribosomes involves a massive transfer of material across the nuclear envelope in both directions. Nuclear localization signals have been identified for at least three ribosomal proteins; they are similar but not identical to those identified for the simian virus 40 T antigen. There is no information about how ribosomal subunits are transported from the nucleus to the cytoplasm.(ABSTRACT TRUNCATED AT 400 WORDS)

MeSH Terms
DNA Replication DNA, Fungal/biosynthesis,genetics DNA, Ribosomal/biosynthesis,genetics RNA Splicing RNA, Fungal/biosynthesis,genetics RNA, Ribosomal/biosynthesis,genetics Ribosomal Proteins/biosynthesis,genetics Ribosomes Saccharomyces cerevisiae/genetics Transcription, Genetic
Chemicals
DNA, Fungal DNA, Ribosomal RNA, Fungal RNA, Ribosomal Ribosomal Proteins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Warner J R
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Article Info
Journal
Microbiological reviews
Abbr.
Microbiol Rev
ISSN
0146-0749
DOI
10.1128/mr.53.2.256-271.1989
Published
1989-06-00
Pages
256-71
Language
English
Region
United States
NLM ID
7806086
PMCID
PMC372731
Subset
IM
Grants
NCI NIH HHS · CA13330 · United States
NIGMS NIH HHS · GM25532 · United States
External Links
PubMed source DOI: 10.1128/mr.53.2.256-271.1989 PMC Full Text
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