Literature DB >> 410815

Nonidentity of ribosomal structural proteins in growing and starved Tetrahymena.

R L Hallberg, C A Sutton.   

Abstract

We have examined the ribosomal structural proteins isolated from vegetatively growing Tetrahymena pyriformis and from cells that had been starved of all nutrients for 24 h. Reproducible, nonartifactual differences in protein complement, primarily associated with the large ribosomal subunit, were found. The kinetics of change in ribosomal protein complement were followed both in refed and in newly starved cells. Furthermore, attempts at correlating a certain protein "phenotype" with a particular functional state of the ribosome were made. It was concluded that the alterations seen could not be correlated with a specific stage in the normal ribosome cycle. We did show, however, that the change in protein complement could occur as a result of altering preexisting ribosomes. In addition, we showed that the change correlates with a decrease in growth rate rather than being caused by the starvation conditions themselves. Speculations as to the functional significance of the protein changes are presented.

Entities:  

Mesh:

Substances:

Year:  1977        PMID: 410815      PMCID: PMC2111568          DOI: 10.1083/jcb.75.1.268

Source DB:  PubMed          Journal:  J Cell Biol        ISSN: 0021-9525            Impact factor:   10.539


  11 in total

Review 1.  Growth and differentiation of the water mold Blastocladiella emersonii: cytodifferentiation and the role of ribonucleic acid and protein synthesis.

Authors:  J S Lovett
Journal:  Bacteriol Rev       Date:  1975-12

2.  Heterogeneity of native ribosomal 60-S subunits in Ehrlich ascites tumor cells cultured in vitro.

Authors:  W J Venrooij; A P Janssen
Journal:  Eur J Biochem       Date:  1976-10-01

3.  Temperature sensitive mutations affecting ribosome synthesis in Saccharomyces cerevisiae.

Authors:  J R Warner; S A Udem
Journal:  J Mol Biol       Date:  1972-03-28       Impact factor: 5.469

4.  The ribosome cycle in mammalian protein synthesis. I. The place of monomeric ribosomes and ribosomal subunits in the cycle.

Authors:  E C Henshaw; D G Guiney; C A Hirsch
Journal:  J Biol Chem       Date:  1973-06-25       Impact factor: 5.157

5.  Relationship of cellular energetics to RNA metabolism in Tetrahymena pyriformis W.

Authors:  R L Conner; M J Koroly
Journal:  J Protozool       Date:  1974-02

6.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

7.  Sporulation-specific translational discrimination in Bacillus subtilis.

Authors:  T Leighton
Journal:  J Mol Biol       Date:  1974-07-15       Impact factor: 5.469

8.  Free ribosomes in physiologically nondividing cells. Human peripheral lymphocytes.

Authors:  H L Cooper; S L Berger; R Braverman
Journal:  J Biol Chem       Date:  1976-08-25       Impact factor: 5.157

9.  The ribosomal proteins of Saccharomyces cerevisiae. Phosphorylated and exchangeable proteins.

Authors:  S Zinker; J R Warner
Journal:  J Biol Chem       Date:  1976-03-25       Impact factor: 5.157

10.  Ribosome biosynthesis in Tetrahymena pyriformis. Regulation in response to nutritional changes.

Authors:  R L Hallberg; P J Bruns
Journal:  J Cell Biol       Date:  1976-11       Impact factor: 10.539

View more
  3 in total

1.  Analysis of RNA and protein synthesis in temperature-sensitive mutants of Tetrahymena pyriformis.

Authors:  R L Hallberg; L R Gritz; P Sylvan
Journal:  Mol Gen Genet       Date:  1978-01-17

2.  Starved Tetrahymena thermophila cells that are unable to mount an effective heat shock response selectively degrade their rRNA.

Authors:  R L Hallberg; K W Kraus; R C Findly
Journal:  Mol Cell Biol       Date:  1984-10       Impact factor: 4.272

3.  The breakdown of Tetrahymena ribosomes in vivo. The effects of inhibitors.

Authors:  H G Klemperer; D J Pilley
Journal:  Biochem J       Date:  1982-12-15       Impact factor: 3.857

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.