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The fate of membrane-bound ribosomes following the termination of protein synthesis.

Publication ,  Journal Article
Seiser, RM; Nicchitta, CV
Published in: J Biol Chem
October 27, 2000

Contemporary models for protein translocation in the mammalian endoplasmic reticulum (ER) identify the termination of protein synthesis as the signal for ribosome release from the ER membrane. We have utilized morphometric and biochemical methods to assess directly the fate of membrane-bound ribosomes following the termination of protein synthesis. In these studies, tissue culture cells were treated with cycloheximide to inhibit elongation, with pactamycin to inhibit initiation, or with puromycin to induce premature chain termination, and ribosome-membrane interactions were subsequently analyzed. It was found that following the termination of protein synthesis, the majority of ribosomal particles remained membrane-associated. Analysis of the subunit structure of the membrane-bound ribosomal particles remaining after termination was conducted by negative stain electron microscopy and sucrose gradient sedimentation. By both methods of analysis, the termination of protein synthesis on membrane-bound ribosomes was accompanied by the release of small ribosomal subunits from the ER membrane; the majority of the large subunits remained membrane-bound. On the basis of these results, we propose that large ribosomal subunit release from the ER membrane is regulated independently of protein translocation.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

October 27, 2000

Volume

275

Issue

43

Start / End Page

33820 / 33827

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Ribosomes
  • Protein Biosynthesis
  • Microscopy, Electron
  • Humans
  • Endoplasmic Reticulum
  • Biochemistry & Molecular Biology
  • 34 Chemical sciences
  • 32 Biomedical and clinical sciences
  • 31 Biological sciences
 

Citation

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Seiser, R. M., & Nicchitta, C. V. (2000). The fate of membrane-bound ribosomes following the termination of protein synthesis. J Biol Chem, 275(43), 33820–33827. https://doi.org/10.1074/jbc.M004462200
Seiser, R. M., and C. V. Nicchitta. “The fate of membrane-bound ribosomes following the termination of protein synthesis.J Biol Chem 275, no. 43 (October 27, 2000): 33820–27. https://doi.org/10.1074/jbc.M004462200.
Seiser RM, Nicchitta CV. The fate of membrane-bound ribosomes following the termination of protein synthesis. J Biol Chem. 2000 Oct 27;275(43):33820–7.
Seiser, R. M., and C. V. Nicchitta. “The fate of membrane-bound ribosomes following the termination of protein synthesis.J Biol Chem, vol. 275, no. 43, Oct. 2000, pp. 33820–27. Pubmed, doi:10.1074/jbc.M004462200.
Seiser RM, Nicchitta CV. The fate of membrane-bound ribosomes following the termination of protein synthesis. J Biol Chem. 2000 Oct 27;275(43):33820–33827.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

October 27, 2000

Volume

275

Issue

43

Start / End Page

33820 / 33827

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Ribosomes
  • Protein Biosynthesis
  • Microscopy, Electron
  • Humans
  • Endoplasmic Reticulum
  • Biochemistry & Molecular Biology
  • 34 Chemical sciences
  • 32 Biomedical and clinical sciences
  • 31 Biological sciences