Ribosome binding to mitochondria is regulated by GTP and the transit peptide

Kathleen S. Crowley, R. Payne

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

The association between ribosomes and the pore proteins at the endoplasmic reticulum membrane is important to co-translational translocation. To determine if a similar association occurs between the ribosome and mitochondrial membrane protein(s) during protein import in higher eukaryotes, we examined ribosome-mitochondria binding. By using spectral measurements, analysis of mitochondrial associated RNA, and electron microscopy, we demonstrated that ribosomes stably bind to purified rat liver mitochondria in vitro. Binding of ribosomes to mitochondria was markedly reduced by GTP and nearly abolished by the non-hydrolyzable GTP analogue, guanosine-5'-[thio]-triphosphate (GTPγS), but was only modestly reduced by GDP or ATP and unaffected by CTP. The initial rate of GTP hydrolysis by mitochondria was increased by ribosomes, whereas the rate of ATP hydrolysis by mitochondria was not affected. Ribosomes programmed with mRNA for 92 amino acids of the N terminus of mitochondrial malate dehydrogenase bound to mitochondria, but unlike unprogrammed rat liver ribosomes, neither GTP nor GDP disrupted binding; however, GTPγS did. These data show that receptors specific for ribosomes are present on the mitochondrial membrane, and a GTP- dependent process mediates this binding. The presence of a nascent chain alters these binding characteristics. These findings support the hypothesis that a co-translational translocation pathway exists for import of proteins into mitochondria.

Original languageEnglish (US)
Pages (from-to)17278-17285
Number of pages8
JournalJournal of Biological Chemistry
Volume273
Issue number27
DOIs
StatePublished - Jul 3 1998
Externally publishedYes

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Mitochondria
Guanosine Triphosphate
Ribosomes
Peptides
Mitochondrial Membranes
Liver
Rats
Hydrolysis
Adenosine Triphosphate
Association reactions
Membranes
Cytidine Triphosphate
Porins
Malate Dehydrogenase
Guanosine
Liver Mitochondrion
Mitochondrial Proteins
Electron microscopy
Eukaryota
Endoplasmic Reticulum

ASJC Scopus subject areas

  • Biochemistry

Cite this

Ribosome binding to mitochondria is regulated by GTP and the transit peptide. / Crowley, Kathleen S.; Payne, R.

In: Journal of Biological Chemistry, Vol. 273, No. 27, 03.07.1998, p. 17278-17285.

Research output: Contribution to journalArticle

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