Mitochondrial gene expression in saccharomyces cerevisiae. I. Optimal conditions for protein synthesis in isolated mitochondria - PubMed (original) (raw)

. 1984 Jul 25;259(14):9320-31.

PMID: 6086632

Free article

Mitochondrial gene expression in saccharomyces cerevisiae. I. Optimal conditions for protein synthesis in isolated mitochondria

E E McKee et al. J Biol Chem. 1984.

Free article

Abstract

An in vitro mitochondrial protein-synthesizing system, which makes use of intact yeast mitochondria, has been developed in order to study mitochondrial gene expression and its control by nuclear-coded proteins. Studies with this system have revealed that: isolated mitochondria synthesize polypeptide gene products which can be radiolabeled to high specific radioactivities when incubated in a "protein-synthesizing medium" that has been optimized with respect to each of its components; two energy-generating systems, endogenous oxidative phosphorylation and an exogenous ATP-regenerating system, support the highest level of protein synthesis; and the omission of an oxidizable substrate results in the synthesis of two new polypeptides (19.5 and 18 kDa) and a decrease in the amounts of cytochrome c oxidase subunits I and II which are synthesized. They have also revealed that added adenine and guanine nucleotides increase the overall level of protein synthesis and that the added guanine nucleotides facilitate polypeptide chain elongation. Although isolated mitochondria which have been optimized for protein synthesis synthesize normal gene products (McKee, E. E., McEwen, J. E., and Poyton, R. O., (1984) J. Biol. Chem. 259, 9332-9338) they still respond to an added dialyzed S-100 fraction from yeast cells by increasing their level of protein synthesis. This stimulation is observed in the presence of optimal concentrations of GTP, making it unlikely that guanyl nucleotides or enzymes which synthesize them are the sole stimulatory factors present in cellular cytosolic fractions, as suggested by Ohashi and Schatz (Ohashi, A., and Schatz, G. (1980) J. Biol. Chem. 255, 7740-7745).

PubMed Disclaimer

Cited by

Phenotypic suppression and nuclear accommodation of the mit- oxi1-V25 mutation in isolated yeast mitochondria.
Zagórski W, Boguta M, Mieszczak M, Claisse M, Guiard B, Spyridakis A, Slonimski PP. Zagórski W, et al. Curr Genet. 1987;12(5):305-10. doi: 10.1007/BF00405752. Curr Genet. 1987. PMID: 3328651
Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA.
Herrmann JM, Stuart RA, Craig EA, Neupert W. Herrmann JM, et al. J Cell Biol. 1994 Nov;127(4):893-902. doi: 10.1083/jcb.127.4.893. J Cell Biol. 1994. PMID: 7962074 Free PMC article.
Identification of potential calorie restriction-mimicking yeast mutants with increased mitochondrial respiratory chain and nitric oxide levels.
Li B, Skinner C, Castello PR, Kato M, Easlon E, Xie L, Li T, Lu SP, Wang C, Tsang F, Poyton RO, Lin SJ. Li B, et al. J Aging Res. 2011 Mar 31;2011:673185. doi: 10.4061/2011/673185. J Aging Res. 2011. PMID: 21584246 Free PMC article.
The absence of a mitochondrial genome in rho0 yeast cells extends lifespan independently of retrograde regulation.
Woo DK, Poyton RO. Woo DK, et al. Exp Gerontol. 2009 Jun-Jul;44(6-7):390-7. doi: 10.1016/j.exger.2009.03.001. Epub 2009 Mar 12. Exp Gerontol. 2009. PMID: 19285548 Free PMC article.
Oxa1p, an essential component of the N-tail protein export machinery in mitochondria.
Hell K, Herrmann JM, Pratje E, Neupert W, Stuart RA. Hell K, et al. Proc Natl Acad Sci U S A. 1998 Mar 3;95(5):2250-5. doi: 10.1073/pnas.95.5.2250. Proc Natl Acad Sci U S A. 1998. PMID: 9482871 Free PMC article.

Mitochondrial gene expression in saccharomyces cerevisiae. I. Optimal conditions for protein synthesis in isolated mitochondria - PubMed (original) (raw)