The Biogenesis of Mitochondria

Ashwell, Margaret; Work, T. S.

doi:10.1146/annurev.bi.39.070170.001343

Cited by 368 publications

(93 citation statements)

References 114 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…When S. cerevisiae, N. crassa, or mammalian cells are labeled in the presence of cycloheximide, 8-10 prominant radioactive protein bands are seen in polyacrylamide gels of mitochondria solubilized with sodium dodecyl sulfate (19,20). Minor bands are also occasionally observed but they most likely arise from incomplete inhibition of cytoplasmic protein synthesis.…”

Section: In Vivo Studiesmentioning

confidence: 99%

Mitochondrial Genes and Translation Products

Tzagoloff¹,

Macino²

1979

Annu. Rev. Biochem.

245

View full text Add to dashboard Cite

Section: In Vivo Studiesmentioning

confidence: 99%

Mitochondrial Genes and Translation Products

Tzagoloff¹,

Macino²

1979

Annu. Rev. Biochem.

245

View full text Add to dashboard Cite

“…Since that time, numerous studies have detailed this process in mitochondria isolated from mammalian and insect tissues, as well as from cultured mammalian cells, yeast, fungi, and plants (cf. [2,31). In these studies, it was demonstrated that amino acid incorporation by isolated mitochondria was not due to either microsomal [4] or bacterial contamination [5, 61. In recent publications, Hochberg et al [7,81 have suggested that mitochondrial protein synthesis in vitro may be an artifact resulting from specific binding of radioactive amino acids to mitochondrial protein-lipid structures.…”

Section: Introductionmentioning

confidence: 99%

Mitochondrial protein synthesis in vitro is not an artifact

1973

View full text Add to dashboard Cite

“…Chloramphenicol treatment of the rats was investigated to establish whether this inhibitor of mitochondrial protein synthesis [29,30] had any short term effects on luteal mitochondrial cholesterol metabolism. It has been reported that chloramphenicol inhibits the synthesis of adrenal cortex mitochondrial cytochrome P-450 [31].…”

Section: Discussionmentioning

confidence: 99%

The Effect of Inhibitors of Protein Synthesis on Cholesterol Side‐Chain Cleavage in the Mitochondria of Luteinized Rat Ovaries

Arthur

Boyd

1974

European Journal of Biochemistry

View full text Add to dashboard Cite

Conversion of cholesterol to pregnenolone, termed cholesterol side‐chain cleavage, has been studied in isolated mitochondria from luteinized rat ovaries. Cholesterol in these mitochondria in the presence of cyanoketone is converted to one product pregnenolone on addition of a suitable electron donor. The percentage conversion of total mitochondrial cholesterol to pregnenolone is comparable to that measured by the percentage conversion of [4‐14C]cholesterol to [4‐14C]pregnenolone when the label has been preincubated at 29°C for 10 min with the mitochondria. In mitochondrial incubations the depletion of endogenous cholesterol follows the production of pregnenolone. The initial rate of production of pregnenolone (0.8 nmol × mg protein−1× min−1) was maintained in incubations for 5–6 min. Addition of free cholesterol to incubations allowed the production of pregnenolone to continue at the initial rate for at least 30 min. Treatment of rats with cycloheximide 20 min prior to killing, caused a 58% inhibition of luteal mitochondrial cholesterol side‐chain cleavage and a small but significant rise in the cholesterol content of isolated mitochondria. The cycloheximide treatment did not affect the total luteal mitochondrial cytochrome P‐450 but caused a 56% decrease in the inverted type I pregnenolone‐binding spectrum, suggesting cholesterol binding to cytochrome P‐450 had been reduced. Rats treated with chloramphenicol 3 and 10 h before killing exhibited no differences in total luteal mitochondrial cytochrome P‐450 or mitochondrial cholesterol metabolism when contrasted with saline‐injected animals. Puromycin was shown to bind to the rat luteal mitochondrial cytochrome P‐450 to produce a type I1 difference spectrum and to inhibit luteal mitochondrial cholesterol side‐chain cleavage in vitro. The results are discussed in terms of a protein which is rapidly turning over and which may be synthesised extra‐mitochondrially and in some way affect the binding of cholesterol to luteal mitochondrial cytochrome P‐450.

show abstract

The Biogenesis of Mitochondria

Cited by 368 publications

References 114 publications

Mitochondrial Genes and Translation Products

Mitochondrial Genes and Translation Products

Mitochondrial protein synthesis in vitro is not an artifact

The Effect of Inhibitors of Protein Synthesis on Cholesterol Side‐Chain Cleavage in the Mitochondria of Luteinized Rat Ovaries

Contact Info

Product

Resources

About