Characterization of mitochondrial ribosomes from yeast.
نویسندگان
چکیده
A method for the preparation of mitochondrial ribosomes from yeast is presented. Mitochondrial ribosomes differ from their cytoplasmic counterpart in nucleotide composition, electrophoretic mobility of a number of their respective ribosomal proteins, and thermal denaturation profiles. The mitochondrial and cytoplasmic ribosomes have identical sedimentation coefficients (80 S) and dissociate into 60S and 40S subunits. These findings demonstrate that, in yeast, mitochondrial ribosomes are distinct from cytoplasmic ribosomes.
منابع مشابه
Characterization of New Mutants in the 16s Ribosomal Subunit Region of the Mitochondrial Genome of Saccharomyces Cerevisiae
............................................................................. ix Introduction ......................................................................... 1 Yeast Life Cycle............................................................. 2 Mitochondria..................................................................4 Nuclear vs. Mitochondrial Inheritance.................................
متن کاملCyclic AMP receptor protein from yeast mitochondria: submitochondrial localization and preliminary characterization.
We have identified and characterized a cyclic AMP receptor protein in mitochondria of the yeast Saccharomyces cerevisiae. The binding is specific for cyclic nucleotides, particularly for cyclic AMP which is bound with high affinity (Kd of 10(-9) M) at 1 to 5 pmol/mg of mitochondrial protein. The mitochondrial cyclic AMP receptor is synthesized on cytoplasmic ribosomes and has an apparent molecu...
متن کاملMitochondrial ribosomal proteins (MRPs) of yeast.
Mitochondrial ribosomal proteins (MRPs) are the counterparts in that organelle of the cytoplasmic ribosomal proteins in the host. Although the MRPs fulfil similar functions in protein biosynthesis, they are distinct in number, features and primary structures from the latter. Most progress in the eludication of the properties of individual MRPs, and in the characterization of the corresponding g...
متن کاملThe sensitivity of rat liver and yeast mitochondrial ribosomes to inhibitors of protein synthesis.
Amino acid incorporation by isolated intact rat liver mitochondria was severely inhibited by chloramphenicol, carbomycin, or sparsomycin, partially inhibited by emetine, and unatIected by erytbromycin or lincomycin. By contrast, amino acid incorporation by inner membrane-matrix fractions prepared from rat liver mitochondria by digitonin was strongly inhibited by emetine, erythromycin, and linco...
متن کاملCytochrome c oxidase from bakers' yeast. III. Physical characterization of isolated subunits and chemical evidence for two different classes of polypeptides.
Earlier studies have shown that cytochrome c oxidase from bakers' yeast is an oligomeric enzyme which contains three polypeptides (I to III) synthesized on mitochondrial ribosomes and four polypeptides (IV to VII) synthesized on cytoplasmic ribosomes. These polypeptide subunits have now been isolated by a simple protocol which utilizes differences in polypeptide charge, solubility, and size. Th...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 68 2 شماره
صفحات -
تاریخ انتشار 1971