Mitochondrial ATPase complex from Neurospora crassa.

نویسندگان

  • W Sebald
  • G Wild
چکیده

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Synthesis of a larger precursor for the proteolipid subunit of the mitochondrial ATPase complex of Neurospora crassa in a cell-free wheat germ system.

The proteolipid subunit of the ATPase complex from Neuraspara crassa [ 1] is synthesized on cytoplasmic ribosomes [2] and coded for by a nuclear gene [3]. This raises the question of how this extremely hydrophobic protein [ 4] is transported into the mitochondria and how it is assembled with the numerous other subunit polypeptides to form the functional ATPase complex located in the mitochondri...

متن کامل

The dicyclohexylcarbodiimide-binding protein of the mitochondrial ATPase complex from Neurospora crassa and Saccharomyces cerevisiae. Identification and isolation.

Incubation of mitochondria from Neurospora crassa and Saccharomyces cerevisiae with the radioactive ATPase inhibitor [14C]dicyclohexylcarbodiimide results in the irreversible and rather specific labelling of a low-molecular-weight polypeptide. This dicyclohexylcarbodiimide-binding protein is identical with the smallest subunit (Mr 8000) of the mitochondrial ATPase complex, and it occurs as olig...

متن کامل

Identification of two products of mitochondrial protein synthesis associated with mitochondrial adenosine triphosphatase from Neurospora crassa.

Soluble mitochondrial ATPase (F1) isolated from Neurospora crassa is resolved by dodecylsulfate-gel electrophoresis into five polypeptide bands with apparent molecular weights of 59000, 55000, 36000, 15000 and 12000. At least nine further polypeptides remain associated with ATPase after disintegration of mitochondria with Triton X-100 as shown by the analysis of an immunoprecipitate obtained wi...

متن کامل

Structural studies of the vacuolar membrane ATPase from Neurospora crassa and comparison with the tonoplast membrane ATPase from Zea mays.

The H+-translocating ATPase located on vacuolar membranes of Neurospora crassa was partially purified by solubilization in two detergents, Triton X-100 and N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate, followed by centrifugation on sucrose density gradients. Two polypeptides of Mr approximately equal to 70,000 and approximately equal to 62,000 consistently migrated with activity, along...

متن کامل

Nucleotide sequence of a full-length cDNA coding for the mitochondrial precursor protein of the beta-subunit of F1-ATPase from Neurospora crassa.

Subunits of mitochondrial H-ATPases are investigated under a variety of different aspects: (i) mechanisms of energy coupling (1, 2); (ii) evolution of ATPases (3) and (iii) mechanisms of mitochondrial import and assembly of the nuclear coded subunits (4—7). For the latter reason, we have cloned and expressed a full-length cDNA coding for the nuclear coded /8-subunit of the Fj-ATPase from Neuros...

متن کامل

ذخیره 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 نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Methods in enzymology

دوره 55  شماره 

صفحات  -

تاریخ انتشار 1979