Reconstitution of cyanobacterial photophosphorylation by a latent Ca2+-ATPase.

نویسندگان

  • L Owers-Narhi
  • S J Robinson
  • C S DeRoo
  • C F Yocum
چکیده

RECONSTITUTION OF CYANOBACTERIAL PHOTOPHOSPHORYLATION BY A LATENT Cat2-ATPase Linda Owers-Narhi, Steven J. Robinson*, Cathy Selvius DeRoo, and C.F. Yocum* Division of Biological Sciences The University of Michigan Ann Arbor, Mi. 48109 Received August 16,1979 Summary: Photosynthetic membranes derived from sonic extracts of the cyanobacterium Spirulina platensis contain a latent Ca+2-ATPase which is activated by exposure to trypsin. When sonic membranes are washed with ethylenediaminetetraacetic acid, the ATPase is removed from these membranes with an accompanying loss of photophosphorylation activity. The latent ATPase activity solubilized by washing has been partially purified, and addition of the enzyme to depleted membranes restores photophosphorylation activity to levels approaching 50% of the rates observed in unwashed membranes. These data indicate that this ATPase is the coupling factor responsible forphotosynthetic energy transduction in Spirulina platensis.

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

Properties of the cyanobacterial coupling factor ATPase from Spirulina platensis. I. Electrophoretic characterization and reconstitution of photophosphorylation.

The coupling factor ATPase (F1) from photosynthetic membranes of the cyanobacterium Spirulina platensis was purified to homogeneity by a combination of ion-exchange chromatography and sucrose density gradient centrifugation. The ATPase activity of purified Spirulina F1 is latent but can be elicited by trypsin treatment, resulting in specific activities (CaATPase) of 27-37 mumol Pi min-1 mg prot...

متن کامل

A Cyanobacterial ATPase Distinct from the Coupling Factor of Photophosphorylation

A particle-bound, Mg2+-dependent ATPase activity is investigated in cell-free extracts o f the cyanobacterium Anabaena variabilis. The enzyme can be clearly distinguished from the cyanobacterialcoupling factor o f photophosphoiylation and from the alkaline phosphatase. It requires low concentrations o f Ca2+ for maximal activity and is inhibited by orz/io-vanadate, indicating that the enzyme ma...

متن کامل

Immunological evidence for the presence of latent Ca2 dependent ATPase and carboxydismutase on the thylakoid surface.

Antibodies were prepared against carboxydismutase and latent Ca2® dependent ATPase (coupling factor) purified from Nicotiana tabacum. The antibodies against carboxydismutase inhi­ bit the enzymatic activity of the purified protein, while those against coupling factor inhibit the Ca2© dependent ATPase activity of the protein as well as the photophosphorylation of the chloro­ plasts. The antisera...

متن کامل

Studies on the Retention of CFt with or without Induced ATPase Activity by Pyrophosphate Treated Thylakoids and Its Relation to the Regeneration of Photophosphorylation

The reconstitution of chloroplast coupling factor 1 (CFj) into thylakoid membranes was in­ vestigated by the fluorescence of the covalently attached label fluorescamine. In contrast to a func­ tional regeneration of ATP synthesis, a rebinding of CFX was observed regardless if the protein was in its native, purified state or had been activated for ATPase activity by heat, dithiothreitol (DTT) or...

متن کامل

Coupling factor adenosine-5'-triphosphatase from Rhodospirillum rubrum: a simple and rapid procedure for its purification.

When photosynthetic membranes from Rhodospirillum rubrum, devoid of loosely bound small molecules and proteins, were passed through a French-pressure cell, the enzyme adenosine-5'-triphosphatase (EC 3.6.1.3.) (ATPase) was released into the soluble fraction. The solubilized ATPase was purified to homogeneity. In many respects it behaved like the enzyme purified by other workers, but it also hydr...

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:
  • Biochemical and biophysical research communications

دوره 90 3  شماره 

صفحات  -

تاریخ انتشار 1979