scholarly journals Thylakoid Polypeptides of Light and Dark Aged Chloroplasts

1982 ◽  
Vol 70 (3) ◽  
pp. 795-802 ◽  
Author(s):  
Cesar P. dos Santos ◽  
David O. Hall
Keyword(s):  
Thylakoid Polypeptides

scholarly journals Thylakoid polypeptides analysis of intertribal cytoplasmic hybrids

1991 ◽  
Vol 7 (4) ◽  
pp. 39-45
Author(s):  
L. A. Kovler ◽  
L. R. Shlumukov ◽  
Yu. Yu. Gleba
Keyword(s):  
Thylakoid Polypeptides ◽  
Cytoplasmic Hybrids

Photolability of Thylakoid Polypeptides during Photoinhibition in vitro

1986 ◽  
Vol 122 (2) ◽  
pp. 187-192 ◽  
Author(s):  
Peter J. Holloway ◽  
Angela M. Nettleton ◽  
Michael J. Dalling
Keyword(s):  
Thylakoid Polypeptides

Topology of the Thylakoid Polypeptides of Rhodopseudomonas viridis

1984 ◽  
pp. 361-364 ◽  
Author(s):  
Frances Jay ◽  
Marianne Lambillotte ◽  
Franz Wyss ◽  
Rene Brunisholz ◽  
Kurt Muehlethaler
Keyword(s):  
Rhodopseudomonas Viridis ◽  
Thylakoid Polypeptides

scholarly journals Regulation of accumulation of the major thylakoid polypeptides in Chlamydomonas reinhardtii y-1 at 25 degrees C and 38 degrees C.

1982 ◽  
Vol 95 (2) ◽  
pp. 552-558 ◽  
Author(s):  
J K Hoober ◽  
D B Marks ◽  
B J Keller ◽  
M M Margulies
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Messenger Rna ◽  
Cellular Level ◽  
In Vitro Translation ◽  
Molecular Weights ◽  
Thylakoid Polypeptides ◽  
Translatable Mrna ◽  
Membrane Components

The amount of messenger RNA (mRNA) for polypeptides of the chlorophyll a/b-protein complex of thylakoid membranes in etiolated and greening cells of Chlamydomonas reinhardtii y-1 was examined by immunoprecipitation and electrophoresis of products of in vitro translation to determine at which stage production of these polypeptides is regulated. Cells grown 4 d in the dark at 25 degrees C contained small amounts of translatable mRNA for the major membrane polypeptides. Exposure of these etiolated cells to light, under conditions in which the membrane polypeptides accumulated, resulted in a significant increase in the quantity of the mRNA. In contrast, when etiolated cells were incubated for 1-2 h in the dark at 38 degrees C, translation assays indicated that mRNA for the membrane polypeptides became abundant. Moreover, the quantity of the mRNA did not increase when these cells subsequently were exposed to light. Therefore, at 38 degrees C the cellular level of the polypeptides is not regulated by synthesis of mRNA. The in vitro synthesized polypeptides, which were precipitated with antibodies prepared against the purified thylakoid polypeptides, had apparent molecular weights of 31,500 and 30,000. The corresponding immunoprecipitated polypeptides made in vivo had apparent molecular weights of 29,500 and 26,000. Thus, the membrane polypeptides are made as precursors. No net accumulation of the polypeptides occurred in cells in the dark at 38 degrees C, but immunoreactive polypeptides the size of the mature membrane components were labeled during incubation of cells with [14C]acetate in the dark. These results indicated that the mRNA was translated in the dark, but since the polypeptides did not accumulate, the products of translation were probably degraded. We conclude from our experiments that at 25 degrees C production of the polypeptides is regulated by the level of translatable mRNA in the cells. At 38 degrees C, however, the accumulation of the polypeptides is controlled by posttranslational processes.

The "Additional Subunit" CF0II of the Photosynthetic ATP-Synthase and the Thylakoid Polypeptide, Binding Ferredoxin NADP Reductase: Are they Different?

1990 ◽  
Vol 45 (7-8) ◽  
pp. 772-784 ◽  
Author(s):  
Helmut E. Meyer
Keyword(s):  
Molecular Weight ◽  
Atp Synthase ◽  
Binding Protein ◽  
Apparent Molecular Weight ◽  
Amino Acid Sequences ◽  
The Other ◽  
Oxygen Evolving Complex ◽  
Ps Ii ◽  
Thylakoid Polypeptides ◽  
Oxygen Evolving

Abstract Evidence is presented to support the notion that the 16 kDa thylakoid polypeptide, called CF0II, is an essential subunit of the photosynthetic ATP-synthase complex CF0CF1: It is co-isolated with the other subunits of CF0CF1 in preparations either using octylgluco- side/cholate or Triton X-100. It is co-precipitated by antibodies together with the other CF0CF1 subunits. It is immunochemically not related to thylakoid polypeptides of higher molecular weight nor to some thylakoid polypeptides with similar apparent molecular weight be- tween 16 and 18 kDa: CF1ɛ, CF0I, subunit IV of the b6f complex, the 16.5 kDa peripheral poly- peptide of the oxygen evolving complex of PS II, and the intrinsic ferredoxin NADP reductase binding protein. The N-terminal amino acid sequences of CF0II and the reductase binding protein is determined by Edman degradation and compared: The two sequences arc different and not identical to other characterized thylakoid polypeptides. Monospecific antibodies against CF0II inhibit rebinding of CF1 to EDTA treated thylakoid membranes, H+ efflux from EDTA treated membranes and cyclic photophosphorylation. Thus the additional polypeptide CF0II qualifies for a functional subunit of the photosynthetic ATP-synthase.

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