Thylakoid protein phosphorylation: in vitro and in vivo

1984 ◽  
Vol 12 (5) ◽  
pp. 771-774 ◽  
Author(s):  
JOHN BENNETT
Keyword(s):  
Protein Phosphorylation ◽  
Thylakoid Protein ◽  
Thylakoid Protein Phosphorylation

scholarly journals Use of Zinc Ions To Study Thylakoid Protein Phosphorylation and the State 1-State 2 Transition In Vitro

1984 ◽  
Vol 74 (2) ◽  
pp. 348-354 ◽  
Author(s):  
John P. Markwell ◽  
Neil R. Baker ◽  
Michael Bradbury ◽  
J. Philip Thornber
Keyword(s):  
Protein Phosphorylation ◽  
The State ◽  
Zinc Ions ◽  
Thylakoid Protein ◽  
State 1 ◽  
Thylakoid Protein Phosphorylation

Microtubule-entrained kinase activities associated with the cortical cytoskeleton during cytokinesis

1997 ◽  
Vol 110 (12) ◽  
pp. 1373-1386 ◽  
Author(s):  
G.R. Walker ◽  
C.B. Shuster ◽  
D.R. Burgess
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Immunoblot Analysis ◽  
Negative Regulator ◽  
Mitogen Activated Protein Kinase ◽  
Mitotic Apparatus ◽  
Cortical Cytoskeleton

Research over the past few years has demonstrated the central role of protein phosphorylation in regulating mitosis and the cell cycle. However, little is known about how the mechanisms regulating the entry into mitosis contribute to the positional and temporal regulation of the actomyosin-based contractile ring formed during cytokinesis. Recent studies implicate p34cdc2 as a negative regulator of myosin II activity, suggesting a link between the mitotic cycle and cytokinesis. In an effort to study the relationship between protein phosphorylation and cytokinesis, we examined the in vivo and in vitro phosphorylation of actin-associated cortical cytoskeletal (CSK) proteins in an isolated model of the sea urchin egg cortex. Examination of cortices derived from eggs or zygotes labeled with 32P-orthophosphate reveals a number of cortex-associated phosphorylated proteins, including polypeptides of 20, 43 and 66 kDa. These three major phosphoproteins are also detected when isolated cortices are incubated with [32P]ATP in vitro, suggesting that the kinases that phosphorylate these substrates are also specifically associated with the cortex. The kinase activities in vivo and in vitro are stimulated by fertilization and display cell cycle-dependent activities. Gel autophosphorylation assays, kinase assays and immunoblot analysis reveal the presence of p34cdc2 as well as members of the mitogen-activated protein kinase family, whose activities in the CSK peak at cell division. Nocodazole, which inhibits microtubule formation and thus blocks cytokinesis, significantly delays the time of peak cortical protein phosphorylation as well as the peak in whole-cell histone H1 kinase activity. These results suggest that a key element regulating cortical contraction during cytokinesis is the timing of protein kinase activities associated with the cortical cytoskeleton that is in turn regulated by the mitotic apparatus.

scholarly journals Evidence for different kinases in thylakoid protein phosphorylation

1987 ◽  
Vol 248 (1) ◽  
pp. 103-108 ◽  
Author(s):  
C H Foyer
Keyword(s):  
Electron Transport ◽  
Protein Kinase ◽  
Photosystem Ii ◽  
Protein Phosphorylation ◽  
System A ◽  
Intact Chloroplasts ◽  
Thylakoid Protein ◽  
Dimethyl Urea ◽  
Thylakoid Protein Phosphorylation ◽  
Differential Action

Thylakoid protein phosphorylation was facilitated in darkness by using the ferredoxin-NADPH system. CoCl2 and DBMIB (2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone) were potent inhibitors of LHCP (light-harvesting chlorophyll-binding protein) phosphorylation, but 3-(3,4-dichlorophenyl)-1,1-dimethyl-urea and atrazine had no significant effect. Differential effects on phosphorylation of the 9 kDa polypeptide and LHCP were observed in darkness with DBMIB and certain other inhibitors specific for Photosystem-II electron transport. Similarly, during illumination of intact chloroplasts or of the reconstituted chloroplast system, a differential action of bicarbonate was observed on the relative phosphorylation of the two proteins. The degree of phosphorylation of the 9 kDa polypeptide was increased in the presence of bicarbonate compared with its absence, whereas that of LHCP was relatively unchanged. Changes in the degree of phosphorylation of the 32 kDa polypeptide in these experiments did not correlate consistently with changes in phosphorylation of either LHCP or the 9 kDa polypeptide, although changes in the 32 kDa polypeptide more often paralleled phosphorylation of the 9 kDa polypeptide rather than the phosphorylation of LHCP. These observations suggest that the protein kinase that phosphorylates LHCP is distinct from that which phosphorylates the 9 kDa polypeptide.

Rapid and highly specific monitoring of reversible thylakoid protein phosphorylation by polyclonal antibody to phosphothreonine-containing proteins

2002 ◽  
Vol 159 (4) ◽  
pp. 371-377 ◽  
Author(s):  
Elena Bergo ◽  
Saijliisa Pursiheimo ◽  
Virpi Paakkarinen ◽  
Giorgio M. Giacometti ◽  
Arianna Donella-Deana ◽  
...  
Keyword(s):  
Protein Phosphorylation ◽  
Polyclonal Antibody ◽  
Thylakoid Protein ◽  
Thylakoid Protein Phosphorylation
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