Bestimmung der Strahlenwirkung auf die Thymidinkinaseaktivität innerhalb eines Zellzyklus synchroner Chlorella / Determination of Irradiation Effects on the Thymidine Kinase Activities Within a Cell-Cycle of Synchronously Growing Chlorella

Ingestigations on the thymidine kinase activities within a cell-cycle of synchronously growing Chlorella cells showed a marked increase of the enzyme-activity towards the end of the DNA-reduplication.Immediately after γ-irradiation with doses of 15 krad and 35 krad, no significant changes in activity could be found; three hours after irradiation a remarkable decrease of the enzyme-activity was observed.

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The Gene Expression and Enzyme Activity of Plant 3-Deoxy-D-Manno-2-Octulosonic Acid-8-Phosphate Synthase Are Preferentially Associated with Cell Division in a Cell Cycle-Dependent Manner

PLANT PHYSIOLOGY ◽

10.1104/pp.103.026872 ◽

2003 ◽

Vol 133 (1) ◽

pp. 348-360 ◽

Cited By ~ 20

Author(s):

Frédéric Delmas ◽

Johann Petit ◽

Jérôme Joubès ◽

Martial Séveno ◽

Thomas Paccalet ◽

...

Keyword(s):

Gene Expression ◽

Cell Cycle ◽

Enzyme Activity ◽

Cell Division ◽

Dependent Manner ◽

A Cell ◽

Cycle Dependent ◽

Phosphate Synthase

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A cell cycle model for the tachyzoite of Toxoplasma gondii using the Herpes simplex virus thymidine kinase

Molecular and Biochemical Parasitology ◽

10.1016/s0166-6851(98)00074-7 ◽

1998 ◽

Vol 94 (2) ◽

pp. 237-247 ◽

Cited By ~ 64

Author(s):

Jay R Radke ◽

Michael W White

Keyword(s):

Cell Cycle ◽

Herpes Simplex Virus ◽

Herpes Simplex ◽

Toxoplasma Gondii ◽

Thymidine Kinase ◽

Cycle Model ◽

A Cell ◽

Simplex Virus

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Overexpression of Thymidine Kinase mRNA Eliminates Cell Cycle Regulation of Thymidine Kinase Enzyme Activity

Journal of Biological Chemistry ◽

10.1074/jbc.271.2.853 ◽

1996 ◽

Vol 271 (2) ◽

pp. 853-860 ◽

Cited By ~ 17

Author(s):

Wolfgang Mikulits ◽

Markus Hengstschläger ◽

Thomas Sauer ◽

Erhard Wintersberger ◽

Ernst W. Müllner

Keyword(s):

Cell Cycle ◽

Enzyme Activity ◽

Thymidine Kinase ◽

Cell Cycle Regulation ◽

Cycle Regulation

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Degradation of human thymidine kinase is dependent on serine-13 phosphorylation: involvement of the SCF-mediated pathway

Biochemical Journal ◽

10.1042/bj20021335 ◽

2003 ◽

Vol 370 (1) ◽

pp. 265-273 ◽

Cited By ~ 9

Author(s):

Po-Yuan KE ◽

Che-Chuan YANG ◽

I-Chun TSAI ◽

Zee-Fen CHANG

Keyword(s):

Cell Cycle ◽

Protein Degradation ◽

Thymidine Kinase ◽

Yeast Cells ◽

Temperature Sensitive ◽

Dependent Manner ◽

Proteolytic Pathway ◽

A Cell ◽

The Stability ◽

Cycle Dependent

The expression level of human thymidine kinase (hTK) is regulated in a cell-cycle-dependent manner. One of the mechanisms responsible for the fluctuation of TK expression in the cell cycle can be attributed to protein degradation during mitosis. Given the facts that cell-cycle-dependent proteolysis is highly conserved in all eukaryotes and yeast cells are an excellent model system for protein-degradation study, here we report on the use of Saccharomyces cerevisiae and Schizosaccharomyces pombe to investigate the degradation signal and mechanism required for hTK degradation. We found that the stability of hTK is significantly reduced in mitotic yeasts. Previously, we have observed that Ser-13 is the site of mitotic phosphorylation of hTK in HeLa cells [Chang, Huang and Chi (1998) J. Biol. Chem. 273, 12095—12100]. Here, we further provide evidence that the replacement of Ser-13 by Ala (S13A) renders hTK stable in S. pombe and S. cerevisiae. Most interestingly, we demonstrated that degradation of hTK is impaired in S. cerevisiae carrying a temperature-sensitive mutation in the proteasomal gene pre1-1 or the Skp1-Cullin-1/CDC53-F-box (SCF) complex gene cdc34 or cdc53, suggesting the contribution of the SCF-mediated pathway in hTK degradation. As phosphorylation is a prerequisite signal for SCF recognition, our results implied that phosphorylation of Ser-13 probably contributes to the degradation signal for hTK via the SCF-mediated proteolytic pathway.

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