Regulation of CDC9, the Saccharomyces cerevisiae gene that encodes DNA ligase

1985 ◽  
Vol 5 (1) ◽  
pp. 226-235
Author(s):  
T A Peterson ◽  
L Prakash ◽  
S Prakash ◽  
M A Osley ◽  
S I Reed
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Steady State ◽  
Uv Light ◽  
State Level ◽  
S Phase ◽  
Dna Ligase ◽  
Mrna Levels ◽  
Steady State Level ◽  
High Level

We have cloned CDC9, the structural gene for Saccharomyces cerevisiae DNA ligase, and investigated its transcriptional regulation both as a function of cell cycle stage and after UV irradiation. The steady-state level of DNA ligase mRNA increases at least fourfold in late G1, after the completion of start but before S phase. This high level of CDC9 mRNA then decays with an apparent half-life of ca. 20 min and remains at a low basal level throughout the rest of the cell cycle. The accumulation of CDC9 mRNA in late G1 is dependent upon the completion of start but not the CDC7 and CDC8 functions. Exposure of cells to UV light elicits an eightfold increase in DNA ligase mRNA levels.

scholarly journals Regulation of CDC9, the Saccharomyces cerevisiae gene that encodes DNA ligase.

1985 ◽  
Vol 5 (1) ◽  
pp. 226-235 ◽  
Author(s):  
T A Peterson ◽  
L Prakash ◽  
S Prakash ◽  
M A Osley ◽  
S I Reed
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Steady State ◽  
Uv Light ◽  
State Level ◽  
S Phase ◽  
Dna Ligase ◽  
Mrna Levels ◽  
Steady State Level ◽  
High Level

We have cloned CDC9, the structural gene for Saccharomyces cerevisiae DNA ligase, and investigated its transcriptional regulation both as a function of cell cycle stage and after UV irradiation. The steady-state level of DNA ligase mRNA increases at least fourfold in late G1, after the completion of start but before S phase. This high level of CDC9 mRNA then decays with an apparent half-life of ca. 20 min and remains at a low basal level throughout the rest of the cell cycle. The accumulation of CDC9 mRNA in late G1 is dependent upon the completion of start but not the CDC7 and CDC8 functions. Exposure of cells to UV light elicits an eightfold increase in DNA ligase mRNA levels.

scholarly journals Post-translational processing of urea amidolyase in Saccharomyces cerevisiae.

1982 ◽  
Vol 2 (7) ◽  
pp. 800-804 ◽  
Author(s):  
R A Sumrada ◽  
G Chisholm ◽  
T G Cooper
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Steady State ◽  
State Level ◽  
Steady State Level ◽  
Prosthetic Group ◽  
Apparent Paradox ◽  
Multifunctional Protein ◽  
Group A ◽  
Time Required ◽  
Sequential Induction

Urea amidolyase catalyzes the two reactions (urea carboxylase and a allophanate hydrolase) associated with urea degradation in Saccharomyces cerevisiae. Past work has shown that both reactions are catalyzed by a 204-kilodalton, multifunctional protein. In view of these observations, it was surprising to find that on induction at 22 degrees C, approximately 2 to 6 min elapsed between the appearance of allophanate hydrolase and urea carboxylase activities. In search of an explanation for this apparent paradox, we determined whether or not a detectable period of time elapsed between the appearance of allophanate hydrolase activity and activation of the urea carboxylase domain by the addition of biotin. We found that a significant portion of the protein produced immediately after the onset of induction lacked the prosthetic group. A steady-state level of biotin-free enzyme was reached 16 min after induction and persisted indefinitely thereafter. These data are consistent with the suggestion that sequential induction of allophanate hydrolase and urea carboxylase activities results from the time required to covalently bind biotin to the latter domain of the protein.

scholarly journals Cell cycle-dependent expression of thymidylate synthase in Saccharomyces cerevisiae.

1984 ◽  
Vol 4 (12) ◽  
pp. 2858-2864 ◽  
Author(s):  
R K Storms ◽  
R W Ord ◽  
M T Greenwood ◽  
B Mirdamadi ◽  
F K Chu ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Dna Synthesis ◽  
Thymidylate Synthase ◽  
S Phase ◽  
Mrna Levels ◽  
Activity Profile ◽  
S Period ◽  
Cycle Dependent ◽  
Specific Mrna

Synchronous populations of Saccharomyces cerevisiae cells, generated by two independent methods, have been used to show that thymidylate synthase, in contrast to the vast majority of cellular proteins thus far examined, fluctuates periodically during the S. cerevisiae cell cycle. The enzyme, as assayed by two different methods, accumulated during S period and peaked in mid to late S phase, and then its level dropped. These observations suggest that both periodic synthesis and the instability of the enzyme contribute to the activity profile seen during the cell cycle. Accumulation of thymidylate synthase is determined at the level of its transcript, with synthase-specific mRNA levels increasing at least 10-fold to peak near the beginning of S period and then falling dramatically to basal levels after the onset of DNA synthesis. This mRNA peak coincided with the time during the cell cycle when thymidylate synthase levels were increasing maximally and immediately preceded the peak of DNA synthesis, for which the enzyme provides precursor dTMP.

Cell cycle-dependent expression of thymidylate synthase in Saccharomyces cerevisiae

1984 ◽  
Vol 4 (12) ◽  
pp. 2858-2864
Author(s):  
R K Storms ◽  
R W Ord ◽  
M T Greenwood ◽  
B Mirdamadi ◽  
F K Chu ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Dna Synthesis ◽  
Thymidylate Synthase ◽  
S Phase ◽  
Mrna Levels ◽  
Activity Profile ◽  
S Period ◽  
Cycle Dependent ◽  
Specific Mrna

Synchronous populations of Saccharomyces cerevisiae cells, generated by two independent methods, have been used to show that thymidylate synthase, in contrast to the vast majority of cellular proteins thus far examined, fluctuates periodically during the S. cerevisiae cell cycle. The enzyme, as assayed by two different methods, accumulated during S period and peaked in mid to late S phase, and then its level dropped. These observations suggest that both periodic synthesis and the instability of the enzyme contribute to the activity profile seen during the cell cycle. Accumulation of thymidylate synthase is determined at the level of its transcript, with synthase-specific mRNA levels increasing at least 10-fold to peak near the beginning of S period and then falling dramatically to basal levels after the onset of DNA synthesis. This mRNA peak coincided with the time during the cell cycle when thymidylate synthase levels were increasing maximally and immediately preceded the peak of DNA synthesis, for which the enzyme provides precursor dTMP.

scholarly journals The steady-state level and stability of TLS polymerase eta are cell cycle dependent in the yeast S. cerevisiae

DNA Repair ◽  
2015 ◽  
Vol 29 ◽  
pp. 147-153 ◽  
Author(s):  
Michal Plachta ◽  
Agnieszka Halas ◽  
Justyna McIntyre ◽  
Ewa Sledziewska-Gojska
Keyword(s):  
Cell Cycle ◽  
Steady State ◽  
State Level ◽  
Steady State Level ◽  
Polymerase Eta ◽  
Cycle Dependent

Post-translational processing of urea amidolyase in Saccharomyces cerevisiae

1982 ◽  
Vol 2 (7) ◽  
pp. 800-804
Author(s):  
R A Sumrada ◽  
G Chisholm ◽  
T G Cooper
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Steady State ◽  
State Level ◽  
Steady State Level ◽  
Prosthetic Group ◽  
Apparent Paradox ◽  
Multifunctional Protein ◽  
Group A ◽  
Time Required ◽  
Sequential Induction

Urea amidolyase catalyzes the two reactions (urea carboxylase and a allophanate hydrolase) associated with urea degradation in Saccharomyces cerevisiae. Past work has shown that both reactions are catalyzed by a 204-kilodalton, multifunctional protein. In view of these observations, it was surprising to find that on induction at 22 degrees C, approximately 2 to 6 min elapsed between the appearance of allophanate hydrolase and urea carboxylase activities. In search of an explanation for this apparent paradox, we determined whether or not a detectable period of time elapsed between the appearance of allophanate hydrolase activity and activation of the urea carboxylase domain by the addition of biotin. We found that a significant portion of the protein produced immediately after the onset of induction lacked the prosthetic group. A steady-state level of biotin-free enzyme was reached 16 min after induction and persisted indefinitely thereafter. These data are consistent with the suggestion that sequential induction of allophanate hydrolase and urea carboxylase activities results from the time required to covalently bind biotin to the latter domain of the protein.

scholarly journals Transcriptional regulation of osteopontin production in rat osteoblast-like cells by parathyroid hormone.

1989 ◽  
Vol 108 (2) ◽  
pp. 713-718 ◽  
Author(s):  
M Noda ◽  
G A Rodan
Keyword(s):  
Extracellular Matrix ◽  
Steady State ◽  
Parathyroid Hormone ◽  
Matrix Protein ◽  
State Level ◽  
Extracellular Matrix Protein ◽  
Osteosarcoma Cell ◽  
Mrna Levels ◽  
Steady State Level ◽  
Rat Osteoblast

Osteopontin (OP) or bone sialoprotein is a recently characterized extracellular matrix protein which is abundant in bone and is produced by osteoblasts. Parathyroid hormone (PTH) is a potent calcitropic hormone which regulates osteoblastic function including the synthesis of extracellular matrix proteins. This study examines the effect of human PTH (hPTH-[1-34]) on the expression of this novel protein in rat osteoblast-like cells. hPTH(1-34) significantly decreased the amount of OP in culture media of the rat osteoblastic osteosarcoma cell line, ROS 17/2.8, detected by Western immunoblot analysis. hPTH(1-34) also suppressed the steady-state level of OP mRNA two- to threefold with an ED50 of approximately 3 X 10(-10) M. This inhibition was detectable at 24 h, reached its nadir at 48 h, and lasted at least up to 96 h. The hPTH(1-34) effects were mimicked by isobutylmethylxanthine, cholera toxin, 8-bromo-cAMP, forskolin, and isoproterenol. hPTH(1-34) suppressed by two- to threefold the rate of OP gene transcription, estimated by nuclear run-on assays. The suppression of OP mRNA levels by hPTH(1-34) was also seen when basal levels were increased by transforming growth factor type beta, or 1,25-dihydroxyvitamin D3, or were decreased by dexamethasone. A similar decrease in the steady-state level of OP mRNA by hPTH(1-34) was also observed in primary cultures of osteoblast-enriched cells from fetal rat calvaria. These findings indicate that hPTH(1-34) suppresses the production of the novel extracellular matrix protein, OP, in osteoblasts at least in part through transcriptional control.

Factors influencing the accumulation of tetraphenylphosphonium cation in HeLa cells

1984 ◽  
Vol 4 (1) ◽  
pp. 199-202
Author(s):  
R Hiller ◽  
A Schaefer ◽  
R Zibirre ◽  
H R Kaback ◽  
G Koch
Keyword(s):  
Cell Cycle ◽  
Amino Acids ◽  
Steady State ◽  
Hela Cells ◽  
Alkylating Agent ◽  
State Level ◽  
Steady State Level ◽  
Factors Influencing ◽  
Rapid Accumulation ◽  
External K

Exposure of HeLa cells to tetraphenylphosphonium cation (TPP+) results in a rapid accumulation intracellularly, and a steady-state level is reached within 10 min. Accumulation of [3H]TPP+ in HeLa cells is reduced under the following conditions: (i) after preincubation of cells in buffered saline or in medium containing two- to fourfold higher concentrations of amino acids, (ii) exposure to the alkylating agent L-1-tosylamido-2-phenyl-ethylchloromethyl ketone, (iii) ouabain-mediated inhibition of the Na+, K+ ATPase, and (iv) high external K+ concentrations. In contrast, addition of serum increases the uptake of TPP+. In synchronized cells, intracellular levels of TPP+ differ at various stages of cell cycle and are lowest in mitosis.

scholarly journals Factors influencing the accumulation of tetraphenylphosphonium cation in HeLa cells.

1984 ◽  
Vol 4 (1) ◽  
pp. 199-202 ◽  
Author(s):  
R Hiller ◽  
A Schaefer ◽  
R Zibirre ◽  
H R Kaback ◽  
G Koch
Keyword(s):  
Cell Cycle ◽  
Amino Acids ◽  
Steady State ◽  
Hela Cells ◽  
Alkylating Agent ◽  
State Level ◽  
Steady State Level ◽  
Factors Influencing ◽  
Rapid Accumulation ◽  
External K

Exposure of HeLa cells to tetraphenylphosphonium cation (TPP+) results in a rapid accumulation intracellularly, and a steady-state level is reached within 10 min. Accumulation of [3H]TPP+ in HeLa cells is reduced under the following conditions: (i) after preincubation of cells in buffered saline or in medium containing two- to fourfold higher concentrations of amino acids, (ii) exposure to the alkylating agent L-1-tosylamido-2-phenyl-ethylchloromethyl ketone, (iii) ouabain-mediated inhibition of the Na+, K+ ATPase, and (iv) high external K+ concentrations. In contrast, addition of serum increases the uptake of TPP+. In synchronized cells, intracellular levels of TPP+ differ at various stages of cell cycle and are lowest in mitosis.

The effect of all-trans and 9-cis retinoic acid on the steady state level of HPV16 E6/E7 mRNA and cell cycle in cervical carcinoma cells

Life Sciences ◽  
1998 ◽  
Vol 63 (7) ◽  
pp. 565-573 ◽  
Author(s):  
Bhagavathi A. Narayanan ◽  
E.Blair Holladay ◽  
Daniel W. Nixon ◽  
Charles T. Maure
Keyword(s):  
Cell Cycle ◽  
Retinoic Acid ◽  
Steady State ◽  
Cervical Carcinoma ◽  
State Level ◽  
Carcinoma Cells ◽  
Steady State Level ◽  
Hpv16 E6
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