Research note: Identification of a cDNA homologous to the cell-cycle-controlling cdc2 gene in Acrosiphonia duriuscula (Acrosiphoniales, Chlorophyta)

2001 ◽  
Vol 49 (3) ◽  
pp. 201-205
Author(s):  
Atsushi Kato ◽  
Hirofumi Aruga ◽  
Taizo Motomura
Keyword(s):  
1983 ◽  
Vol 3 (9) ◽  
pp. 1665-1669 ◽  
Author(s):  
M N Conrad ◽  
C S Newlon

DNA isolated from Saccharomyces cerevisiae strains carrying temperature-sensitive mutations in the CDC2 gene after incubation at the restrictive temperature contains multiple stably denatured regions 200 to 700 base pairs long. These regions are probably stabilized by a DNA-binding protein. They are found in both replicated and unreplicated portions of DNA molecules, suggesting that they are not an early stage in the initiation of DNA replication.


1992 ◽  
Vol 12 (5) ◽  
pp. 2295-2301
Author(s):  
U N Fleig ◽  
K L Gould ◽  
P Nurse

The cdc2 gene product, a 34-kDa phosphoprotein with serine/threonine protein kinase activity, has been implicated as the key component in the regulation of the eucaryotic cell cycle. Activation of the cdc2 protein kinase is regulated by its phosphorylation state and by interaction with other proteins. We have mutagenized the fission yeast cdc2 gene to obtain conditionally dominant negative alleles. One of these mutants, named DL2, is characterized in this report. Overexpression of the mutant protein in a wild-type cdc2 background is lethal and leads to arrest in the G2 phase of the cell cycle. The mutant phenotype is the result of a single amino acid change in the GDSEID motif of the protein, a region of identity in all cdc2 homologs, and results in a nonfunctional protein that shows an altered content of phosphothreonine. Multicopy suppressors of the dominant negative phenotype have been isolated, and one of these has been shown to encode the cdc13 cyclin B gene product.


1992 ◽  
Vol 20 (6) ◽  
pp. 1121-1130 ◽  
Author(s):  
Catherine Bergounioux ◽  
Claudette Perennes ◽  
Adriana S. Hemerly ◽  
Li Xian Qin ◽  
Claudine Sarda ◽  
...  

1993 ◽  
Vol 20 (5) ◽  
pp. 503 ◽  
Author(s):  
PCL John ◽  
K Zhang ◽  
C Dong ◽  
L Diederich ◽  
F Wightman

Progress through the plant cell cycle involves changes of phosphorylation state and catalytic activity in p34cdc2 -like protein. The plant protein has protein kinase activity, binds p13suc1, copurifies with cyclin B-like protein and its catalytic activation at mitosis is shown, by a metaphase arresting mutant, to be tightly coupled to cyclin accumulation and breakdown. These properties correlate with findings in other laboratories that some plant cdc2 genes can complement the yeast cdc2 gene. Activation of p34cdc2 at mitosis is proposed to trigger preprophase band breakdown since these two events continue in cells inhibited with okadaic acid although completion of chromosome condensation and spindle formation, which normally precede breakdown, do not occur and are therefore not triggers. In plant development the level of this key division protein relative to other proteins declines in cells entering division to less than one-tenth of that in dividing cells and resumption of division follows restoration of the level in all tissues that have been tested, including cotyledon, stem pith and root. Hormonal induction of division revealed tissue-specific differences in effects of individual hormones on p34cdc2-like protein accumulation and its catalytic activation. In tobacco pith, auxin could induce synthesis of p34cdc2-like protein but cytokinin was necessary for its activation and for cell cycle activity. Within the cell cycle, hormone-dependent control points were identified at late G1 and at mitotic initiation by measurement of nuclear DNA content and the timing of activation of p34cdc2 and cell division, in Nicotiana suspension culture cells restimulated with hormone. Auxin was required at both control points, but cytokinin was required only at mitotic initiation. A direct effect of auxin on cdc2 gene expression is indicated by an increase of cdc2 mRNA levels within 10 min of exposing root tissue to 3-indolylacetic acid (IAA).


1992 ◽  
Vol 12 (5) ◽  
pp. 2295-2301 ◽  
Author(s):  
U N Fleig ◽  
K L Gould ◽  
P Nurse

The cdc2 gene product, a 34-kDa phosphoprotein with serine/threonine protein kinase activity, has been implicated as the key component in the regulation of the eucaryotic cell cycle. Activation of the cdc2 protein kinase is regulated by its phosphorylation state and by interaction with other proteins. We have mutagenized the fission yeast cdc2 gene to obtain conditionally dominant negative alleles. One of these mutants, named DL2, is characterized in this report. Overexpression of the mutant protein in a wild-type cdc2 background is lethal and leads to arrest in the G2 phase of the cell cycle. The mutant phenotype is the result of a single amino acid change in the GDSEID motif of the protein, a region of identity in all cdc2 homologs, and results in a nonfunctional protein that shows an altered content of phosphothreonine. Multicopy suppressors of the dominant negative phenotype have been isolated, and one of these has been shown to encode the cdc13 cyclin B gene product.


1983 ◽  
Vol 3 (9) ◽  
pp. 1665-1669
Author(s):  
M N Conrad ◽  
C S Newlon

DNA isolated from Saccharomyces cerevisiae strains carrying temperature-sensitive mutations in the CDC2 gene after incubation at the restrictive temperature contains multiple stably denatured regions 200 to 700 base pairs long. These regions are probably stabilized by a DNA-binding protein. They are found in both replicated and unreplicated portions of DNA molecules, suggesting that they are not an early stage in the initiation of DNA replication.


Gene ◽  
1991 ◽  
Vol 105 (2) ◽  
pp. 159-165 ◽  
Author(s):  
Hirayama Takashi ◽  
Imajuku Yoshiro ◽  
Anai Toyoaki ◽  
Matsui Minami ◽  
Oka Atsuhiro

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