• Journal of Microbiology
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• 제33권4호
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• pp.350-354
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• 1995

Saccharomyces cervisiae has a highly ordered ring of filaments that lies just inside the cytoplasmic membrane in the region of the mother-bud neck. Mutants defective in any one of the our cell division cycle genes (CDC3, CDC10, CDC11, CDC12) fail to form these filaments and exhibit a pleiotropic phenotype that includes failure to complete cytokinesis and abnormal bud growth. However, the role of the filament is not clear. In order to find out the role of filament, the similar gene in S pombe (called cdc103$\^$+) to the CDC3 was cloned and sequenced. Here I report the sequence analysis of the cdc103$\^$+/ ) to the CDC3 was cloned and sequenced. Here I report the sequence analysis of the cdc103$\^$+/. Comparison of the predicted amino acid sequences of cdc103$\^$+/ and CDC3 revealed that they share significant similarity (43% identity and 56% identity or similarity) to each other.

• 미생물학회지
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• 제31권3호
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• pp.197-202
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• 1993

출아법으로 분열하는 S. cerevisiae 는 mother cell 과 bud cell 과의 연결부위근처의 원형질막 내부에 10-nm filament ring 이 존재한다. CDC3, CDC10, CDC11, CDC12 유전자가 이 filament 를 암호화할 가능성이 많은 것으로 알려져 있으며, 근래에 CDC3 와 CDC12 유전자의 생성물들이 filament ring 에 존재한다는 것이 형광현미경을 이용하여 밝혀졌으나 그 기능은 밝혀지지 않았다. 이에 본인은 10-nm filament ring 의 지능을 알아보기 위하여 ring을 이루고 있는 S. cerevisiae 의 CDC3유전자와 유사한 S. pombe 유전자의 clone 을 시도하였다. 이를 위하여 .lambda. gt11 expression vector 에 S. pombe genomic library 를 만들고 CDC3 항채를 이용하여 screen 하였다. Screen 된 유전자를 sequencing 하여 본 결과, 2개 이상의 intron 이 존재하는 것이 밝혀졌으나, 일부 부위의 아미노산 서열과 CDC3 아미노산 서열을 비교하여 본 결과, 약 62%의 유사성이 존재하였다.

• Molecules and Cells
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• 제40권12호
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• pp.925-934
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• 2017

The Cdc6 protein is essential for the initiation of chromosomal replication and functions as a licensing factor to maintain chromosome integrity. During the S and G2 phases of the cell cycle, Cdc6 has been found to inhibit the recruitment of pericentriolar material (PCM) proteins to the centrosome and to suppress centrosome over-duplication. In this report, we analyzed the correlation between these two functions of Cdc6 at the centrosome. Cdc6 depletion increased the population of cells showing centrosome over-duplication and premature centrosome separation; Cdc6 expression reversed these changes. Deletion and fusion experiments revealed that the 18 amino acid residues (197-214) of Cdc6, which were fused to the Cdc6-centrosomal localization signal, suppressed centrosome over-duplication and premature centrosome separation. Cdc6 mutant proteins that showed defective ATP binding or hydrolysis did not exhibit a significant difference in suppressing centrosome over-duplication, compared to the wild type protein. In contrast to the Cdc6-mediated inhibition of PCM protein recruitment to the centrosome, the independence of Cdc6 on its ATPase activity for suppressing centrosome over-duplication, along with the difference between the Cdc6 protein regions participating in the two functions, suggested that Cdc6 controls centrosome duplication in a manner independent of its recruitment of PCM proteins to the centrosome.

• 미생물학회지
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• 제52권3호
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• pp.383-387
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• 2016

분열효모 Schizosaccharomyces pombe의 cdc31 유전자는 진화적으로 잘 보존된 $Ca^{2+}$-결합 centrin/CDC31 계열에 속하며 방추극체(spindle pole body)의 한 성분인 단백질을 암호화하고 있다. 이 논문에서는 S. pombe의 Cdc31 단백질이 방추극체뿐만 아니라 TREX-2 복합체의 구성인자로서 mRNA의 핵에서 세포질로의 방출에 영향을 미치는지 알아보았다. cdc31 유전자의 발현을 억제하면 생장 결함을 보였고, $poly(A)^+$ RNA도 핵 안에 축적되는 현상을 보였다. 한편 cdc31 유전자를 과발현시키면, 생장과 mRNA 방출에 결함을 보이진 않았지만 세포의 길이가 길어지는 형태를 보였다. Yeast two-hybrid 분석에서 Cdc31 단백질은 TREX-2 복합체의 또 다른 구성인자인 Sac3 그리고 Pci2와 상호작용을 하였다. 이와 같은 결과들은 S. pombe의 Cdc31 단백질도 역시 TREX-2 복합체의 구성인자로 mRNA 방출에 관여하고 있음을 시사한다.

• 미생물학회지
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• 제27권3호
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• pp.210-215
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• 1989

In order to elucidate and characterize the signal transduction pathway(s) whereby yeast cells respond to mating pheromone, we have isolated mutants which are able to conjugate in the absence of the alpha-factor receptor. Sixty-one suppressors of a ste2-deletion mutation which also confer a ts conditional "start" arrest phenotypw have been subjected to genetic analysis. The mutants could be assigned to three complementation groups designated CDC70, CDC72 and CDC73, which are unlinked to each other as well as to the previously identified start genes. Quantitation of mating ability of the cdc70, cdc72 and cdc73 mutations in a ste2-deletion background gives levels ranging from 0.1% to 0.3% of wild type, depending on the allele and the gene. The results indicate that the signals from mating pheromone might be mediated by the CDC70, CDC72 and CDC73 products. products.

• Molecules and Cells
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• 제28권1호
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• pp.57-65
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• 2009

CDC48 is a member of the AAA ATPase superfamily. Yeast CDC48 and its mammalian homolog p97 are implicated in diverse cellular processes, including mitosis, membrane fusion, and ubiquitin-dependent protein degradation. However, the cellular functions of plant CDC48 proteins are largely unknown. In the present study, we performed virus-induced gene silencing (VIGS) screening and found that silencing of a gene encoding a tobacco CDC48 homolog, NgCDC48, resulted in severe abnormalities in leaf and shoot development in tobacco. Furthermore, transgenic tobacco plants (35S:anti-NgCDC48), in which the NgCDC48 gene was suppressed using the antisense RNA method, exhibited severely aberrant development of both vegetative and reproductive organs, resulting in arrested shoot and leaf growth and sterile flowers. Approximately 57-83% of 35S:anti-NgCDC48 plants failed to develop mature organs and died at early stage of development. Scanning electron microscopy showed that both adaxial and abaxial epidermal pavement cells in antisense transgenic leaves were significantly smaller and more numerous than those in wild type leaves. These results indicate that NgCDC48 is critically involved in cell growth and development of tobacco plants. An in vivo targeting experiment revealed that NgCDC48 resides in the endoplasmic reticulum (ER) in tobacco protoplasts. We consider the tantalizing possibility that CDC48-mediated degradation of an as-yet unidentified protein(s) in the ER might be a critical step for cell growth and expansion in tobacco leaves.

• Journal of Microbiology
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• 제34권3호
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• pp.248-254
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• 1996

$cdc103^+$ gene in Schizosaccharomyces pombe which is similar to the CDC3 gene in Saccharomyces cerevisiae was cloned and sequenced. Comparison of the predicted amino acid sequences of $cdc103^+$ and CDC3 revealed that they share significant similarity (43% identity and 56% identity or similarity) to each other. The gene product of CDC3 in S. cerevisiae is known to be a highly ordered ring of filaments that lies just inside the cytoplasmic membrane in the region of the mother-bud neck. In order to characterize the gene product of $cdc103^+$ in Schizosaccharomyces pombe, fusion proteins were used to generate the polyclonal antibodies specific for the gene product (cdc103p). In immunofluorescence experiments, these antibodies decorate the region of the septum formation as a double ring structure late in the cell division cycle.

• Asian Pacific Journal of Cancer Prevention
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• 제13권3호
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• pp.931-935
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• 2012

Cdc25 phosphatases are important regulators of the cell cycle. Their abnormal expression detected in a number of tumors implies that their dysregulation is involved in malignant transformation. However, the role of Cdc25B in renal cell carcinomas remains unknown. To shed light on influence on renal cell carcinogenesis and subsequent progression, Cdc25B expression was examined by real-time RT-PCR and western blotting in renal cell carcinoma and normal tissues. 65 kDa Cdc25B expression was higher in carcinomas than in the adjacent normal tissues (P<0.05), positive correlations being noted with clinical stage and histopathologic grade (P<0.05). To additionally investigate the role of Cdc25B alteration in the development of renal cell carcinoma, Cdc25B siRNA was used to knockdown the expression of Cdc25B. Down-regulation resulted in slower growth, more G2/M cells, weaker capacity for migration and invasion, and induction of apoptosis in 769-P transfectants. Reduction of 14-3-3 protein expression appeared related to Cdc25B knockdown. These findings suggest an important role of Cdc25B in renal cell carcinoma development and provide a rationale for investigation of Cdc2B-based gene therapy.

• 혜화의학회지
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• 제14권1호
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• pp.201-211
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• 2005

Cdc2 kinase is a prototypical cyclin-dependent kinase critical for G2 to M phase cell cycle transition. Yet, its function in the nervous system is largely unknown. Here, we investigated possible role of Cdc2 in axonal regeneration using sciatic nerve system in rat. Cdc2 protein levels and activity were increased in the injured sciatic nerves 3 and 7 days after crush injury and then decreased to basal level 14 days later. Administration of Cdc2 kinase inhibitor roscovitine in vivo at the time of crush injury significantly inhibited axonal regeneration when regrowing axons were analyzed using retrograde tracers. Cdc2 protein levels in cultured Schwann cells which were prepared from sciatic nerves 7 days after crush injury were much higher compared with those from uninjured sciatic nerves, suggesting that Cdc2 protein expression was primarily induced in the Schwann cells. To further investigate Cdc2 function in Schwann cell, we examined changes in cultured Schwann cell proliferation and migration in culture system. Both the number of proliferating Schwann cells and the extent of neurite outgrowth from co-cultured DRG neurons were significantly decreased by Cdc2 inhibitor roscovitine treatment in DRG culture which was prepared from animals with sciatic nerve injury for 7 days. Also, Schwann cell migration in the injured sciatic nerve explant was significantly inhibited by roscovitine treatment. Taken together, the present data suggest that Cdc2 may be involved in peripheral nerve regeneration via Schwann cell proliferation and migration.

• Molecules and Cells
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• 제39권11호
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• pp.834-840
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• 2016

Caenorhabditis elegans (C. elegans) utilizes two different cell-cycle modes, binucleations during the L1 larval stage and endoreduplications at four larval moltings, for its postembryonic intestinal development. Previous genetic studies indicated that CDC-25.2 is specifically required for binucleations at the L1 larval stage and is repressed before endoreduplications. Furthermore, LIN-23, the C. elegans ${\beta}$-TrCP ortholog, appears to function as a repressor of CDC-25.2 to prevent excess intestinal divisions. We previously reported that intestinal hyperplasia in lin-23(e1883) mutants was effectively suppressed by the RNAi depletion of cdc-25.2. Nevertheless, LIN-23 targeting CDC-25.2 for ubiquitination as a component of E3 ubiquitin ligase has not yet been tested. In this study, LIN-23 is shown to be the major E3 ubiquitin ligase component, recognizing CDC-25.2 to repress their activities for proper transition of cell-cycle modes during the C. elegans postembryonic intestinal development. In addition, for the first time that LIN-23 physically interacts with both CDC-25.1 and CDC-25.2 and facilitates ubiquitination for timely regulation of their activities during the intestinal development.