A fission yeast RCC1-related protein is required for the mitosis to interphase transition.

Sazer, Shelley; Nurse, Paul

doi:10.1002/j.1460-2075.1994.tb06298.x

Cited by 127 publications

(102 citation statements)

References 55 publications

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“…When cells are shifted to the restrictive temperature in the S-phase, the RCC1 mutation results in an interruption of DNA replication, PCC, and a premature mitosis (Nishimoto et al, 1978; ing protein, ran or TC4 in mammalian cells, spil in S. pombe, and GSP1 and GSP2 in S. cerevisiae (Bischoff and Ponstingl, 1991;Matsumoto and Beach, 1991;Coutavas et al, 1993;Saitoh and Dasso, 1995;Azuma et al, 1996). Both proteins are required for normal cell cycle regulation (Matsumoto and Beach, 1991;Sazer and Nurse, 1994).…”

Section: Introductionmentioning

confidence: 99%

RCC1 and nuclear organization.

Huang

Mayeda

Krainer

et al. 1997

MBoC

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We have examined the effect of RCC1 function on the nuclear organization of pre-mRNA splicing factors and poly(A)+ RNA in the tsBN2 cells, a RCC1 temperature-sensitive mutant cell line. We have found that at 4-6 h after shifting cells from the permissive temperature (32.5°C) to the restrictive temperature (39.5°C), both small nuclear ribonucleoprotein particles and a general splicing factor SC35 reorganized into 4-10 large round clusters in the nucleus, as compared with the typical speckled distribution seen in cells at the permissive temperature. In situ hybridization to poly(A)+ RNA resulted in a similar pattern. Examination by double labeling demonstrated that the redistribution of splicing factors coincides with that of poly(A)+ RNA. Such changes in the nuclear organization of splicing factors and poly(A)+ RNA were not the result of the temperature shift or of chromatin condensation. Cellular transcription was not significantly altered in these cells and extracts made from both the permissive and restrictive temperature were splicing competent. Electron microscopic examination demonstrated that the large clusters containing both splicing factors and poly(A)+ RNA were fused interchromatin granule clusters. In addition, small electron-dense dot-like structures measuring approximately 80 nm in diameter were also observed, most of which are accumulated in enlarged interchromatin granule clusters in the nucleoplasm of RCC1 -cells. In spite of the significant changes observed in the nucleoplasm, relatively little alteration was observed in nucleolar structure by both light and electron microscopic examination. The above observations suggest that the RCC1 protein directly or indirectly regulates the organization of splicing components and poly(A)+ RNA in the cell nucleus and that RCC1 may play a role in nuclear organization.

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Section: Introductionmentioning

confidence: 99%

RCC1 and nuclear organization.

Huang

Mayeda

Krainer

et al. 1997

MBoC

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“…Many of the original hints come from defects in cell cycle progression associated with mutations in nuclear transport factors (Nishitani et al 1991;Sazer and Nurse 1994;Loeb et al 1995;Gruss et al 2001;Nachury et al 2001). For example, the first evidence for involvement of Ran in the cell cycle was the observation that cultured cells containing a conditional allele of RCC1, the Ran guanine nucleotide exchange factor (RanGEF), prematurely entered mitosis in the presence of unreplicated DNA (Nishitani et al 1991).…”

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confidence: 99%

“…For example, the first evidence for involvement of Ran in the cell cycle was the observation that cultured cells containing a conditional allele of RCC1, the Ran guanine nucleotide exchange factor (RanGEF), prematurely entered mitosis in the presence of unreplicated DNA (Nishitani et al 1991). Furthermore, in a conditional allele of RanGEF in fission yeast cells, the mutant cells progress through one round of DNA replication and mitosis before arresting at the mitosisinterphase transition of the cell cycle due to the failure of chromatin decondensation (Sazer and Nurse 1994). Subsequent studies have revealed that RanGTP regulates the activity of several mitotic proteins primarily by modulating interactions with import factors (Sazer and Dasso 2000;Gruss et al 2001;Nachury et al 2001;Wiese et al 2001;Du et al 2002).…”

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The Classical Nuclear Localization Signal Receptor, Importin-α, Is Required for Efficient Transition Through the G1/S Stage of the Cell Cycle inSaccharomyces cerevisiae

et al. 2009

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There is significant evidence linking nucleocytoplasmic transport to cell cycle control. The budding yeast, Saccharomyces cerevisiae, serves as an ideal model system for studying transport events critical to cell cycle progression because the nuclear envelope remains intact throughout the cell cycle. Previous studies linked the classical nuclear localization signal (cNLS) receptor, importin-a/Srp1, to the G 2 /M transition of the cell cycle. Here, we utilize two engineered mutants of importin-a/Srp1 with specific molecular defects to explore how protein import affects cell cycle progression. One mutant, Srp1-E402Q, is defective in binding to cNLS cargoes that contain two clusters of basic residues termed a bipartite cNLS. The other mutant, Srp1-55, has defects in release of cNLS cargoes into the nucleus. Consistent with distinct in vivo functional consequences for each of the Srp1 mutants analyzed, we find that overexpression of different nuclear transport factors can suppress the temperature-sensitive growth defects of each mutant. Studies aimed at understanding how each of these mutants affects cell cycle progression reveal a profound defect at the G 1 to S phase transition in both srp1-E402Q and srp1-55 mutants as well as a modest G 1 /S defect in the temperature-sensitive srp1-31 mutant, which was previously implicated in G 2 /M. We take advantage of the characterized defects in the srp1-E402Q and srp1-55 mutants to predict candidate cargo proteins likely to be affected in these mutants and provide evidence that three of these cargoes, Cdc45, Yox1, and Mcm10, are not efficiently localized to the nucleus in importin-a mutants. These results reveal that the classical nuclear protein import pathway makes important contributions to the G 1 /S cell cycle transition.

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“…When the Ran GTPase is misregulated, S. pombe cells arrest after mitosis with hypercondensed, unreplicated chromosomes, fragmented nuclear envelopes, and a wide medial septum (Sazer and Nurse 1994;Demeter et al 1995;Matynia et al 1996). A nucleocytoplasmictransport-independent role for Ran in regulating microtubule structure has also been established (Fleig et al 2000;Salus et al 2002).…”

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confidence: 99%

The Fission Yeast Schizosaccharomyces pombe Has Two Importin-α Proteins, Imp1p and Cut15p, Which Have Common and Unique Functions in Nucleocytoplasmic Transport and Cell Cycle Progression

et al. 2005

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The nuclear import of classical nuclear localization signal-containing proteins depends on importin-a transport receptors. In budding yeast there is a single importin-a gene and in higher eukaryotes there are multiple importin-a-like genes, but in fission yeast there are two: the previously characterized cut15 and the more recently identified imp1. Like other importin-a family members, Imp1p supports nuclear protein import in vitro. In contrast to cut15, imp1 is not essential for viability, but imp1D mutant cells exhibit a telophase delay and mild temperature-sensitive lethality. Differences in the cellular functions that depend on Imp1p and Cut15p indicate that they each have unique physiological roles. They also have common roles because the imp1D and the cut15-85 temperature-sensitive mutations are synthetically lethal; overexpression of cut15 partially suppresses the temperature sensitivity, but not the mitotic delay in imp1D cells; and overexpression of imp1 partially suppresses the mitotic defect in cut15-85 cells but not the loss of viability. Both Imp1p and Cut15p are required for the efficient nuclear import of both an SV40 nuclear localization signal-containing reporter protein and the Pap1p component of the stress response MAP kinase pathway. Imp1p and Cut15p are essential for efficient nuclear protein import in S. pombe.

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A fission yeast RCC1-related protein is required for the mitosis to interphase transition.

Cited by 127 publications

References 55 publications

RCC1 and nuclear organization.

RCC1 and nuclear organization.

The Classical Nuclear Localization Signal Receptor, Importin-α, Is Required for Efficient Transition Through the G1/S Stage of the Cell Cycle inSaccharomyces cerevisiae

The Fission Yeast Schizosaccharomyces pombe Has Two Importin-α Proteins, Imp1p and Cut15p, Which Have Common and Unique Functions in Nucleocytoplasmic Transport and Cell Cycle Progression

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