An essential G1 function for cyclin-like proteins in yeast

Richardson, Helena E.; Wittenberg, Curt; Cross, Frederick R.; Reed, Steven I.

doi:10.1016/0092-8674(89)90768-x

Cited by 559 publications

(365 citation statements)

References 27 publications

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“…All stains are derivatives of BF264-15 15DU: MATa ura3⌬ns ade1 his2 leu2-3112 trp1-1 a (Richardson et al, 1989). Strains were grown at 30°C except for temperature-sensitive mutants that were grown at 24°C in overnight cultures and at the nonpermissive temperatures during time-course experiments.…”

Section: Yeast Strainsmentioning

confidence: 99%

In Vivo Analysis of Chromosome Condensation inSaccharomyces cerevisiae

Vas

Andrews

Matesky

et al. 2007

MBoC

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Although chromosome condensation in the yeast Saccharomyces cerevisiae has been widely studied, visualization of this process in vivo has not been achieved. Using Lac operator sequences integrated at two loci on the right arm of chromosome IV and a Lac repressor-GFP fusion protein, we were able to visualize linear condensation of this chromosome arm during G2/M phase. As previously determined in fixed cells, condensation in yeast required the condensin complex. Not seen after fixation of cells, we found that topoisomerase II is required for linear condensation. Further analysis of perturbed mitoses unexpectedly revealed that condensation is a transient state that occurs before anaphase in budding yeast. Blocking anaphase progression by activation of the spindle assembly checkpoint caused a loss of condensation that was dependent on Mad2, followed by a delayed loss of cohesion between sister chromatids. Release of cells from spindle checkpoint arrest resulted in recondensation before anaphase onset. The loss of condensation in preanaphase-arrested cells was abrogated by overproduction of the aurora B kinase, Ipl1, whereas in ipl1-321 mutant cells condensation was prematurely lost in anaphase/telophase. In vivo analysis of chromosome condensation has therefore revealed unsuspected relationships between higher order chromatin structure and cell cycle control. INTRODUCTIONAccurate chromosome segregation during mitosis is facilitated by the resolution of chromosomes into compact structures. From the level of the nucleosome, chromatin undergoes several changes in organization (Earnshaw, 1988;Filipski et al., 1990). A scaffold of proteins form an axis along which solenoidal chromatin loops are folded into rosettes, which then coalesce to form a sausage-shaped chromonema Marsden and Laemmli, 1979; Johnson, 1979, 1980;Earnshaw and Laemmli, 1983;Earnshaw, 1988). The metaphase chromosome consists of a folded or coiled chromonema (Manton, 1950). In a more recent model of chromosome organization, chromatin is folded into fibers around the central axis, which acts as a "glue" (Kireeva et al., 2004). In both of these models, the protein scaffold is proposed to condense linearly during mitosis.The mitotic scaffold was first observed in histone-depleted mammalian chromosomes and components of this protein scaffold have been of considerable interest (Adolphs et al., 1977;Paulson and Laemmli, 1977). In higher eukaryotes, the process of condensing chromosomes before anaphase requires a protein scaffold comprised of at least condensin and topoisomerase II (Earnshaw et al., 1985;Gasser et al., 1986;Adachi et al., 1991;Saitoh et al., 1994;Gimenez-Abian et al., 1995;Hirano et al., 1997;Maeshima and Laemmli, 2003). Condensin is a five-subunit complex that was first identified in Xenopus egg extracts (Hirano, 2005). Homologues of mitotic scaffold proteins are present in all eukaryotes (reviewed in Hirano, 2005). In the budding yeast Saccharomyces cerevisiae, homologues of the condensin complex, encoded by SMC2, SMC4, YCG1, YCS4, and BRN...

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Section: Yeast Strainsmentioning

confidence: 99%

In Vivo Analysis of Chromosome Condensation inSaccharomyces cerevisiae

Vas

Andrews

Matesky

et al. 2007

MBoC

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“…Passage through START requires the activation of the Cdc28 gene [77]. Activation of Cdc28 for the START transition requires its association with the positive regulatory subunits, the GI cyclius or Clns [78]. Cdc28 is also required for progression through the S phase and the G2/M transition, but this involves association with another class of cyclins, Clbs [79-811.…”

Section: Lessons From Yeast Cellsmentioning

confidence: 99%

Linking Protein Kinase C to Cell‐Cycle Control

Livneh

Fishman

1997

European Journal of Biochemistry

199

114

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Protein kinase C (PKC) isoenzymes are involved in diverse cellular functions, including differentiation, growth control, tumor promotion, and cell death. In recent years, evidence has began to emerge suggesting a role for PKC in cell cycle control. A paper published recently, demonstrating a functional link between PKC and cell cycle control in yeast (Marini, N. J., Meldrum, E., Buehrer, B., Hubberstey, A. V., Stone, D. E., Traynor-Kaplan, A. & Reed, S. I. (1996) EMBO J. 15, 3040-3052), strengthens this data. Thus, the existence of cell-cycle-regulated pathways involving PKC in both yeast and mammals indicate that PKC may be a conserved regulator of cell cycle events that links signal transduction pathways and the cell-cycle machinery. In this paper, we will review current data on the cell cycle components that are targets for PKC regulation.PKC enzymes appear to operate as regulators of the cell cycle at two sites, during G1 progression and G 2 M transition. In G1, the overall effect of PKC activation is inhibition of the cell cycle at mid to late G1. This cell cycle inhibition correlates with a blockage in the normal phosphorylation of the tumor suppressor retinoblastoma Rb protein, presumably through an indirect mechanism. The reduced activity of the cyclin-dependent kinase, Cdk2, appears to be the major effect of PKC activation in various cell systems. This may also underlie the inhibition of Rb phosphorylation exhibited by PKC activation. Several mechanisms were described in different studieq on the regulation of Cdk2 activity by PKC; reduced Cdk-activating kinase activity, diminished expression of the Cdk2 partners cyclins E or A, and the increased expression of the cyclin-dependent inhibitors, p2lWAF1 and p27K'P', which are capable of binding to cyclidCdk2 complexes.PKC enzymes were also shown to play a role in G2/M transition. Among the suggested mechanisms is suppression of Cdc2 activity. However, most of the published data strongly implicate PKC in lamin B phosphorylation and nuclear envelope disassembly.Keywords: protein kinase C ; cell cycle; cyclin ; cyclin-dependent kinase; Cdk inhibitor; retinoblastoma protein; p53 protein; phorbol ester; GUS transition; G2/M transition. Protein kinase C and growth regulationThe term protein kinase C (PKC) stands for a group of at least ten serinehhreonine kinases that are characterized by a high degree of similarity in their catalytic kinase domains and cysteine-rich regions [l-41. The PKC family is subdivided into three groups; the classical PKC members (a, p, y) are Ca2+ and diacylglycerol-dependent, the novel PKCs (6, E , q and d) are Ca2+-independent but diacylglycerol-dependent and the atypical PKCs ([ and 2) are not activated by Ca*+ and diacylglycerol in vitro [3, 41. This may account for the multiplicity and diversity of the cellular activities implicated to be mediated by PKC, sinceCorrespondence to

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“…Cells which have passed a point called START in G 1 are committed to undergo a new cell cycle and cannot respond to mating pheromone until they reach G 1 again (9,10). Transition through START is mediated by the function of the G 1 cyclins Cln1, Cln2, and Cln3, which are the regulatory subunits of the Cdc28 kinase (11)(12)(13)(14)(15). In response to mating pheromone the activity of the Cdc28-Cln kinase gets inhibited, so that the cell cannot pass START (16).…”

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confidence: 99%

Overexpression of the G1-cyclin Gene CLN2Represses the Mating Pathway in Saccharomyces cerevisiaeat the Level of the MEKK Ste11

Wassmann¹,

Ammerer

1997

Journal of Biological Chemistry

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Basal and induced transcription of pheromonedependent genes is regulated in a cell cycle-dependent way. FUS1, a gene strongly induced after pheromone treatment, shows high mRNA levels in mitosis and early G 1 phase of the cell cycle, a decrease in G 1 after START and again an increase in S phase. Overexpression of CLN2 was shown to repress the transcript number of pheromone-dependent genes (1). We asked whether the activities of components of the mating pathway fluctuate during the cell cycle. We were also interested in determining at what level Cln2 represses the signal transduction machinery. Here we show that the activity of the mitogen-activated protein kinase Fus3 indeed fluctuates during the cell cycle, reflecting the oscillations of the gene transcripts. CLN2 overexpression represses Fus3 kinase activity, independently of the phosphatase Msg5. Additionally, we show that the activity of the MEK Ste7 also fluctuates during the cell cycle. Increased Cln2 levels repress the ability of hyperactive STE11 alleles to induce the pathway. G protein-independent activation of Ste11 caused by an rga1 pbs2 mutation is resistant to high levels of Cln2 kinase. Therefore our results suggest that Cln2-dependent repression of the mating pathway occurs at the level of Ste11.

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An essential G1 function for cyclin-like proteins in yeast

Cited by 559 publications

References 27 publications

In Vivo Analysis of Chromosome Condensation inSaccharomyces cerevisiae

In Vivo Analysis of Chromosome Condensation inSaccharomyces cerevisiae

Linking Protein Kinase C to Cell‐Cycle Control

Overexpression of the G1-cyclin Gene CLN2Represses the Mating Pathway in Saccharomyces cerevisiaeat the Level of the MEKK Ste11

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