CSE1 and CSE2, two new genes required for accurate mitotic chromosome segregation in Saccharomyces cerevisiae.

Xiao, Zhi‐Xiong Jim; McGrew, Jeffrey T.; Schroeder, Andrew J.; Fitzgerald-Hayes, Molly

doi:10.1128/mcb.13.8.4691

Cited by 123 publications

(127 citation statements)

References 62 publications

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“…Mcklp is a dosage suppressor of weak CDE III mutations [30] and Cbf3a mutations [20]. In addition, Mcklp can phosphorylate Cbf3a in vitro [20]. However, the phosphorylation observed in vitro is unlikely to reflect CBF3 activation because already active CBF3 was used as a source for Cbf3a in this experiment.…”

Section: Regulation Of Kinetochore Activitymentioning

confidence: 88%

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The Saccharomyces cerevisiae kinetochore

Lechner¹,

Ortiz²

1996

FEBS Letters

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Accurate chromosome segregation is dependent on a specialized chromosomal structure, the kinetochore/centromere. The only essential constituent of the S. cerevisiae kinetochore established today is CBF3, a multisubunit complex that binds to S. cerevisiae centromere DNA. Therefore CBF3 and its four components, Cbf3a, Cbf3b, Cbf3c and Cbf3d, will form the centerpiece of this review. In addition, we will describe proteins that are putatively involved in kinetochore function specifically in the context with CBF3 interaction. Furthermore, we discuss the role of the S. cerevisiae kinetochores in a putative cell cycle checkpoint control and in microtubule attachment. Key words:Centromere; Kinetochore; CBF3; Saccharomyces cerevisiae Recent reviews that describe the S. cerevisiae kinetochore are available [1,5,6]. This review focuses on the protein components of the S. cerevisiae kinetochore. First we describe proteins that physically interact with the CEN DNA and we emphasize the analysis of CBF3 (_centromere DNA binding factor), a key component of the S. cerevisiae kinetochore. Second we describe proteins that are putatively involved in kinetochore function (as structural components or regulators) as deduced from genetic interactions with CEN DNA or CEN DNA binding proteins. Finally we discuss the role of the S. cerevisiae kinetochore as a putative cell cycle checkpoint and in microtubule interaction. CEN DNA binding proteins

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Section: Regulation Of Kinetochore Activitymentioning

confidence: 88%

“…The protein serine/threonine kinase, Mcklp, may be involved in CBF3 phosphorylation. Mcklp is a dosage suppressor of weak CDE III mutations [30] and Cbf3a mutations [20]. In addition, Mcklp can phosphorylate Cbf3a in vitro [20].…”

Section: Regulation Of Kinetochore Activitymentioning

confidence: 99%

The Saccharomyces cerevisiae kinetochore

Lechner¹,

Ortiz²

1996

FEBS Letters

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“…The localization of GR-GFP was monitored in 14 yeast strains each deficient in a different nuclear transport receptor: CRMI (Stade et al, 1997), CSEI (Xiao et al, 1993), Kap95 (Iovine et al, 1995), Kap104 (Aitchison et al, 1996), Kap123 (Seedorf and Silver, 1997), LOS1 (Hopper et al, 1980), MSN5 (Kaffman et al, 1998a), MTR10 (Kadowaki et al, 1994), NMD5 (He and Jacobson, 1995), PSEI (Seedorf and Silver, 1997), SRP1 (Yano et al, 1992), SXM1 (Seedorf and Silver, 1997), Kap114 (Morehouse et al, 1999;Pemberton et al, 1999), and PDR6 (Titov and Blobel, 1999). Yeast strains PSY580, pse1-1, PSY1200, and PSY902 have been described (Seedorf and Silver, 1997).…”

Section: Yeast Strains Handling Transformations and Localization Smentioning

confidence: 99%

Importin 7 and Importin α/Importin β Are Nuclear Import Receptors for the Glucocorticoid Receptor

Freedman

2004

MBoC

192

151

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The vertebrate glucocorticoid receptor (GR) is cytoplasmic without hormone and localizes to the nucleus after hormone binding. GR has two nuclear localization signals (NLS): NL1 is similar in sequence to the SV40 NLS; NL2 is poorly defined, residing in the ligand-binding domain. We found that GR displayed similar hormone-regulated compartmentalization in Saccharomyces cerevisiae and required the Sxm1 nuclear import receptor for NL2-mediated import. Two metazoan homologues of Sxm1, importin 7 and importin 8, bound both NL1 and NL2, whereas importin ␣ selectively bound NL1. In an in vitro nuclear import assay, both importin 7 and the importin ␣-importin ␤ heterodimer could import a GR NL1 fragment. Under these conditions, full-length GR localized to nuclei in the presence but not absence of an unidentified component in cell extracts. Interestingly, importin 7, importin 8, and importin ␣ bound GR even in the absence of hormone; thus, hormonal control of localization is exerted at a step downstream of import receptor binding. INTRODUCTIONTo survive in a complex environment, cells sense external cues and commonly respond by altering gene expression, in part by regulating the intracellular localization and activity of transcriptional regulatory factors. For example, the intracellular localization of the yeast Pho4 and mammalian SREBP factors is altered in response to changes in external phosphate and circulating sterol concentrations, respectively (Kaffman et al., 1998b;Nagoshi et al., 1999). Similarly, changes in blood glucose levels and a wide range of physiological stress signals modulate the circulating level of glucocorticoids, changing the activity and localization of the glucocorticoid receptor (GR). Within minutes of glucocorticoid binding, GR enters the nucleus and activates or represses target gene transcription (Picard and Yamamoto, 1987). However, hormone binding is reversible; after hormone withdrawal, GR locates back to the cytoplasm (t 1/2 ϭ 10 h; Hache et al., 1999).Proteins and RNAs enter and exit the nucleus through the nuclear pore, a 125-MDa complex in the nuclear envelope (Stoffler et al., 1999). Small molecules readily diffuse through the nuclear pore, whereas molecules greater than ϳ40 kDa require import and export machinery for transport (Davis, 1995;Pante and Aebi, 1995). The first nuclear localization sequence (NLS) was identified in the SV40 large T-antigen (Kalderon et al., 1984). Development of an in vitro nuclear import assay facilitated the identification of two proteins that import substrates containing SV40 NLS-like domains. The adapter molecule importin ␣ binds to the NLS of the substrate and the importin ␤ transport receptor, creating a trimeric complex that imports the substrate into the nucleus through the nuclear pore (Strom and Weis, 2001).Based on similarity to importin ␤, a family of nuclear import and export receptors was identified and shown to transport a wide variety of proteins and RNAs into and out of the nucleus. After reaching the nucleoplasm, import receptors bind the...

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“…The CAS (cellular apoptosis susceptibility) gene was isolated as a result of a genetic screen for cDNAs that would render cancer cells resistant to bacterial toxins and immunotoxins. CAS, which maps to 20q13.2, is the human homolog of the yeast chromosome segregation gene, CSE1 (Xiao et al, 1993). The CSE1 gene product is a microtubule protein involved in chromosome spindle formation; CSE1 mutations lead to a chromosome segregation deficiency phenotype in yeast (Xiao et al, 1993;Scherf et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

“…CAS, which maps to 20q13.2, is the human homolog of the yeast chromosome segregation gene, CSE1 (Xiao et al, 1993). The CSE1 gene product is a microtubule protein involved in chromosome spindle formation; CSE1 mutations lead to a chromosome segregation deficiency phenotype in yeast (Xiao et al, 1993;Scherf et al, 1996). Based on its homology to CSE1, it is reasonable to hypothesize that CAS might play a role in chromosome segregation in human cells.…”

Section: Introductionmentioning

confidence: 99%

20q gain associates with immortalization: 20q13.2 amplification correlates with genome instability in human papillomavirus 16 E7 transformed human uroepithelial cells

et al. 1997

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Breast, bladder, colon, and ovarian carcinomas show frequent low level 20q gain and less frequently high level 20q13.2 ampli®cation, but the signi®cance of these 20q ampli®cations in transformation has not been de®ned. Using karyotypic and comparative genomic hybridization (CGH) analyses, chromosome losses and gains were analysed in six newly immortalized human uroepithelial cell (HUC) lines transformed by Human Papillomavirus 16 (HPV16) E7. Results showed clonal chromosomes with 20q11-4qter gain in all six lines. CGH revealed a peak of 20q13.2 ampli®cation in two cell lines. FISH with whole chromosome 20 paint showed expanded chromosome regions (ECRs) and double minute chromosomes (DMs) that contained chromosome 20 material in cell lines with 20q13.2 ampli®cation. FISH with probes from the center of the 20q13.2 human breast cancer amplicon showed as many as 24 signals in cells with 20q13.2 ampli®cation. The acquisition of genome instability in these E7-HUCs did not correlate with TP53 mutation, as all E7-HUCs contained only wildtype TP53. These results suggest that low level 20q gain is associated with overcoming cellular senescence in E7 transformed cells (P-value=2610 77 ), but does not confer genome instability, while high level 20q13.2 ampli®cation is associated with chromosome instability. Loss of 10p (P-value=3610 75 ) was also important in immortalization of E7-transformed HUCs. Thus, these results have profound implications for interpreting the signi®cance of high versus low level 20q gains in human cancers.

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CSE1 and CSE2, two new genes required for accurate mitotic chromosome segregation in Saccharomyces cerevisiae.

Abstract: (14,18,19,39), CDEIII is essential for function (15,34,40).A protein (CP1, CPF1, or CBF1) that binds to CDEI has been identified (1,7,31). Disruption of the gene encoding this protein causes pleiotropic effects, including a 10-fold increase in mitotic chromosome missegregation (2,8,36

Cited by 123 publications

References 62 publications

The Saccharomyces cerevisiae kinetochore

The Saccharomyces cerevisiae kinetochore

Importin 7 and Importin α/Importin β Are Nuclear Import Receptors for the Glucocorticoid Receptor

20q gain associates with immortalization: 20q13.2 amplification correlates with genome instability in human papillomavirus 16 E7 transformed human uroepithelial cells

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