The fission yeast dis3+ gene encodes a 110-kDa essential protein implicated in mitotic control.

The fission yeast mutant dis3-54 is defective in mitosis and fails in chromosome disjunction. Its phenotype is similar to that of dis2-11, a mutant with a mutation in the type 1 protein phosphatase gene. We cloned the dis3+ gene by transformation. Nucleotide sequencing predicts a coding region of 970 amino acids interrupted by a 164-bp intron at the 65th codon. The predicted dis3+ protein shares a weak but significant similarity with the budding yeast SSD1 or SRK1 gene product, the gene for which is a suppressor for the absence of a protein phosphatase SIT4 gene or the BCY1 regulatory subunit of cyclic AMP-dependent protein kinase. Anti-dis3 antibodies recognized the 110-kDa dis3+ gene product, which is part of a 250- to 350-kDa oligomer and is enriched in the nucleus. The cellular localization of the dis3+ protein is reminiscent of that of the dis2+ protein, but these two proteins do not form a complex. A type 1 protein phosphatase activity in the dis3-54 mutant extracts is apparently not affected. The dis3+ gene is essential for growth; gene disruptant cells do not germinate and fail in cell division. Increased dis3+ gene dosage reverses the Ts+ phenotype of a cdc25 wee1 strain, as does increased type 1 protein phosphatase gene dosage. Double mutant dis3 dis2 is lethal even at the permissive temperature, suggesting that the dis2+ and dis3+ genes may be functionally overlapped. The role of the dis3+ gene product in mitosis is unknown, but this gene product may be directly or indirectly involved in the regulation of mitosis.

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Sequence of the human glycogen-associated regulatory subunit of type 1 protein phosphatase and analysis of its coding region and mRNA level in muscle from patients with NIDDM

Diabetes ◽

10.2337/diabetes.43.10.1234 ◽

1994 ◽

Vol 43 (10) ◽

pp. 1234-1241 ◽

Cited By ~ 26

Author(s):

Y. H. Chen ◽

L. Hansen ◽

M. X. Chen ◽

C. Bjorbaek ◽

H. Vestergaard ◽

...

Keyword(s):

Protein Phosphatase ◽

Mrna Level ◽

Regulatory Subunit ◽

Coding Region

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Sequence of the Human Glycogen-Associated Regulatory Subunit of type 1 Protein Phosphatase and Analysis of Its Coding Region and mRNA Level in Muscle From Patients With NIDDM

Diabetes ◽

10.2337/diab.43.10.1234 ◽

1994 ◽

Vol 43 (10) ◽

pp. 1234-1241 ◽

Cited By ~ 11

Author(s):

Y. Hua Chen ◽

L. Hansen ◽

M. Xiang Chen ◽

C. Bjorbaek ◽

H. Vestergaard ◽

...

Keyword(s):

Protein Phosphatase ◽

Mrna Level ◽

Regulatory Subunit ◽

Coding Region

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Fission yeast sts1+ gene encodes a protein similar to the chicken lamin B receptor and is implicated in pleiotropic drug-sensitivity, divalent cation-sensitivity, and osmoregulation.

Molecular Biology of the Cell ◽

10.1091/mbc.3.3.263 ◽

1992 ◽

Vol 3 (3) ◽

pp. 263-273 ◽

Cited By ~ 21

Author(s):

M Shimanuki ◽

M Goebl ◽

M Yanagida ◽

T Toda

Keyword(s):

Fission Yeast ◽

Drug Sensitivity ◽

Genomic Library ◽

Kinase Inhibitor ◽

Divalent Cations ◽

Cold Sensitivity ◽

Nucleotide Sequencing ◽

Permissive Temperature ◽

Lamin B ◽

Lamin B Receptor

The Schizosaccharomyces pombe sts1+ gene, identified by supersensitive mutations to a protein kinase inhibitor, staurosporine, was isolated by complementation by the use of a fission yeast genomic library. Nucleotide sequencing shows that the sts1+ gene encodes a 453 amino acid putative membrane-associated protein that is significantly similar (26% identity) to the chicken lamin B receptor. It is also highly related (53% identity) to a budding yeast ORF, YGL022. These three proteins contain a similar hydrophobicity pattern consisting of eight or nine putative transmembrane domains. By gene disruption we demonstrate that the sts1+ gene is not essential for viability. These disruptants exhibit pleiotropic defects, such as cold-sensitivity for growth and at the permissive temperature, a supersensitivity to divalent cations and several unrelated drugs including staurosporine, caffeine, chloramphenicol, sorbitol, and SDS. Disruption of the sts1+ gene does not lead to a sensitivity to thiabendazole or hydroxyurea.

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Ypi1, a Positive Regulator of Nuclear Protein Phosphatase Type 1 Activity in Saccharomyces cerevisiae

Molecular Biology of the Cell ◽

10.1091/mbc.e07-05-0499 ◽

2008 ◽

Vol 19 (3) ◽

pp. 1032-1045 ◽

Cited By ~ 29

Author(s):

Jennifer P. Bharucha ◽

Jennifer R. Larson ◽

Lu Gao ◽

Lisa K. Daves ◽

Kelly Tatchell

Keyword(s):

Protein Phosphatase ◽

Nuclear Protein ◽

Spindle Checkpoint ◽

Regulatory Subunit ◽

Aurora B ◽

Binding Partner ◽

Protein Phosphatase Type 1 ◽

Positive Regulators ◽

Protein Phosphatase Type

The catalytic subunit of protein phosphatase type 1 (PP1) has an essential role in mitosis, acting in opposition to the Ipl1/Aurora B protein kinase to ensure proper kinetochore-microtubule interactions. However, the regulatory subunit(s) that completes the PP1 holoenzyme that functions in this capacity is not known. We show here that the budding yeast Ypi1 protein is a nuclear protein that functions with PP1 (Glc7) in this mitotic role. Depletion of cellular Ypi1 induces mitotic arrest due to activation of the spindle checkpoint. Ypi1 depletion is accompanied by a reduction of nuclear PP1 and by loss of nuclear Sds22, a Glc7 binding partner that is found in a ternary complex with Ypi1 and Glc7. Expression of a Ypi1 variant that binds weakly to PP1 also activates the spindle checkpoint and suppresses the temperature sensitivity of an ipl1-2 mutant. These results, together with genetic interactions among YPI1, GLC7, and SDS22 mutants, indicate that Ypi1 and Sds22 are positive regulators of the nuclear Glc7 activity that is required for mitosis.

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An N-terminal Arginine-rich Cluster and a Proline-Alanine-Threonine Repeat Region Determine the Cellular Localization of the Herpes Simplex Virus Type 1 ICP34.5 Protein and Its Ligand, Protein Phosphatase 1

Journal of Biological Chemistry ◽

10.1074/jbc.m111553200 ◽

2002 ◽

Vol 277 (13) ◽

pp. 11423-11431 ◽

Cited By ~ 18

Author(s):

Hanwen Mao ◽

Kenneth S. Rosenthal

Keyword(s):

Herpes Simplex Virus ◽

Herpes Simplex ◽

Herpes Simplex Virus Type ◽

Protein Phosphatase ◽

Cellular Localization ◽

Protein Phosphatase 1 ◽

Repeat Region ◽

Rich Cluster ◽

Simplex Virus

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Identification of sds21 in fission yeast in an inhibitor-resistant high molecular mass protein phosphatase-1 complex

Biochemistry and Cell Biology ◽

10.1139/o99-062 ◽

1999 ◽

Vol 77 (6) ◽

pp. 551-558 ◽

Cited By ~ 1

Author(s):

John F Dawson ◽

Charles FB Holmes

Keyword(s):

Protein Kinase ◽

Molecular Mass ◽

Fission Yeast ◽

Phosphatase Activity ◽

Protein Phosphatase ◽

High Molecular Mass ◽

Protein Phosphatase 1 ◽

Dependent Protein Kinase ◽

Dependent Protein

While characterizing the type-1 protein phosphatases sds21 and dis2 in fission yeast (Schizosaccharomyces pombe) a novel high molecular mass protein was identified with serine/threonine phosphatase activity (referred to as PP-R) that was resistant to a panel of characteristic inhibitors of protein phosphatases. Purification of the native sds21 catalytic isoform of protein phosphatase-1 (PP-1) from an S. pombe knockout strain lacking dis2 (Δdis2) resulted predominantly in identification of PP-R. To test the hypothesis that the catalytic activity of PP-R comprised sds21, a parallel purification was performed of PP-1 activity from an S. pombe knockout strain lacking sds21 (Δsds21). Both Δsds21 and Δdis2 strains exhibited similar protein phosphatase activity profiles as determined by DEAE-sepharose, Mono-Q and Superdex gel filtration chromatography. However, the peak of protein phosphatase activity from Δsds21 S. pombe that co-migrated with PP-R from Δdis2 S. pombe exhibited the sensitivity to a panel of inhibitors that was characteristic of a type-1 protein phosphatase. These data suggest that the catalytic subunit of PP-R comprises sds21 and that the resistance to inhibitors may originate from structural differences between dis2 and sds21 isoforms. A key structural feature present in sds21, but lacking in dis2, is a classical phosphorylation consensus sequence surrounding serine-145 of sds21. The previous hypothesis was that PP-1 activity among several lower eukaryotes may be regulated directly by cAMP-dependent protein kinase (PKA) phosphorylation. However, this study demonstrated that recombinant sds21 is not a target for PKA in vitro. The constrained configuration of the putative PKA site on the PP-1 holoenzyme may restrict its ability to be targeted by PKA.Key words: cAMP-dependent protein kinase, protein phosphatase-1, sds21, dis2, G-subunit, microcystin-LR, okadaic acid, S. pombe.

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GAC1 may encode a regulatory subunit for protein phosphatase type 1 in Saccharomyces cerevisiae.

The EMBO Journal ◽

10.1002/j.1460-2075.1992.tb05031.x ◽

1992 ◽

Vol 11 (1) ◽

pp. 87-96 ◽

Cited By ~ 97

Author(s):

J.M. François ◽

S. Thompson-Jaeger ◽

J. Skroch ◽

U. Zellenka ◽

W. Spevak ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Protein Phosphatase ◽

Regulatory Subunit ◽

Protein Phosphatase Type 1 ◽

Protein Phosphatase Type

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Natural Genetic Exchanges between Vaccine and Wild Poliovirus Strains in Humans

Journal of Virology ◽

10.1128/jvi.74.18.8434-8443.2000 ◽

2000 ◽

Vol 74 (18) ◽

pp. 8434-8443 ◽

Cited By ~ 146

Author(s):

Sophie Guillot ◽

Valérie Caro ◽

Nancy Cuervo ◽

Ekaterina Korotkova ◽

Mariana Combiescu ◽

...

Keyword(s):

Paralytic Poliomyelitis ◽

Nucleotide Sequencing ◽

Wild Type ◽

Coding Region ◽

Wild Poliovirus ◽

Type 3 ◽

Recombinant Genome ◽

Natural Means

ABSTRACT In a previous study of poliovirus vaccine-derived strains isolated from patients with vaccine-associated paralytic poliomyelitis (VAPP) (9, 11), we reported that a high proportion (over 50%) of viruses had a recombinant genome. Most were intertypic vaccine/vaccine recombinants. However, some had restriction fragment length polymorphism (RFLP) profiles different from those of poliovirus vaccine strains. We demonstrate here that five such recombinants, of 88 VAPP strains examined, carried sequences of wild (nonvaccine) origin. To identify the parental wild donor of these sequences, we used RFLP profiles and nucleotide sequencing to look for similarity in the 3D polymerase-coding region of 61 wild, cocirculating poliovirus isolates (43 type 1, 16 type 2, and 2 type 3 isolates). In only one case was the donor identified, and it was a wild type 1 poliovirus. For the other four vaccine/wild recombinants, the wild parent could not be identified. The possibility that the wild sequences were of a non-poliovirus-enterovirus origin could not be excluded. Another vaccine/wild recombinant, isolated in Belarus from a VAPP case, indicated that the poliovirus vaccine/wild recombination is not an isolated phenomenon. We also found wild polioviruses (2 of 15) carrying vaccine-derived sequences in the 3′ moiety of their genome. All these results suggest that genetic exchanges with wild poliovirus and perhaps with nonpoliovirus enteroviruses, are also a natural means of evolution for poliovirus vaccine strains.

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