scholarly journals 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.

1992 ◽  
Vol 3 (3) ◽  
pp. 263-273 ◽  
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.

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

1991 ◽  
Vol 11 (12) ◽  
pp. 5839-5847 ◽  
Author(s):  
N Kinoshita ◽  
M Goebl ◽  
M Yanagida
Keyword(s):  
Fission Yeast ◽  
Gene Product ◽  
Protein Phosphatase ◽  
Cellular Localization ◽  
Gene Dosage ◽  
Regulatory Subunit ◽  
Nucleotide Sequencing ◽  
Permissive Temperature ◽  
Coding Region

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.

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

1991 ◽  
Vol 11 (12) ◽  
pp. 5839-5847
Author(s):  
N Kinoshita ◽  
M Goebl ◽  
M Yanagida
Keyword(s):  
Fission Yeast ◽  
Gene Product ◽  
Protein Phosphatase ◽  
Cellular Localization ◽  
Gene Dosage ◽  
Regulatory Subunit ◽  
Nucleotide Sequencing ◽  
Permissive Temperature ◽  
Coding Region

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.

Lamin B receptor: role on chromatin structure, cellular senescence and possibly aging

2020 ◽  
Vol 477 (14) ◽  
pp. 2715-2720
Author(s):  
Susana Castro-Obregón
Keyword(s):  
Cellular Senescence ◽  
Nuclear Membrane ◽  
Chromatin Structure ◽  
Cholesterol Synthesis ◽  
Reductase Activity ◽  
Chimeric Protein ◽  
Nuclear Lamina ◽  
Lamin B ◽  
Inner Nuclear Membrane ◽  
Lamin B Receptor

The nuclear envelope is composed by an outer nuclear membrane and an inner nuclear membrane, which is underlain by the nuclear lamina that provides the nucleus with mechanical strength for maintaining structure and regulates chromatin organization for modulating gene expression and silencing. A layer of heterochromatin is beneath the nuclear lamina, attached by inner nuclear membrane integral proteins such as Lamin B receptor (LBR). LBR is a chimeric protein, having also a sterol reductase activity with which it contributes to cholesterol synthesis. Lukasova et al. showed that when DNA is damaged by ɣ-radiation in cancer cells, LBR is lost causing chromatin structure changes and promoting cellular senescence. Cellular senescence is characterized by terminal cell cycle arrest and the expression and secretion of various growth factors, cytokines, metalloproteinases, etc., collectively known as senescence-associated secretory phenotype (SASP) that cause chronic inflammation and tumor progression when they persist in the tissue. Therefore, it is fundamental to understand the molecular basis for senescence establishment, maintenance and the regulation of SASP. The work of Lukasova et al. contributed to our understanding of cellular senescence establishment and provided the basis that lead to the further discovery that chromatin changes caused by LBR reduction induce an up-regulated expression of SASP factors. LBR dysfunction has relevance in several diseases and possibly in physiological aging. The potential bifunctional role of LBR on cellular senescence establishment, namely its role in chromatin structure together with its enzymatic activity contributing to cholesterol synthesis, provide a new target to develop potential anti-aging therapies.

scholarly journals Slm9, a Novel Nuclear Protein Involved in Mitotic Control in Fission Yeast

Genetics ◽  
2000 ◽  
Vol 155 (2) ◽  
pp. 623-631
Author(s):  
Junko Kanoh ◽  
Paul Russell
Keyword(s):  
Cell Cycle ◽  
Fission Yeast ◽  
Cell Elongation ◽  
Nuclear Protein ◽  
G1 Arrest ◽  
Permissive Temperature ◽  
Cdc2 Kinase ◽  
Synthetic Lethal ◽  
Cycle Arrest ◽  
Novel Protein

Abstract In the fission yeast Schizosaccharomyces pombe, as in other eukaryotic cells, Cdc2/cyclin B complex is the key regulator of mitosis. Perhaps the most important regulation of Cdc2 is the inhibitory phosphorylation of tyrosine-15 that is catalyzed by Wee1 and Mik1. Cdc25 and Pyp3 phosphatases dephosphorylate tyrosine-15 and activate Cdc2. To isolate novel activators of Cdc2 kinase, we screened synthetic lethal mutants in a cdc25-22 background at the permissive temperature (25°). One of the genes, slm9, encodes a novel protein of 807 amino acids. Slm9 is most similar to Hir2, the histone gene regulator in budding yeast. Slm9 protein level is constant and Slm9 is localized to the nucleus throughout the cell cycle. The slm9 disruptant is delayed at the G2-M transition as indicated by cell elongation and analysis of DNA content. Inactivation of Wee1 fully suppressed the cell elongation phenotype caused by the slm9 mutation. The slm9 mutant is defective in recovery from G1 arrest after nitrogen starvation. The slm9 mutant is also UV sensitive, showing a defect in recovery from the cell cycle arrest after UV irradiation.

scholarly journals Autosomal Recessive HEM/Greenberg Skeletal Dysplasia Is Caused by 3β-Hydroxysterol Δ14-Reductase Deficiency Due to Mutations in the Lamin B Receptor Gene

2003 ◽  
Vol 72 (4) ◽  
pp. 1013-1017 ◽  
Author(s):  
Hans R. Waterham ◽  
Janet Koster ◽  
Petra Mooyer ◽  
Gerard van Noort ◽  
Richard I. Kelley ◽  
...  
Keyword(s):  
Skeletal Dysplasia ◽  
Autosomal Recessive ◽  
Receptor Gene ◽  
Lamin B ◽  
Reductase Deficiency ◽  
Lamin B Receptor

Alterations of nuclear envelope and chromatin organization in mandibuloacral dysplasia, a rare form of laminopathy

2005 ◽  
Vol 23 (2) ◽  
pp. 150-158 ◽  
Author(s):  
Ilaria Filesi ◽  
Francesca Gullotta ◽  
Giovanna Lattanzi ◽  
Maria Rosaria D'Apice ◽  
Cristina Capanni ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Protein A ◽  
Nuclear Architecture ◽  
Mendelian Inheritance ◽  
Premature Aging ◽  
Lamin A ◽  
Lamin B ◽  
Lamin B Receptor ◽  
Epigenetic Events ◽  
Mandibuloacral Dysplasia

Autosomal recessive mandibuloacral dysplasia [mandibuloacral dysplasia type A (MADA); Online Mendelian Inheritance in Man (OMIM) no. 248370 ] is caused by a mutation in LMNA encoding lamin A/C. Here we show that this mutation causes accumulation of the lamin A precursor protein, a marked alteration of the nuclear architecture and, hence, chromatin disorganization. Heterochromatin domains are altered or completely lost in MADA nuclei, consistent with the finding that heterochromatin-associated protein HP1β and histone H3 methylated at lysine 9 and their nuclear envelope partner protein lamin B receptor (LBR) are delocalized and solubilized. Both accumulation of lamin A precursor and chromatin defects become more severe in older patients. These results strongly suggest that altered chromatin remodeling is a key event in the cascade of epigenetic events causing MADA and could be related to the premature-aging phenotype.

Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger–Huët anomaly)

10.1038/ng925 ◽  
2002 ◽  
Vol 31 (4) ◽  
pp. 410-414 ◽  
Author(s):  
Katrin Hoffmann ◽  
Christine K. Dreger ◽  
Ada L. Olins ◽  
Donald E. Olins ◽  
Leonard D. Shultz ◽  
...  
Keyword(s):  
Nuclear Morphology ◽  
Gene Encoding ◽  
Lamin B ◽  
Lamin B Receptor

Accumulation of glycated proteins suggesting premature ageing in lamin B receptor deficient mice

2017 ◽  
Vol 19 (1) ◽  
pp. 95-100 ◽  
Author(s):  
Frank Hause ◽  
Dietmar Schlote ◽  
Andreas Simm ◽  
Katrin Hoffmann ◽  
Alexander Navarrete Santos
Keyword(s):  
Lamin B ◽  
Premature Ageing ◽  
Lamin B Receptor ◽  
Glycated Proteins ◽  
Deficient Mice

Lamin B receptor-related disorder is associated with a spectrum of skeletal dysplasia phenotypes

Bone ◽  
2019 ◽  
Vol 120 ◽  
pp. 354-363 ◽  
Author(s):  
Eliza Thompson ◽  
Ebtesam Abdalla ◽  
Andrea Superti-Furga ◽  
William McAlister ◽  
Lisa Kratz ◽  
...  
Keyword(s):  
Skeletal Dysplasia ◽  
Related Disorder ◽  
Lamin B ◽  
Lamin B Receptor

scholarly journals GREENBERG'S DYSPLASIA- A RARE GENETIC CONDITION

2020 ◽  
pp. 16-17
Author(s):  
Sundari S ◽  
Javeri Aarti Harish
Keyword(s):  
Skeletal Dysplasia ◽  
Autosomal Recessive ◽  
Ectopic Calcification ◽  
Genetic Condition ◽  
Lamin B ◽  
Lamin B Receptor

Greenberg’s Dysplasia, also known as Hydrops-Ectopic calcification-Moth-Eaten (HEM) Skeletal Dysplasia, is a rare autosomal recessive osteochondrodysplasia, caused by mutation in the Lamin B Receptor (LBR) Gene, on chromosome 1q42.

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