scholarly journals Ubiquitination regulates cytoophidium assembly in Schizosaccharomyces pombe

2021 ◽  
Author(s):  
Christos Andreadis ◽  
Tianhao Li ◽  
Ji-Long Liu
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
De Novo ◽  
Metabolic Enzyme ◽  
Filamentous Structure ◽  
Deubiquitinating Enzymes ◽  
Evolutionarily Conserved ◽  
Ctp Synthase

AbstractCTP synthase (CTPS), a metabolic enzyme responsible for the de novo synthesis of CTP, can form filamentous structures termed cytoophidia, which are evolutionarily conserved from bacteria to humans. Here we used Schizosaccharomyces pombe to study the cytoophidium assembly regulation by ubiquitination. We tested the CTP synthase’s capacity to be epigenetically modified by ubiquitin or be affected by the ubiquitination state of the cell, showed that CTPS is immunoprecipitated with ubiquitin, and that ubiquitination is important for the maintenance of the CTPS filamentous structure in fission yeast. We have identified proteins which are in complex with CTPS, including specific ubiquitination regulators which significantly affect CTPS filamentation, and mapped probable ubiquitination targets on CTPS. Furthermore, we discovered that a cohort of deubiquitinating enzymes is significant for the regulation of cytoophidium morphology. Our study provides a framework for the analysis of the effects that ubiquitination and deubiquitination have on the formation of CTPS filaments.

scholarly journals Alp7-Mto1 and Alp14 synergize to promote interphase microtubule regrowth from the nuclear envelope

2019 ◽  
Vol 11 (11) ◽  
pp. 944-955 ◽  
Author(s):  
Wenyue Liu ◽  
Fan Zheng ◽  
Yucai Wang ◽  
Chuanhai Fu
Keyword(s):  
Nuclear Envelope ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Microtubule Assembly ◽  
Dependent Manner ◽  
Microtubule Nucleation ◽  
Microtubule Organizing Centers ◽  
Evolutionarily Conserved ◽  
Microtubule Growth ◽  
In Cells

Abstract Microtubules grow not only from the centrosome but also from various noncentrosomal microtubule-organizing centers (MTOCs), including the nuclear envelope (NE) and pre-existing microtubules. The evolutionarily conserved proteins Mto1/CDK5RAP2 and Alp14/TOG/XMAP215 have been shown to be involved in promoting microtubule nucleation. However, it has remained elusive as to how the microtubule nucleation promoting factors are specified to various noncentrosomal MTOCs, particularly the NE, and how these proteins coordinate to organize microtubule assembly. Here, we demonstrate that in the fission yeast Schizosaccharomyces pombe, efficient interphase microtubule growth from the NE requires Alp7/TACC, Alp14/TOG/XMAP215, and Mto1/CDK5RAP2. The absence of Alp7, Alp14, or Mto1 compromises microtubule regrowth on the NE in cells undergoing microtubule repolymerization. We further demonstrate that Alp7 and Mto1 interdependently localize to the NE in cells without microtubules and that Alp14 localizes to the NE in an Alp7 and Mto1-dependent manner. Tethering Mto1 to the NE in cells lacking Alp7 partially restores microtubule number and the efficiency of microtubule generation from the NE. Hence, our study delineates that Alp7, Alp14, and Mto1 work in concert to regulate interphase microtubule regrowth on the NE.

scholarly journals Utilization and interconversions of purine derivatives in the fission yeastSchizosaccharomyces pombe

1971 ◽  
Vol 18 (1) ◽  
pp. 33-44 ◽  
Author(s):  
J. Pourquié ◽  
H. Heslot
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
De Novo ◽  
Growth Responses ◽  
Purine Derivatives ◽  
Purine Synthesis ◽  
Purine Bases ◽  
Purine Ring

SUMMARYIn the fission yeastSchizosaccharomyces pombe, growth responses of mutants strains in the de novo purine synthesis pathway, in the purine interconversion system, and of various double mutants, have been studied upon different purine-supplemented media. The results show that exogenous purine utilization as nucleotide source is based exclusively upon pyrophosphorylation of purine bases, and they make it possible to identify most of the enzymic steps acting, in this organism, upon a purine ring to give another purine ring.A scheme of the interconversion system inSchizosaccharomyces pombeis given.

scholarly journals CTP synthase forms cytoophidia in archaea

2019 ◽  
Author(s):  
Shuang Zhou ◽  
Hua Xiang ◽  
Ji-Long Liu
Keyword(s):  
De Novo ◽  
Stimulated Emission ◽  
Metabolic Enzyme ◽  
De Novo Synthesis ◽  
Low Salt ◽  
Ctp Synthase ◽  
Intracellular Compartments ◽  
Domains Of Life ◽  
Haloarcula Hispanica ◽  
Rate Limiting

AbstractCTP synthase (CTPS) is an important metabolic enzyme that catalyzes the rate-limiting reaction of de novo synthesis of the nucleotide CTP. Since 2010, a series of studies have demonstrated that CTPS can form filamentous structures termed cytoophidia in bacteria and eukaryotes. However, it remains unknown whether cytoophidia exist in archaea, the third domain of life. Using Haloarcula hispanica as a model system, here we demonstrate that CTPS forms distinct intracellular compartments in archaeal cells. Under stimulated emission depletion (STED) microscopy, we find that some HhCTPS compartments have elongated filamentous structures, resembling cytoophidia in bacteria and eukaryotes. When Haloarcula cells are cultured in low-salt medium, the occurrence of cytoophidia increases dramatically. Moreover, overexpression of CTPS or glutamine analog treatment promotes cytoophidium assembly in H. hispanica. Our study reveals that CTPS forms cytoophidia in all three domains of life, suggesting that this is an ancient property of CTPS.

scholarly journals De Novo Biosynthesis of Vanillin in Fission Yeast (Schizosaccharomyces pombe) and Baker's Yeast (Saccharomyces cerevisiae)

2009 ◽  
Vol 75 (9) ◽  
pp. 2765-2774 ◽  
Author(s):  
Esben H. Hansen ◽  
Birger Lindberg Møller ◽  
Gertrud R. Kock ◽  
Camilla M. Bünner ◽  
Charlotte Kristensen ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
De Novo ◽  
Global Market ◽  
Baker’S Yeast ◽  
Yeast Cells ◽  
Vanillyl Alcohol ◽  
Baker's Yeast ◽  
Yeast Saccharomyces Cerevisiae

ABSTRACT Vanillin is one of the world's most important flavor compounds, with a global market of 180 million dollars. Natural vanillin is derived from the cured seed pods of the vanilla orchid (Vanilla planifolia), but most of the world's vanillin is synthesized from petrochemicals or wood pulp lignins. We have established a true de novo biosynthetic pathway for vanillin production from glucose in Schizosaccharomyces pombe, also known as fission yeast or African beer yeast, as well as in baker's yeast, Saccharomyces cerevisiae. Productivities were 65 and 45 mg/liter, after introduction of three and four heterologous genes, respectively. The engineered pathways involve incorporation of 3-dehydroshikimate dehydratase from the dung mold Podospora pauciseta, an aromatic carboxylic acid reductase (ACAR) from a bacterium of the Nocardia genus, and an O-methyltransferase from Homo sapiens. In S. cerevisiae, the ACAR enzyme required activation by phosphopantetheinylation, and this was achieved by coexpression of a Corynebacterium glutamicum phosphopantetheinyl transferase. Prevention of reduction of vanillin to vanillyl alcohol was achieved by knockout of the host alcohol dehydrogenase ADH6. In S. pombe, the biosynthesis was further improved by introduction of an Arabidopsis thaliana family 1 UDP-glycosyltransferase, converting vanillin into vanillin β-d-glucoside, which is not toxic to the yeast cells and thus may be accumulated in larger amounts. These de novo pathways represent the first examples of one-cell microbial generation of these valuable compounds from glucose. S. pombe yeast has not previously been metabolically engineered to produce any valuable, industrially scalable, white biotech commodity.

scholarly journals Hap2-Ino80 facilitated transcription promotes de novo establishment of CENP-A chromatin

2019 ◽  
Author(s):  
Puneet P. Singh ◽  
Manu Shukla ◽  
Sharon A. White ◽  
Pin Tong ◽  
Tatsiana Auchynnikava ◽  
...  
Keyword(s):  
Fission Yeast ◽  
De Novo ◽  
Histone H3 ◽  
Chromatin Assembly ◽  
Centromere Function ◽  
Kinetochore Assembly ◽  
Auxiliary Subunit ◽  
Evolutionarily Conserved ◽  
Histone H3 Variant ◽  
Chromatin Integrity

SUMMARYCentromeres are maintained epigenetically by the presence of CENP-A, an evolutionarily-conserved histone H3 variant, which directs kinetochore assembly and hence, centromere function. To identify factors that promote assembly of CENP-A chromatin, we affinity selected solubilised fission yeast CENP-ACnp1 chromatin. All subunits of the Ino80 complex were enriched, including the auxiliary subunit Hap2. In addition to a role in maintenance of CENP-ACnp1 chromatin integrity at endogenous centromeres, Hap2 is required for de novo assembly of CENP-ACnp1 chromatin on naïve centromere DNA and promotes H3 turnover on centromere regions and other loci prone to CENP-ACnp1 deposition. Prior to CENP-ACnp1 chromatin assembly, Hap2 facilitates transcription from centromere DNA. These analyses suggest that Hap2-Ino80 destabilises H3 nucleosomes on centromere DNA through transcription-coupled histone H3 turnover, driving the replacement of resident H3 nucleosomes with CENP-ACnp1 nucleosomes. These inherent properties define centromere DNA by directing a program that mediates CENP-ACnp1 assembly on appropriate sequences.

scholarly journals A quantitative screen for metabolic enzyme structures reveals patterns of assembly across the yeast metabolic network

2019 ◽  
Vol 30 (21) ◽  
pp. 2721-2736 ◽  
Author(s):  
Chalongrat Noree ◽  
Kyle Begovich ◽  
Dane Samilo ◽  
Risa Broyer ◽  
Elena Monfort ◽  
...  
Keyword(s):  
Branch Point ◽  
Biological Networks ◽  
Metabolic Pathways ◽  
Metabolic Regulation ◽  
De Novo ◽  
Metabolic Enzyme ◽  
Control Points ◽  
Branch Points ◽  
De Novo Purine Biosynthesis ◽  
Evolutionarily Conserved

Despite the proliferation of proteins that can form filaments or phase-separated condensates, it remains unclear how this behavior is distributed over biological networks. We have found that 60 of the 440 yeast metabolic enzymes robustly form structures, including 10 that assemble within mitochondria. Additionally, the ability to assemble is enriched at branch points on several metabolic pathways. The assembly of enzymes at the first branch point in de novo purine biosynthesis is coordinated, hierarchical, and based on their position within the pathway, while the enzymes at the second branch point are recruited to RNA stress granules. Consistent with distinct classes of structures being deployed at different control points in a pathway, we find that the first enzyme in the pathway, PRPP synthetase, forms evolutionarily conserved filaments that are sequestered in the nucleus in higher eukaryotes. These findings provide a roadmap for identifying additional conserved features of metabolic regulation by condensates/filaments.

scholarly journals Structural catalog of core Atg proteins opens new era of autophagy research

2021 ◽  
Author(s):  
Kazuaki Matoba ◽  
Nobuo N Noda
Keyword(s):  
De Novo ◽  
Structural Information ◽  
Membrane Dynamics ◽  
Autophagosome Formation ◽  
New Era ◽  
Intracellular Degradation ◽  
Atg Proteins ◽  
Biological Studies ◽  
Evolutionarily Conserved ◽  
Biological Methods

Summary Autophagy, which is an evolutionarily conserved intracellular degradation system, involves de novo generation of autophagosomes that sequester and deliver diverse cytoplasmic materials to the lysosome for degradation. Autophagosome formation is mediated by approximately 20 core autophagy-related (Atg) proteins, which collaborate to mediate complicated membrane dynamics during autophagy. To elucidate the molecular functions of these Atg proteins in autophagosome formation, many researchers have tried to determine the structures of Atg proteins by using various structural biological methods. Although not sufficient, the basic structural catalog of all core Atg proteins was established. In this review article, we summarize structural biological studies of core Atg proteins, with an emphasis on recently unveiled structures, and describe the mechanistic breakthroughs in autophagy research that have derived from new structural information.

scholarly journals Upstream – News in Genomics

2002 ◽  
Vol 3 (3) ◽  
pp. 221-225
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ovarian Cancer ◽  
Oryza Sativa ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Proteomic Analysis ◽  
Large Scale ◽  
Protein Complexes ◽  
The Other ◽  
Blood Samples

In recent months a bumper crop of genomes has been completed, including the fission yeast (Schizosaccharomyces pombe) and rice (Oryza sativa). Two large-scale studies ofSaccharomyces cerevisiaeprotein complexes provided a picture of the eukaryotic proteome as a network of complexes. Amongst the other stories of interest was a demonstration that proteomic analysis of blood samples can be used to detect ovarian cancer, perhaps even as early as stage I.

Sign in / Sign up

Export Citation Format

Share Document