scholarly journals A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells

2018 ◽  
Author(s):  
Güleycan Lutfullahoğlu-Bal ◽  
Ayşe Bengisu Seferoğlu ◽  
Abdurrahman Keskinb ◽  
Emel Akdoğan ◽  
Cory D. Dunna
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Horizontal Gene Transfer ◽  
Genetic Information ◽  
Mammalian Cells ◽  
Eukaryotic Cells ◽  
Peroxisomal Biogenesis ◽  
Endogenous Role ◽  
Excellent Tool ◽  
Peroxisomal Function

ABSTRACTProkaryotes can provide new genetic information to eukaryotes by horizontal gene transfer (HGT), and such transfers are likely to have been particularly consequential at the dawn of eukaryogenesis. Since eukaryotes are highly compartmentalized, it is worthwhile to consider the mechanisms by which newly transferred proteins might reach diverse organellar destinations. Toward this goal, we have focused our attention upon the behavior of bacteria-derived tail anchors (TAs) expressed in the eukaryote Saccharomyces cerevisiae. In this study, we report that a predicted membrane-associated domain of the Escherichia coli YgiM protein is specifically trafficked to peroxisomes in budding yeast, can be found at a pre-peroxisomal compartment (PPC) upon disruption of peroxisomal biogenesis, and can functionally replace an endogenous peroxisome-directed TA. Furthermore, the YgiM(TA) can also localize to peroxisomes in mammalian cells. Since the YgiM(TA) plays no endogenous role in peroxisomal function or assembly, this domain is likely to serve as an excellent tool toward illumination of the mechanisms by which TAs can travel to peroxisomes. Moreover, our findings emphasize the ease with which bacteria-derived sequences might target to organelles in eukaryotic cells following HGT, and we discuss the importance of flexible recognition of organelle targeting information during and after eukaryogenesis.

scholarly journals Minimal and RNA-free RNase P in Aquifex aeolicus

2017 ◽  
Vol 114 (42) ◽  
pp. 11121-11126 ◽  
Author(s):  
Astrid I. Nickel ◽  
Nadine B. Wäber ◽  
Markus Gößringer ◽  
Marcus Lechner ◽  
Uwe Linne ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Rnase P ◽  
Aquifex Aeolicus ◽  
Trna Processing ◽  
Hyperthermophilic Bacterium ◽  
Domains Of Life

RNase P is an essential tRNA-processing enzyme in all domains of life. We identified an unknown type of protein-only RNase P in the hyperthermophilic bacterium Aquifex aeolicus: Without an RNA subunit and the smallest of its kind, the 23-kDa polypeptide comprises a metallonuclease domain only. The protein has RNase P activity in vitro and rescued the growth of Escherichia coli and Saccharomyces cerevisiae strains with inactivations of their more complex and larger endogenous ribonucleoprotein RNase P. Homologs of Aquifex RNase P (HARP) were identified in many Archaea and some Bacteria, of which all Archaea and most Bacteria also encode an RNA-based RNase P; activity of both RNase P forms from the same bacterium or archaeon could be verified in two selected cases. Bioinformatic analyses suggest that A. aeolicus and related Aquificaceae likely acquired HARP by horizontal gene transfer from an archaeon.

scholarly journals Pi sensing and signalling: from prokaryotic to eukaryotic cells

2016 ◽  
Vol 44 (3) ◽  
pp. 766-773 ◽  
Author(s):  
Wanjun Qi ◽  
Stephen A. Baldwin ◽  
Stephen P. Muench ◽  
Alison Baker
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Energy Metabolism ◽  
Crop Yield ◽  
Molecular Basis ◽  
Eukaryotic Cells ◽  
Future Research ◽  
Use Efficiency ◽  
Similarities And Differences ◽  
Insight Into

Phosphorus is one of the most important macronutrients and is indispensable for all organisms as a critical structural component as well as participating in intracellular signalling and energy metabolism. Sensing and signalling of phosphate (Pi) has been extensively studied and is well understood in single-cellular organisms like bacteria (Escherichia coli) and Saccharomyces cerevisiae. In comparison, the mechanism of Pi regulation in plants is less well understood despite recent advances in this area. In most soils the available Pi limits crop yield, therefore a clearer understanding of the molecular basis underlying Pi sensing and signalling is of great importance for the development of plants with improved Pi use efficiency. This mini-review compares some of the main Pi regulation pathways in prokaryotic and eukaryotic cells and identifies similarities and differences among different organisms, as well as providing some insight into future research.

scholarly journals Bacterial Toxin-Antitoxin Gene System as Containment Control in Yeast Cells

2000 ◽  
Vol 66 (12) ◽  
pp. 5524-5526 ◽  
Author(s):  
P. Kristoffersen ◽  
G. B. Jensen ◽  
K. Gerdes ◽  
J. Piškur
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Yeast Cells ◽  
Eukaryotic Cells ◽  
Bacterial Toxin ◽  
Containment Control ◽  
Industrial Fermentation ◽  
Fermentation Processes ◽  
Gene System ◽  
Potential Applications

ABSTRACT The potential of a bacterial toxin-antitoxin gene system for use in containment control in eukaryotes was explored. The Escherichia coli relE and relB genes were expressed in the yeastSaccharomyces cerevisiae. Expression of therelE gene was highly toxic to yeast cells. However, expression of the relB gene counteracted the effect ofrelE to some extent, suggesting that toxin-antitoxin interaction also occurs in S. cerevisiae. Thus, bacterial toxin-antitoxin gene systems also have potential applications in the control of cell proliferation in eukaryotic cells, especially in those industrial fermentation processes in which the escape of genetically modified cells would be considered highly risky.

Pyridoxamine-phosphate oxidases and pyridoxamine-phosphate oxidase-related proteins catalyze the oxidation of 6-NAD(P)H to NAD(P)+

2019 ◽  
Vol 476 (20) ◽  
pp. 3033-3052 ◽  
Author(s):  
Alexandre Y. Marbaix ◽  
Georges Chehade ◽  
Gaëtane Noël ◽  
Pierre Morsomme ◽  
Didier Vertommen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Arabidopsis Thaliana ◽  
Mammalian Cells ◽  
Reduced Form ◽  
Nostoc Punctiforme ◽  
Catalytic Function ◽  
Related Proteins ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract 6-NADH and 6-NADPH are strong inhibitors of several dehydrogenases that may form spontaneously from NAD(P)H. They are known to be oxidized to NAD(P)+ by mammalian renalase, an FAD-linked enzyme mainly present in heart and kidney, and by related bacterial enzymes. We partially purified an enzyme oxidizing 6-NADPH from rat liver, and, surprisingly, identified it as pyridoxamine-phosphate oxidase (PNPO). This was confirmed by the finding that recombinant mouse PNPO oxidized 6-NADH and 6-NADPH with catalytic efficiencies comparable to those observed with pyridoxine- and pyridoxamine-5′-phosphate. PNPOs from Escherichia coli, Saccharomyces cerevisiae and Arabidopsis thaliana also displayed 6-NAD(P)H oxidase activity, indicating that this ‘side-activity’ is conserved. Remarkably, ‘pyridoxamine-phosphate oxidase-related proteins’ (PNPO-RP) from Nostoc punctiforme, A. thaliana and the yeast S. cerevisiae (Ygr017w) were not detectably active on pyridox(am)ine-5′-P, but oxidized 6-NADH, 6-NADPH and 2-NADH suggesting that this may be their main catalytic function. Their specificity profiles were therefore similar to that of renalase. Inactivation of renalase and of PNPO in mammalian cells and of Ygr017w in yeasts led to the accumulation of a reduced form of 6-NADH, tentatively identified as 4,5,6-NADH3, which can also be produced in vitro by reduction of 6-NADH by glyceraldehyde-3-phosphate dehydrogenase or glucose-6-phosphate dehydrogenase. As 4,5,6-NADH3 is not a substrate for renalase, PNPO or PNPO-RP, its accumulation presumably reflects the block in the oxidation of 6-NADH. These findings indicate that two different classes of enzymes using either FAD (renalase) or FMN (PNPOs and PNPO-RPs) as a cofactor play an as yet unsuspected role in removing damaged forms of NAD(P).

scholarly journals The Saccharomyces cerevisiae SCS2 Gene Product, a Homolog of a Synaptobrevin-Associated Protein, Is an Integral Membrane Protein of the Endoplasmic Reticulum and Is Required for Inositol Metabolism

1998 ◽  
Vol 180 (7) ◽  
pp. 1700-1708 ◽  
Author(s):  
Satoshi Kagiwada ◽  
Kohei Hosaka ◽  
Masayuki Murata ◽  
Jun-ichi Nikawa ◽  
Akira Takatsuki
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Amino Acid ◽  
Gene Product ◽  
Mammalian Cells ◽  
Aplysia Californica ◽  
Integral Membrane Protein ◽  
Yeast Cells ◽  
Eukaryotic Cells ◽  
Genetic Studies

ABSTRACT The Saccharomyces cerevisiae SCS2 gene has been cloned as a suppressor of inositol auxotrophy of CSE1 andhac1/ire15 mutants (J. Nikawa, A. Murakami, E. Esumi, and K. Hosaka, J. Biochem. 118:39–45, 1995) and has homology with a synaptobrevin/VAMP-associated protein, VAP-33, cloned fromAplysia californica (P. A. Skehel, K. C. Martin, E. R. Kandel, and D. Bartsch, Science 269:1580–1583, 1995). In this study we have characterized an SCS2 gene product (Scs2p). The product has a molecular mass of 35 kDa and is C-terminally anchored to the endoplasmic reticulum, with the bulk of the protein located in the cytosol. The disruption of the SCS2 gene causes yeast cells to exhibit inositol auxotrophy at temperatures of above 34°C. Genetic studies reveal that the overexpression of theINO1 gene rescues the inositol auxotrophy of theSCS2 disruption strain. The significant primary structural feature of Scs2p is that the protein contains the 16-amino-acid sequence conserved in yeast and mammalian cells. The sequence is required for normal Scs2p function, because a mutant Scs2p that lacks the sequence does not complement the inositol auxotrophy of theSCS2 disruption strain. Therefore, the Scs2p function might be conserved among eukaryotic cells.

scholarly journals Feedback regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cerevisiae.

1994 ◽  
Vol 5 (6) ◽  
pp. 655-665 ◽  
Author(s):  
D Dimster-Denk ◽  
M K Thorsness ◽  
J Rine
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Mammalian Cells ◽  
Coenzyme A ◽  
Mevalonate Pathway ◽  
Feedback Regulation ◽  
Eukaryotic Cells ◽  
Yeast Gene ◽  
Hmg Coa Reductase ◽  
Common Precursor ◽  
Coa Reductase

In eukaryotic cells all isoprenoids are synthesized from a common precursor, mevalonate. The formation of mevalonate from 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) is catalyzed by HMG-CoA reductase and is the first committed step in isoprenoid biosynthesis. In mammalian cells, synthesis of HMG-CoA reductase is subject to feedback regulation at multiple molecular levels. We examined the state of feedback regulation of the synthesis of the HMG-CoA reductase isozyme encoded by the yeast gene HMG1 to examine the generality of this regulatory pattern. In yeast, synthesis of Hmg1p was subject to feedback regulation. This regulation of HMG-CoA reductase synthesis was independent of any change in the level of HMG1 mRNA. Furthermore, regulation of Hmg1p synthesis was keyed to the level of a nonsterol product of the mevalonate pathway. Manipulations of endogenous levels of several isoprenoid intermediates, either pharmacologically or genetically, suggested that mevalonate levels may control the synthesis of Hmg1p through effects on translation.

Expression of human parathyroid hormone in mammalian cells, Escherichia coli and Saccharomyces cerevisiae

1994 ◽  
Vol 33 (3) ◽  
pp. 293-306 ◽  
Author(s):  
Erik Rokkones ◽  
B. Najma Kareem ◽  
Ole K. Olstad ◽  
Anders Høgset ◽  
Kerstin Schenstrøm ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Parathyroid Hormone ◽  
Mammalian Cells ◽  
Human Parathyroid Hormone

Microbe Engineering of Guaia-6,10(14)-diene as a Building Block for the Semisynthetic Production of Plant-Derived (−)-Englerin A

2019 ◽  
Author(s):  
Thomas Siemon ◽  
Zhangqian Wang ◽  
Guangkai Bian ◽  
Tobias Seitz ◽  
Ziling Ye ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Synthetic Biology ◽  
Chemical Synthesis ◽  
Building Block ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Economical Method ◽  
Englerin A ◽  
Transient Receptor

Herein, we report the semisynthetic production of the potent transient receptor potential canonical (TRPC) channel agonist (−)-englerin A (EA), using guaia-6,10(14)-diene as the starting material. Guaia-6,10(14)-diene was systematically engineered in Escherichia coli and Saccharomyces cerevisiae using the CRISPR/Cas9 system and produced with high titers. This provided us the opportunity to execute a concise chemical synthesis of EA and the two related guaianes (−)-oxyphyllol and (+)-orientalol E. The potentially scalable approach combines the advantages of synthetic biology and chemical synthesis and provides an efficient and economical method for producing EA as well as its analogs.

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