scholarly journals Different Proteins Mediate Step-Wise Chromosome Architectures in Thermoplasma acidophilum and Pyrobaculum calidifontis

2020 ◽  
Vol 11 ◽  
Author(s):  
Hugo Maruyama ◽  
Eloise I. Prieto ◽  
Takayuki Nambu ◽  
Chiho Mashimo ◽  
Kosuke Kashiwagi ◽  
...  
Keyword(s):  
Thermoplasma Acidophilum ◽  
Pyrobaculum Calidifontis

scholarly journals Different Proteins Mediate Step-wise Chromosome Architectures in Thermoplasma acidophilum and Pyrobaculum calidifontis

2020 ◽  
Author(s):  
Hugo Maruyama ◽  
Eloise I. Prieto ◽  
Takayuki Nambu ◽  
Chiho Mashimo ◽  
Kosuke Kashiwagi ◽  
...  
Keyword(s):  
Higher Order ◽  
Micrococcal Nuclease ◽  
Thermoplasma Acidophilum ◽  
Chromosomal Proteins ◽  
Pyrobaculum Calidifontis ◽  
Archaeal Species ◽  
Nuclease Digestion ◽  
Chromosomal Architecture ◽  
Order Structures

AbstractArchaeal species encode a variety of distinct lineage-specific chromosomal proteins. We have previously shown that in Thermococcus kodakarensis, histone, Alba, and TrmBL2 play distinct roles in chromosome organization. Although our understanding of individual archaeal chromosomal proteins has been advancing, how archaeal chromosomes are folded into higher-order structures and how they are regulated are largely unknown. Here, we investigated the primary and higher-order structures of archaeal chromosomes from different archaeal lineages. Atomic force microscopy of chromosome spreads out of Thermoplasma acidophilum and Pyrobaculum calidifontis cells revealed 10-nm fibers and 30–40-nm globular structures, suggesting the occurrence of higher-order chromosomal folding. Our results also indicated that chromosome compaction occurs toward the stationary phase. Micrococcal nuclease digestion indicated that fundamental structural units of the chromosome exist in T. acidophilum and T. kodakarensis but not in P. calidifontis or Sulfolobus solfataricus. In vitro reconstitution showed that, in T. acidophilum, the bacterial HU protein homolog HTa formed a 6-nm fiber by wrapping DNA, and that Alba was responsible for the formation of the 10-nm fiber by binding along the DNA without wrapping. Remarkably, Alba could form different higher-order complexes with histone or HTa on DNA in vitro. Mass spectrometry detected HTa in the T. acidophilum chromosome but not in other species. A putative transcriptional regulator of the AsnC/Lrp family (Pcal_1183) was detected on the P. calidifontis chromosome, but not on that of other species studied. Putative membrane-associated proteins were detected in the chromosomes of the three archaeal species studied, including T. acidophilum, P. calidifontis, and T. kodakarensis. Collectively, our data show that Archaea use different combinations of proteins to achieve chromosomal architecture and functional regulation.

Exemplar Abstract for Pyrobaculum calidifontis Amo et al. 2008.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Kara Mannor ◽  
George M Garrity ◽  
Dorothea Taylor
Keyword(s):  
Pyrobaculum Calidifontis

Probing the Substrate Promiscuity of Isopentenyl Phosphate Kinase as a Platform for Hemiterpene Analogue Production

2019 ◽  
Author(s):  
Sean Lund ◽  
Taylor Courtney ◽  
Gavin Williams
Keyword(s):  
Synthetic Biology ◽  
Building Blocks ◽  
Isoprenoid Biosynthesis ◽  
Thermoplasma Acidophilum ◽  
Substrate Promiscuity ◽  
Enzymatic Pathways ◽  
First Time ◽  
Rate Limiting ◽  
Alcohol Dependent ◽  
Isopentenyl Phosphate

Isoprenoids are a large class of natural products with wide-ranging applications. Synthetic biology approaches to the manufacture of isoprenoids and their new-to-nature derivatives are limited due to the provision in Nature of just two hemiterpene building blocks for isoprenoid biosynthesis. To address this limitation, artificial chemo-enzymatic pathways such as the alcohol-dependent hemiterpene pathway (ADH) serve to leverage consecutive kinases to convert exogenous alcohols to pyrophosphates that could be coupled to downstream isoprenoid biosynthesis. To be successful, each kinase in this pathway should be permissive of a broad range of substrates. For the first time, we have probed the promiscuity of the second enzyme in the ADH pathway, isopentenyl phosphate kinase from Thermoplasma acidophilum, towards a broad range of acceptor monophosphates. Subsequently, we evaluate the suitability of this enzyme to provide non-natural pyrophosphates and provide a critical first step in characterizing the rate limiting steps in the artificial ADH pathway.<br>

Occurrence of -Amino Acids and a Pyridoxal 5′-Phosphate-Dependent Aspartate Racemase in the Acidothermophilic Archaeon, Thermoplasma acidophilum

2001 ◽  
Vol 281 (2) ◽  
pp. 317-321 ◽  
Author(s):  
Zhiqun Long ◽  
Jen-Ai Lee ◽  
Taizo Okamoto ◽  
Masae Sekine ◽  
Noriyuki Nimura ◽  
...  
Keyword(s):  
Amino Acids ◽  
Thermoplasma Acidophilum ◽  
Aspartate Racemase

Enhancing H2O2 resistance of an esterase from Pyrobaculum calidifontis by structure-guided engineering of the substrate binding site

2017 ◽  
Vol 101 (14) ◽  
pp. 5689-5697 ◽  
Author(s):  
Pengfei Zhou ◽  
Dongming Lan ◽  
Grzegorz Maria Popowicz ◽  
Xuping Wang ◽  
Bo Yang ◽  
...  
Keyword(s):  
Binding Site ◽  
Substrate Binding ◽  
Substrate Binding Site ◽  
Pyrobaculum Calidifontis ◽  
H2o2 Resistance

Endotoxin-Like Activities of Mycoplasmal Lipopolysaccharides (Lipoglycans)

1980 ◽  
Vol 29 (3) ◽  
pp. 990-994
Author(s):  
Robert C. Seid ◽  
Paul F. Smith ◽  
Gabriel Guevarra ◽  
H. Donald Hochstein ◽  
Michael F. Barile
Keyword(s):  
Escherichia Coli ◽  
Synthetic Peptide ◽  
Active Role ◽  
Peptide Bond ◽  
Febrile Response ◽  
Thermoplasma Acidophilum ◽  
Amidase Activity ◽  
E Coli

Lipoglycans (previously designated lipopolysaccharides) from several species of Acholeplasma and from Thermoplasma acidophilum were examined for endotoxin-like activities as measured by the standard rabbit fever test and the Limulus amoebocyte lysate assay. The lipoglycans from Acholeplasma granularum, Achloplasma laidlawii, Acholeplasma modicum , and Acholeplasma oculi caused a febrile response at concentrations of 1 ng/ml per kg or greater, whereas with control Escherichia coli EC-2 lipopolysaccharides, 6.25 ng/ml per kg was required. Similar results were obtained in the Limulus amoebocyte lysate test. The minimum concentrations in nanograms per milliliter required to stimulate formation of a solid clot were: Acholeplasma axanthum , 0.22; A. granularum , 0.85; A. modicum , 0.51; A. laidlawii , 1.05; A. oculi , 0.74. Standard E. coli 1B lipopolysaccharide required a concentration of 0.125 ng/ml. Thermoplasma lipoglycan was least active, requiring 4.25 ng/ml. Clotting of the Limulus lysate proceeds by the activation by lipopolysaccharide plus Ca 2+ of a proenzyme which cleaves an arginine-lysine peptide bond of the coagulogen. The clotting and amidase activities are inactivated by deoxycholate and can be reactivated by addition of lipopolysaccharide and Ca 2+ . As with E. coli 1B lipopolysaccharide, acholeplasmal lipoglycans were shown to restore both clotting and amidase activities of the deoxycholate-inactivated Limulus clotting enzyme. The degree of restoration of amidase activity by mycoplasmal lipoglycans relative to E. coli lipopolysaccharide (1.00) were: A. axanthum , 1.71; A. modicum , 1.22; A. granularum , 0.61; and Thermoplasma , 0.37. The coagulating enzyme, restored with either E. coli lipopolysaccharide or mycoplasmal lipoglycans, was able to react with the synthetic peptide benzoyl-Ile-Glu-(γ-OCH 3 )-Gly-p-nitroaniline (an analog of the coagulogen) or with the purified coagulogen itself to form the clot. The mycoplasmal lipoglycans alone were incapable of promoting these reactions when incubated with the synthetic peptide or with the purified coagulogen, thereby ruling out the contamination of these lipoglycans with proteases capable of cleaving the same Arg-Lys peptide bond of the coagulogen. These results show that acholeplasmal lipoglycans possess endotoxin-like activities. Their passive or active role in disease remains to be established.

scholarly journals A Reexamination of Thioredoxin Reductase from Thermoplasma acidophilum, a Thermoacidophilic Euryarchaeon, Identifies It as an NADH-Dependent Enzyme

ACS Omega ◽  
2017 ◽  
Vol 2 (8) ◽  
pp. 4180-4187 ◽  
Author(s):  
Dwi Susanti ◽  
Usha Loganathan ◽  
Austin Compton ◽  
Biswarup Mukhopadhyay
Keyword(s):  
Thioredoxin Reductase ◽  
Thermoplasma Acidophilum

The crystal structure of an esterase from the hyperthermophilic microorganism Pyrobaculum calidifontis VA1 explains its enantioselectivity

2011 ◽  
Vol 91 (4) ◽  
pp. 1061-1072 ◽  
Author(s):  
Gottfried J. Palm ◽  
Elena Fernández-Álvaro ◽  
Xenia Bogdanović ◽  
Sebastian Bartsch ◽  
Jaroslaw Sczodrok ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Pyrobaculum Calidifontis ◽  
Hyperthermophilic Microorganism
Sign in / Sign up

Export Citation Format

Share Document