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Sequencing of mitochondrial genomes of nine Aspergillus and Penicillium species identifies mobile introns and accessory genes as main sources of genome size variability
BackgroundThe genera Aspergillus and Penicillium include some of the most beneficial as well as the most harmful fungal species such as the penicillin-producer Penicillium chrysogenum and the human… Expand
Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways.
- Laura Segatori, P. Paukstelis, H. Gilbert, G. Georgiou
- Medicine, Chemistry
- Proceedings of the National Academy of Sciences…
- 6 July 2004
In the Escherichia coli periplasm, the formation of protein disulfide bonds is catalyzed by DsbA and DsbC. DsbA is a monomer that is maintained in a fully oxidized state by the membrane enzyme DsbB,… Expand
Toward predicting self-splicing and protein-facilitated splicing of group I introns.
In the current era of massive discoveries of noncoding RNAs within genomes, being able to infer a function from a nucleotide sequence is of paramount interest. Although studies of individual group I… Expand
Crystal structure of a DNA/Ba2+ G-quadruplex containing a water-mediated C-tetrad
- D. Zhang, Terry Huang, Philip S. Lukeman, P. Paukstelis
- Biology, Medicine
- Nucleic acids research
- 11 November 2014
We have determined the 1.50 Å crystal structure of the DNA decamer, d(CCACNVKGCGTGG) (CNVK, 3-cyanovinylcarbazole), which forms a G-quadruplex structure in the presence of Ba2+. The structure… Expand
Crystal structure of a continuous three-dimensional DNA lattice.
- P. Paukstelis, J. Nowakowski, J. Birktoft, N. Seeman
- Medicine, Materials Science
- Chemistry & biology
- 1 August 2004
DNA has proved to be a versatile material for the rational design and assembly of nanometer scale objects. Here we report the crystal structure of a continuous three-dimensional DNA lattice formed by… Expand
Structure of a tyrosyl-tRNA synthetase splicing factor bound to a group I intron RNA
The ‘RNA world’ hypothesis holds that during evolution the structural and enzymatic functions initially served by RNA were assumed by proteins, leading to the latter’s domination of biological… Expand
A tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface.
We determined a 1.95 A X-ray crystal structure of a C-terminally truncated Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) that functions in splicing group I introns.… Expand
Identification and evolution of fungal mitochondrial tyrosyl-tRNA synthetases with group I intron splicing activity
- P. Paukstelis, A. Lambowitz
- Medicine, Biology
- Proceedings of the National Academy of Sciences
- 22 April 2008
The bifunctional Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) both aminoacylates mitochondrial tRNATyr and acts as a structure-stabilizing splicing cofactor for group I… Expand
Aminoacyl-Transfer RNA Synthetase Deficiency Promotes Angiogenesis via the Unfolded Protein Response Pathway
- D. Castranova, Andrew E. Davis, +9 authors B. Weinstein
- Biology, Medicine
- Arteriosclerosis, thrombosis, and vascular…
- 1 April 2016
Objective— Understanding the mechanisms regulating normal and pathological angiogenesis is of great scientific and clinical interest. In this report, we show that mutations in 2 different… Expand
NMR Structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
The mitochondrial tyrosyl-tRNA synthetases (mt TyrRSs) of Pezizomycotina fungi are bifunctional proteins that aminoacylate mitochondrial tRNA(Tyr) and are structure-stabilizing splicing cofactors for… Expand