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Wyświetlanie 1-15 z 16
Tytuł:
Ex-translational function of tRNAs and their fragments in cancer
Autorzy:
Mleczko, Anna
Celichowski, Piotr
Bąkowska-Żywicka, Kamilla
Powiązania:
https://bibliotekanauki.pl/articles/1039278.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
tRNA
tRNA-derived fragments
cancer
Opis:
Transfer RNA (tRNA) molecules are most commonly known as the molecular amino acids carriers and also because of the role they play in a protein biosynthesis process. However, tRNA biology has revealed stupendous levels of many unexpected discoveries that put a new light on tRNA function in different processes besides translation, like apoptosis or cancer development. In recent years various species of RNAs have been found differentially expressed in different types of cancer. In this review we focus our attention on tRNAs as well as on tRNA-derived small RNAs ex-translational functions in human cells in oncogenesis and oncobiology.
Źródło:
Acta Biochimica Polonica; 2014, 61, 2; 211-216
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Genomics and the evolution of aminoacyl-tRNA synthesis.
Autorzy:
Ruan, Benfang
Ahel, Ivan
Ambrogelly, Alex
Becker, Hubert
Bunjun, Shipra
Feng, Liang
Tumbula-Hansen, Debra
Ibba, Michael
Korencic, Dragana
Kobayashi, Hiroyuki
Jacquin-Becker, Clarisse
Mejlhede, Nina
Min, Bokkee
Raczniak, Gregory
Rinehart, Jesse
Stathopoulos, Constantinos
Li, Tong
Söll, Dieter
Powiązania:
https://bibliotekanauki.pl/articles/1044116.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
evolution
tRNA
aminoacyl-tRNA
translation
protein synthesis
Opis:
Translation is the process by which ribosomes direct protein synthesis using the genetic information contained in messenger RNA (mRNA). Transfer RNAs (tRNAs) are charged with an amino acid and brought to the ribosome, where they are paired with the corresponding trinucleotide codon in mRNA. The amino acid is attached to the nascent polypeptide and the ribosome moves on to the next codon. Thus, the sequential pairing of codons in mRNA with tRNA anticodons determines the order of amino acids in a protein. It is therefore imperative for accurate translation that tRNAs are only coupled to amino acids corresponding to the RNA anticodon. This is mostly, but not exclusively, achieved by the direct attachment of the appropriate amino acid to the 3'-end of the corresponding tRNA by the aminoacyl-tRNA synthetases. To ensure the accurate translation of genetic information, the aminoacyl-tRNA synthetases must display an extremely high level of substrate specificity. Despite this highly conserved function, recent studies arising from the analysis of whole genomes have shown a significant degree of evolutionary diversity in aminoacyl-tRNA synthesis. For example, non-canonical routes have been identified for the synthesis of Asn-tRNA, Cys-tRNA, Gln-tRNA and Lys-tRNA. Characterization of non-canonical aminoacyl-tRNA synthesis has revealed an unexpected level of evolutionary divergence and has also provided new insights into the possible precursors of contemporary aminoacyl-tRNA synthetases.
Źródło:
Acta Biochimica Polonica; 2001, 48, 2; 313-321
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The new aspects of aminoacyl-tRNA synthetases.
Autorzy:
Szymański, Maciej
Deniziak, Marzanna
Barciszewski, Jan
Powiązania:
https://bibliotekanauki.pl/articles/1044333.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
tRNA
aminoacylation
protein biosynthesis
aminoacyl-tRNA synthetases
Opis:
Aminoacyl-tRNA synthetases (AARS) are essential proteins found in all living organisms. They form a diverse group of enzymes that ensure the fidelity of transfer of genetic information from the DNA into the protein. AARS catalyse the attachment of amino acids to transfer RNAs and thereby establish the rules of the genetic code by virtue of matching the nucleotide triplet of the anticodon with its cognate amino acid. Here we summarise the effects of recent studies on this interesting family of multifunctional enzymes.
Źródło:
Acta Biochimica Polonica; 2000, 47, 3; 821-834
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The genetic code - 40 years on
Autorzy:
Szymański, Maciej
Barciszewski, Jan
Powiązania:
https://bibliotekanauki.pl/articles/1041109.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
tRNA
genetic code
aminoacyl-tRNA synthetase
Opis:
The genetic code discovered 40 years ago, consists of 64 triplets (codons) of nucleotides. The genetic code is almost universal. The same codons are assigned to the same amino acids and to the same START and STOP signals in the vast majority of genes in animals, plants, and microorganisms. Each codon encodes for one of the 20 amino acids used in the synthesis of proteins. That produces some redundancy in the code and most of the amino acids being encoded by more than one codon. The two cases have been found where selenocysteine or pyrrolysine, that are not one of the standard 20 is inserted by a tRNA into the growing polypeptide.
Źródło:
Acta Biochimica Polonica; 2007, 54, 1; 51-54
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Pathways of tRNA turnover in eukaryotic cells
Autorzy:
Turowski, T. W.
Powiązania:
https://bibliotekanauki.pl/articles/115770.pdf
Data publikacji:
2011
Wydawca:
Fundacja na Rzecz Młodych Naukowców
Tematy:
tRNA turnover
rapid tRNA decay
polymerase III
Opis:
Cell ability to control amount of a transfer RNA is one of the ways to regulate rate of protein synthesis. Because 80–90% dry mass of cells are proteins, the level of translation is determinant to the cell growth. Growth of cells is a key question in tumors therapy and biotechnology. tRNA turnover consist of a three pathways described in a last few years: exosome and TRAMP complex dependent pathway in nucleus, directed to hypomodified or affected tRNA; rapid tRNA decay pathway involving two 5’–3’ exonucleases Rat1 and Xrn1, proposed to occur in nucleus and cytoplasm; stress-activated endonucleolytic cleavage to tRNA halves pathway, founded in cytoplasm with a clear role to direct regulation of translation by tRNA half-molecules inhibition.
Źródło:
Challenges of Modern Technology; 2011, 2, 2; 63-65
2082-2863
2353-4419
Pojawia się w:
Challenges of Modern Technology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Methionyl-tRNA synthetase.
Autorzy:
Deniziak, Marzanna
Barciszewski, Jan
Powiązania:
https://bibliotekanauki.pl/articles/1044120.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein-protein interactions
tRNA binding
Opis:
Methionyl-tRNA synthetase (MetRS) belongs to the family of 20 enzymes essential for protein biosynthesis. It links covalently methionine with its cognate tRNA. Crystal structures solved for bacterial MetRSs have given a number of interesting insights into enzyme architecture and methionylation catalysis. A comparison of sequences of MetRSs belonging to all kingdoms of life, as well as numerous biochemical and genetic studies have revealed the presence of various additional domains appended to the catalytic core of synthetase. They are responsible for interactions with tRNA and proteins. Tertiary structure of C-terminal tRNA-binding appendices can be deduced from those determined for their homologues: tRNA binding protein 111 and endothelial monocyte-activating polypeptide II. Contacts between MetRS and other proteins could be mediated not only by noncatalytic peptides but also by structural elements present in the catalytic core, e.g. Arg-Gly-Asp (RGD) motifs. Additional activities involve MetRS in the maintenance of translational fidelity and in coordination of ribosome biogenesis with protein synthesis.
Źródło:
Acta Biochimica Polonica; 2001, 48, 2; 337-350
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Aminoacyl-tRNA synthetases and aminoacylation of tRNA in the nucleus.
Autorzy:
Mucha, Piotr
Powiązania:
https://bibliotekanauki.pl/articles/1043799.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
nuclear translation
nuclear localization signal
nuclear export
aminoacyl-tRNA synthetase
tRNA aminoacylation
Opis:
This review is focused on findings concerning the presence of translation apparatus components (aminoacyl-tRNA synthetases, aminoacyl-tRNA, elongation factors) as well as translation itself in the nucleus. A nuclear role of these molecules is unknown. New findings suggest that well-accepted model of spatial segregation of transcription and translation in eukaryotic cell may be oversimplifcation. Nuclear coupling of both these processes show us how exciting and surprising may be the world of the living cell.
Źródło:
Acta Biochimica Polonica; 2002, 49, 1; 1-10
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Editing of plant mitochondrial transfer RNAs
Autorzy:
Fey, Julien
Weil, Jacques
Tomita, K
Cosset, Anne
Dietrich, André
Small, Ian
Maréchal-Drouard, Laurence
Powiązania:
https://bibliotekanauki.pl/articles/1044127.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
tRNA
pseudouridine
plant mitochondria
processing
RNA editing
Opis:
Editing in plant mitochondria consists in C to U changes and mainly affects messenger RNAs, thus providing the correct genetic information for the biosynthesis of mitochondrial (mt) proteins. But editing can also affect some of the plant mt tRNAs encoded by the mt genome. In dicots, a C to U editing event corrects a C:A mismatch into a U:A base-pair in the acceptor stem of mt tRNAPhe (GAA). In larch mitochondria, three C to U editing events restore U:A base-pairs in the acceptor stem, D stem and anticodon stem, respectively, of mt tRNAHis (GUG). For both these mt tRNAs editing of the precursors is a prerequisite for their processing into mature tRNAs. In potato mt tRNACys (GCA), editing converts a C28:U42 mismatch in the anticodon stem into a U28:U42 non-canonical base-pair, and reverse transcriptase minisequencing has shown that the mature mt tRNACys is fully edited. In the bryophyte Marchantia polymorpha this U residue is encoded in the mt genome and evolutionary studies suggest that restoration of the U28 residue is necessary when it is not encoded in the gene. However, in vitro studies have shown that neither processing of the precursor nor aminoacylation of tRNACys requires C to U editing at this position. But sequencing of the purified mt tRNACys has shown that is present at position 28, indicating that C to U editing is a prerequisite for the subsequent isomerization of U into Ψ at position 28.
Źródło:
Acta Biochimica Polonica; 2001, 48, 2; 383-389
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The fidelity of the translation of the genetic code.
Autorzy:
Sankaranarayanan, Rajan
Moras, Dino
Powiązania:
https://bibliotekanauki.pl/articles/1044119.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
evolution
genetic code
translation
editing
aminoacyl-tRNA synthetase
Opis:
Aminoacyl-tRNA synthetases play a central role in maintaining accuracy during the translation of the genetic code. To achieve this challenging task they have to discriminate against amino acids that are very closely related not only in structure but also in chemical nature. A 'double-sieve' editing model was proposed in the late seventies to explain how two closely related amino acids may be discriminated. However, a clear understanding of this mechanism required structural information on synthetases that are faced with such a problem of amino acid discrimination. The first structural basis for the editing model came recently from the crystal structure of isoleucyl-tRNA synthetase, a class I synthetase, which has to discriminate against valine. The structure showed the presence of two catalytic sites in the same enzyme, one for activation, a coarse sieve which binds both isoleucine and valine, and another for editing, a fine sieve which binds only valine and rejects isoleucine. Another structure of the enzyme in complex with tRNA showed that the tRNA is responsible for the translocation of the misactivated amino-acid substrate from the catalytic site to the editing site. These studies were mainly focused on class I synthetases and the situation was not clear about how class II enzymes discriminate against similar amino acids. The recent structural and enzymatic studies on threonyl-tRNA synthetase, a class II enzyme, reveal how this challenging task is achieved by using a unique zinc ion in the active site as well as by employing a separate domain for specific editing activity. These studies led us to propose a model which emphasizes the mirror symmetrical approach of the two classes of enzymes and highlights that tRNA is the key player in the evolution of these class of enzymes.
Źródło:
Acta Biochimica Polonica; 2001, 48, 2; 323-335
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Regulation of RNA polymerase III transcription by Maf1 protein
Autorzy:
Cieśla, Małgorzata
Boguta, Magdalena
Powiązania:
https://bibliotekanauki.pl/articles/1040733.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
transcription regulation
RNA polymerase III
tRNA synthesis
Maf1 repressor
Opis:
Maf1 was the first protein discovered to regulate polymerase III RNA in yeast and because it is evolutionarily conserved, a Maf1 ortholog also serves to restrain transcription in mouse and human cells. Understanding the mechanism of the regulation has been made possible by recent studies showing that Maf1 is a nuclear/cytoplasmic protein whose subcellular distribution and hence negative regulation of Pol III transcription is mediated by the nutrient-sensing signaling pathways, TOR and RAS. Under stress conditions and during growth in a nonfermentable carbon source Maf1 is dephosphorylated and imported to the nucleus. In its non-phosphorylated form, Maf1 interacts with the polymerase III transcription machinery. Phosphorylation serves to locate Maf1 to the cytoplasm under favorable growth conditions, thereby preventing it from non-negatively regulating polymerase III when high levels of tRNA transcription are required. Relocation of Maf1 to the cytoplasm is dependent on Msn5, a carrier responsible for export of several other phosphoproteins out of the nucleus. The absence of Maf1-mediated control of tRNA synthesis impairs yeast viability in nonfermentable carbon sources. Moreover, in cells grown in a nonfermentable carbon source, Maf1 regulates the levels of different tRNAs to various extents. This differential regulation may contribute to the physiological role of Maf1.
Źródło:
Acta Biochimica Polonica; 2008, 55, 2; 215-225
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Molecular dynamic simulations of large RNA molecules: the yeast tRNA^{Phe}
Autorzy:
Pliszka, B.
Ołodziej, S.
Powiązania:
https://bibliotekanauki.pl/articles/1954518.pdf
Data publikacji:
1999
Wydawca:
Politechnika Gdańska
Tematy:
tRNA Phe
molecular dynamics
modified bases
nucleic acids
electrostatic interaction
Opis:
Molecular dynamics trajectories (700 ps) of the solvated and neutralized 75-residue yeast tRNA Phe were generated using the AMBER 5.0 molecular dynamics software package. The cut-off scheme was used to treat electrostatic interactions; consequently, all long-range interactions beyond 12 angstroms were neglected. The equilibration procedure and conditions during simulations led to a dynamically stable model of the tRNA molecule. During the simulations all base-base interactions (which determine the secondary and the tertiary structure of the molecule) were well preserved. Consequently, the global shape of the molecule was preserved well and the RMS deviation calculated between the starting x-ray structure and the final structure after 700 ps of simulations was 3.25 angstroms. The biggest deviation is observed in the region of the anticodon hairpin loop; this high mobility is associated with the presence of a very unusual Y-base and a binding site of a magnesium ion in this region.
Źródło:
TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk; 1999, 3, 3; 333-342
1428-6394
Pojawia się w:
TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Quality control in tRNA charging - editing of homocysteine
Autorzy:
Jakubowski, Hieronim
Powiązania:
https://bibliotekanauki.pl/articles/1039906.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
tRNA synthetase editing
homocysteine
protein synthesis
protein modification
cardiovascular disease
neurodegeneration
Opis:
All living organisms conduct protein synthesis with a high degree of accuracy maintained in the transmission and flow of information from a gene to protein product. One crucial 'quality control' point in maintaining a high level of accuracy is the selectivity by which aminoacyl-tRNA synthetases furnish correctly activated amino acids, attached to tRNA species, as the building blocks for growing protein chains. When differences in binding energies of amino acids to an aminoacyl-tRNA synthetase are inadequate, editing is used as a major determinant of enzyme selectivity. Some incorrect amino acids are edited at the active site before the transfer to tRNA (pre-transfer editing), while others are edited after transfer to tRNA at a separate editing site (post-transfer editing). Access of natural non-protein amino acids, such as homocysteine, homoserine, or ornithine to the genetic code is prevented by the editing function of aminoacyl-tRNA synthetases. Disabling editing function leads to tRNA mischarging errors and incorporation of incorrect amino acids into protein, which is detrimental to cell homeostasis and inhibits growth. Continuous homocysteine editing by methionyl-tRNA synthetase, resulting in the synthesis of homocysteine thiolactone, is part of the process of tRNA aminoacylation in living organisms, from bacteria to man. Excessive homocysteine thiolactone synthesis in hyperhomocysteinemia caused by genetic or nutritional deficiencies is linked to human vascular and neurological diseases.
Źródło:
Acta Biochimica Polonica; 2011, 58, 2; 149-163
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Rsp5 ubiquitin ligase affects isoprenoid pathway and cell wall organization in S. cerevisiae.
Autorzy:
Kamińska, Joanna
Kwapisz, Marta
Grabińska, Kariona
Orłowski, Jacek
Boguta, Magdalena
Palamarczyk, Grażyna
Żołądek, Teresa
Powiązania:
https://bibliotekanauki.pl/articles/1041478.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Rsp5 ubiquitin ligase
cell wall
Mod5 tRNA: isopentenyltransferase
ergosterol
Opis:
Dimethylallyl diphosphate, an isomer of isopentenyl diphosphate, is a common substrate of Mod5p, a tRNA modifying enzyme, and the farnesyl diphosphate synthase Erg20p, the key enzyme of the isoprenoid pathway. rsp5 mutants, defective in the Rsp5 ubiquitin-protein ligase, were isolated and characterized as altering the mitochondrial/cytosolic distribution of Mod5p. To understand better how competition for the substrate determines the regulation at the molecular level, we analyzed the effect of the rsp5-13 mutation on Erg20p expression. The level of Erg20p was three times lower in rsp5-13 compared to the wild type strain and this effect was dependent on active Mod5p. Northern blot analysis indicated a regulatory role of Rsp5p in ERG20 transcription. ERG20 expression was also impaired in pkc1Δ lacking a component of the cell wall integrity signaling pathway. Low expression of Erg20p in rsp5 cells was accompanied by low level of ergosterol, the main end product of the isoprenoid pathway. Additionally, rsp5 strains were resistant to nystatin, which binds to ergosterol present in the plasma membrane, and sensitive to calcofluor white, a drug destabilizing cell wall integrity by binding to chitin. Furthermore, the cell wall structure appeared abnormal in most rsp5-13 cells investigated by electron microscopy and chitin level in the cell wall was increased two-fold. These results indicate that Rsp5p affects the isoprenoid pathway which has important roles in ergosterol biosynthesis, protein glycosylation and transport and in this way may influence the composition of the plasma membrane and cell wall.
Źródło:
Acta Biochimica Polonica; 2005, 52, 1; 207-220
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Sequence analysis of enzymes with asparaginase activity.
Autorzy:
Borek, Dominika
Jaskólski, Mariusz
Powiązania:
https://bibliotekanauki.pl/articles/1044033.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
N-terminal nucleophile hydrolase
lysophospholipase
tRNA amidotransferase
aspartylglucosaminidase
asparaginase
L-asparagine
Opis:
Asparaginases catalyze the hydrolysis of asparagine to aspartic acid and ammonia. Enzymes with asparaginase activity play an important role both in the metabolism of all living organisms as well as in pharmacology. The main goal of this paper is to attempt a classification of all known enzymes with asparaginase activity, based on their amino acid sequences. Some possible phylogenetic consequences are also discussed using dendrograms and structural information derived from crystallographic studies.
Źródło:
Acta Biochimica Polonica; 2001, 48, 4; 893-902
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
MELAS as an example of a mitochondrial disease
Autorzy:
Piechota, J
Mroczek, K.
Bartnik, E.
Powiązania:
https://bibliotekanauki.pl/articles/2041823.pdf
Data publikacji:
2001
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
encephalopathia
pathogenesis
mitochondrial DNA
genetics
tRNA gene
mitochondrial disease
mutation
mitochondrial myopathy
Źródło:
Journal of Applied Genetics; 2001, 42, 3; 351-358
1234-1983
Pojawia się w:
Journal of Applied Genetics
Dostawca treści:
Biblioteka Nauki
Artykuł
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