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Wyszukujesz frazę "aminoacyl-tRNA synthetase" wg kryterium: Temat


Wyświetlanie 1-3 z 3
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:
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:
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
    Wyświetlanie 1-3 z 3

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