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Wyszukujesz frazę "translation initiation" wg kryterium: Temat


Wyświetlanie 1-2 z 2
Tytuł:
Suppressors of translation initiation defect in hem12 locus of Saccharomyces cerevisiae.
Autorzy:
Góra, Monika
Pluta, Krzysztof
Chełstowska, Anna
Żołądek, Teresa
Powiązania:
https://bibliotekanauki.pl/articles/1044430.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
uroporphyrinogen decarboxylase
eIF2
eIF1
translation initiation
yeast
Opis:
A system for the positive selection of transational initiation suppressors in S. cerevisiae has been developed. A mutant with an ATA initiation codon in the HEM12 gene, encoding uroporphyrinogen decarboxylase, was used to select cis- and trans-acting suppressors. These suppressors partially restore growth on nonfermentable carbon sources, such as glycerol, but still allow the accumulation of porphyrins. All extragenic suppressors are mapped to the SUI1 locus, encoding initiation factor eIF1. The effect of the hem12 mutation is also partially reversed by the known SUI3 suppressor encoding the β subunit of eIF2. In contrast, the sui2 suppressor encoding the α subunit of eIF2 does not affect the hem 12 phenotype. The intragenic suppressors are able to restore the translation of hem12 due to the generation of additional, in frame AUG codons upstream of the hem12-14 mutation. Mutational analysis of the HEM12 leader sequence was also performed to determine the role of small open reading frames (uORFs) present upstream of the HEM12 ORF. Studies on the expression of integrated hem12-1/4-lacZ fusion, devoid of all upstream ATGs, indicate a lack of regulatory effect of uORFs on HEM12 translation.
Źródło:
Acta Biochimica Polonica; 2000, 47, 1; 181-190
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Interaction of three Caenorhabditis elegans isoforms of translation initiation factor eIF4E with mono- and trimethylated mRNA 5 cap analogues.
Autorzy:
Stachelska, Alicja
Wieczorek, Zbigniew
Ruszczyńska, Katarzyna
Stolarski, Ryszard
Pietrzak, Monika
Lamphear, Barry
Rhoads, Robert
Darżynkiewicz, Edward
Jankowska-Anyszka, Marzena
Powiązania:
https://bibliotekanauki.pl/articles/1043732.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
fluorescence quenching
eIF4E
Caenorhabditis elegans
mRNA 5' cap
translation initiation
Opis:
Translation initiation factor eIF4E binds the m7G cap of eukaryotic mRNAs and mediates recruitment of mRNA to the ribosome during cap-dependent translation initiation. This event is the rate-limiting step of translation and a major target for translational control. In the nematode Caenorhabditis elegans, about 70% of genes express mRNAs with an unusual cap structure containing m32,2,7G, which is poorly recognized by mammalian eIF4E. C. elegans expresses five isoforms of eIF4E (IFE-1, IFE-2, etc.). Three of these (IFE-3, IFE-4 and IFE-5) were investigated by means of spectroscopy and structural modelling based on mouse eIF4E bound to m7GDP. Intrinsic fluorescence quenching of Trp residues in the IFEs by iodide ions indicated structural differences between the apo and m7G cap bound proteins. Fluorescence quenching by selected cap analogues showed that only IFE-5 forms specific complexes with both m7G- and m32,2,7G-containing caps (Kas 2×106 M-1 to 7×106 M-1) whereas IFE-3 and IFE-4 discriminated strongly in favor of m7G-containing caps. These spectroscopic results quantitatively confirm earlier qualitative data derived from affinity chromatography. The dependence of Kas on pH indicated optimal cap binding of IFE-3, IFE-4 and IFE-5 at pH 7.2, lower by 0.4 pH units than that of eIF4E from human erythrocytes. These results provide insight into the molecular mechanism of recognition of structurally different caps by the highly homologous IFEs.
Źródło:
Acta Biochimica Polonica; 2002, 49, 3; 671-682
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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