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Wyszukujesz frazę "mismatch repair" wg kryterium: Temat


Wyświetlanie 1-3 z 3
Tytuł:
Transformation of wild Solanum species resistant to late blight by using reporter gene gfp and msh2 genes
Autorzy:
Rakosy-Tican, Lenuta
Aurori, Adriana
Aurori, Cristian M.
Ispas, Gabriela
Famelaer, Ivan
Powiązania:
https://bibliotekanauki.pl/articles/2198986.pdf
Data publikacji:
2004-12-20
Wydawca:
Instytut Hodowli i Aklimatyzacji Roślin
Tematy:
Agrobacterium tumefaciens mediated transformation
DNA mismatch repair
gfp
nptII marker gene
Opis:
Green fluorescent protein (gfp) reporter gene and nptII marker gene were used to optimize Agrobacterium tumefaciens (agro) mediated transformation of wild Solanum genotypes resistant to late blight. Different genotypes of Solanum bulbocastanum, S. chacoense, S. microdontum and S. verrucosum were assessed for their regeneration ability on MS based media and for agro-mediated transformation. As the first step reporter genes were used to optimize transformation protocol for each species and then the transfer of genes involved in mismatch repair of DNA were attempted in Solanum chacoense. For transformation, either leaf or stem fragments were used. It was shown that gfp is a valuable and elegant tool for monitoring the efficiency of transformation or the occurrence of chimera in all genotypes. Transformation efficiency was dependent on a plant genotype. A number of genotypes have been successfully transformed and they expressed constitutively the bright green fluorescence of gfp without any side effects. The most recalcitrant species proved to be S. microdontum, which did not regenerate plants although different media and phytohormones had been used. The best protocol for S. chacoense transformation was also found to work in the transfer of msh2 genes. Msh2 isolated from Arabidopsis was used and transferred either as mutated (Apa) or antisense (As) gene. The integration of msh2-mutated gene into S. chacoense genome was demonstrated by PCR amplification and confirmed by RT-PCR for some of the putative transgenic clones. The implications of mismatch repair in homologous recombination and its importance for potato improvement are discussed. 
Źródło:
Plant Breeding and Seed Science; 2004, 50; 119-127
1429-3862
2083-599X
Pojawia się w:
Plant Breeding and Seed Science
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Bacterial DNA repair genes and their eukaryotic homologues: 2. Role of bacterial mutator gene homologues in human disease. Overview of nucleotide pool sanitization and mismatch repair systems
Autorzy:
Arczewska, Katarzyna
Kuśmierek, Jarosław
Powiązania:
https://bibliotekanauki.pl/articles/1040920.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
MutT protein
human MutT homologue
DNA damage
mismatch repair
hereditary non-polyposis colorectal cancer
DNA repair
Opis:
Since the discovery of the first E. coli mutator gene, mutT, most of the mutations inducing elevated spontaneous mutation rates could be clearly attributed to defects in DNA repair. MutT turned out to be a pyrophosphohydrolase hydrolyzing 8-oxodGTP, thus preventing its incorporation into DNA and suppresing the occurrence of spontaneous AT→CG transversions. Most of the bacterial mutator genes appeared to be evolutionarily conserved, and scientists were continuously searching for contribution of DNA repair deficiency in human diseases, especially carcinogenesis. Yet a human MutT homologue - hMTH1 protein - was found to be overexpressed rather than inactivated in many human diseases, including cancer. The interest in DNA repair contribution to human diseases exploded with the observation that germline mutations in mismatch repair (MMR) genes predispose to hereditary non-polyposis colorectal cancer (HNPCC). Despite our continuously growing knowledge about DNA repair we still do not fully understand how the mutator phenotype contributes to specific forms of human diseases.
Źródło:
Acta Biochimica Polonica; 2007, 54, 3; 435-457
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Mismatch dependent uracil/thymine-DNA glycosylases excise exocyclic hydroxyethano and hydroxypropano cytosine adducts.
Autorzy:
Borys-Brzywczy, Ewa
Arczewska, Katarzyna
Saparbaev, Murat
Hardeland, Ulrike
Schär, Primo
Kuśmierek, Jarosław
Powiązania:
https://bibliotekanauki.pl/articles/1041473.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
base excision repair
E. coli mismatch uracil-DNA glycosylase
exocyclic cytosine adducts
human thymine-DNA glycosylase
S. pombe Thp1p glycosylase
Opis:
Exocyclic adducts of DNA bases, such as etheno- and hydroxyalkano- ones, are generated by a variety of bifunctional agents, including endogenously formed products of lipid peroxidation. In this work we selectively modified cytosines in the 5'-d(TTT TTT CTT TTT CTT TTT CTT TTT T)-3' oligonucleotide using: chloroacetaldehyde to obtain 3,N4-α-hydroxyethano- (HEC) and 3,N4-etheno- (εC), acrolein to obtain 3,N4-α-hydroxypropano- (HPC) and crotonaldehyde to obtain 3,N4-α-hydroxy-γ-methylpropano- (mHPC) adducts of cytosine. The studied adducts are alkali-labile which results in oligonucleotide strain breaks at the sites of modification upon strong base treatment. The oligonucleotides carrying adducted cytosines were studied as substrates of Escherichia coli Mug, human TDG and fission yeast Thp1p glycosylases. All the adducts studied are excised by bacterial Mug although with various efficiency: εC >HEC >HPC >mHPC. The yeast enzyme excises efficiently εC ł HEC >HPC, whereas the human enzyme excises only εC. The pH-dependence curves of excision of εC, HEC and HPC by Mug are bell shaped and the most efficient excision of adducts occurs within the pH range of 8.6-9.6. The observed increase of excision of HEC and HPC above pH 7.2 can be explained by deprotonation of these adducts, which are high pKa compounds and exist in a protonated form at neutrality. On the other hand, since εC is in a neutral form in the pH range studied, we postulate an involvement of an additional catalytic factor. We hypothesize that the enzyme structure undergoes a pH-induced rearrangement allowing the participation of Lys68 of Mug in catalysis via a hydrogen bond interaction of its ε-amino group with N4 of the cytosine exocyclic adducts.
Źródło:
Acta Biochimica Polonica; 2005, 52, 1; 149-165
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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