- Tytuł:
- Sp100 interacts with phage ΦC31 integrase to inhibit its recombination activity
- Autorzy:
-
Lin, Yun
Li, Zhi-Hui
Wang, Jing-Jing
Xu, Gua-Lan
Shen, Qi
Tian, Lin
Xue, Jin-Lun
Chen, Jin-Zhong - Powiązania:
- https://bibliotekanauki.pl/articles/1039951.pdf
- Data publikacji:
- 2011
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
Sp100
ΦC31 integrase
recombination - Opis:
- Phage ΦC31 integrase is a potential vector for the insertion of therapeutic genes into specific sites in the human genome. To understand the mechanism involved in ΦC31 integrase-mediated recombination, it is important to understand the interaction between the integrase and cellular proteins. Using a yeast two-hybrid system with pLexA-ΦC31 integrase as bait, we screened a pB42AD human fetal brain cDNA library for potential interacting cellular proteins. From the 106 independent clones that were screened, 11 potential interacting clones were isolated, of which one encoded C-terminal fragment of Sp100. The interaction between Sp100 and ΦC31 integrase was further confirmed by yeast mating and co-immunoprecipitation assays. The hybridization between a ΦC31 integrase peptide array and an HEK293 cell extract revealed that residues 81RILN84 in the N-terminus of ΦC31 integrase are responsible for the interaction with Sp100. Knocking down endogenous Sp100 with Sp100-specific siRNA increased ΦC31 integrase-mediated recombination but did not impact reporter gene expression. Therefore, endogenous Sp100 may interact with ΦC31 integrase and inhibit the efficiency of ΦC31 integrase-mediated recombination.
- Źródło:
-
Acta Biochimica Polonica; 2011, 58, 1; 67-73
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki