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Sp100 interacts with phage ΦC31 integrase to inhibit its recombination activity

100%

Lin Y., Li Z.-H., Wang J.-J., Xu G.-L., Shen Q., Tian L., Xue J.-L., Chen J.-Z.

Acta Biochimica Polonica

2011

vol. 58

issue 1

67-73

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.

cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type VI.

81%

Zhang J., Dai J., Zhao E., Lin Y., Zeng L., Chen J., Zheng H., Wang Y., Li X., Ying K., Xie Y., Mao Y.

Acta Biochimica Polonica

2004

vol. 51

issue 4

1051-1058

Peptidylarginine deiminase (PAD) catalyzes the post-translational modification of protein through the conversion of arginine to citrulline in the presence of calcium ions. Human, similar to rodents, has four isoforms of PAD (type I, II, III and IV/V), each of which is distinct in substrate specificity and tissue specific expression. In our large-scale sequencing project, we identified a new human PAD cDNA from a human fetal brain cDNA library. The putative protein encoded by this cDNA is designated hPADVI. Expression analysis of hPADVI showed that it is mainly expressed in adult human ovary and peripheral blood leukocytes. We conclude that hPADVI may be orthologous to mouse ePAD, basing on sequence comparison, chromosome localization and exon-intron structure analysis. PAD-mediated deimination of epithelial cell keratin resulting in cytoskeletal remodeling suggests a possible role for hPADVI in cytoskeletal reorganization in the egg and in early embryo development. This study describes a new important member of the human PAD family.

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2 Acta Biochimica Polonica

1 2011

1 2004

2 Lin Y.

1 Chen J.

1 Chen J.-Z.

1 Dai J.

1 Li X.

1 Li Z.-H.

1 Mao Y.

1 Shen Q.

1 Tian L.

1 Wang J.-J.

1 Wang Y.

1 Xie Y.

1 Xu G.-L.

1 Xue J.-L.

1 Ying K.

1 Zeng L.

1 Zhang J.

1 Zhao E.

1 Zheng H.

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Sp100 interacts with phage ΦC31 integrase to inhibit its recombination activity

cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type VI.