Mutation in the FGFR2 gene in a Taiwanese patient with Beare-Stevenson cutis gyrata syndrome

CMUR > China Medical University Hospital > Jurnal articles > Item 310903500/30522

Please use this identifier to cite or link to this item: http://ir.cmu.edu.tw/ir/handle/310903500/30522

Title:	Mutation in the FGFR2 gene in a Taiwanese patient with Beare-Stevenson cutis gyrata syndrome
Authors:	Wang, TJ;Huang, CB;Tsai, FJ;Wu, JY;Lai, RB;Hsiao, M
Contributors:	附設醫院醫研部;Kaohsiung Chang Gung Mem Hosp, Dept Paediat, Niao Sung Hsiang, Kaohsiung Hsien, Taiwan;China Med Coll Hosp, Dept Paediat, Taichung, Taiwan;China Med Coll Hosp, Dept Med Res, Taichung, Taiwan;Kaohsiung Chang Gung Mem Hosp, Dept Plast Surg, Kaohsiung, Taiwan;Kaohsiung Vet Gen Hosp, Dept Med Educ & Res, Kaohsiung, Taiwan
Date:	2002
Issue Date:	2010-09-24 14:56:58 (UTC+8)
Publisher:	BLACKWELL MUNKSGAARD
Abstract:	The pseudorabies virus (PRV) DNase is an alkaline exonuclease and endonuclease, which exhibits an Escherichia coli RecBCD-like catalytic function. The PRV DNA-binding protein (DBP) promotes the renaturation of complementary single strands of DNA, which is an essential function for recombinase. To investigate the functional and physical interactions between PRV DBP and DNase, these proteins were purified to homogeneity. PRV DBP stimulated the DNase activity, especially the exonuclease activity, in a dose-dependent fashion. Acetylation of DBP by acetic anhydride resulted in a loss of DNA-binding ability and a 60% inhibition of the DNase activity, suggesting that DNA-binding ability of PRV DBP was required for stimulating the DNase activity. PRV DNase behaved in a processive mode; however, it was converted into a distributive mode in the presence of DBP, implying that PRV DBP stimulated the dissociation of DNase from DNA substrates. The physical interaction between DBP and DNase was further analyzed by enzyme-linked immunosorbent assay, and a significant interaction was observed. Thus, these results suggested that PRV DBP interacted with PRV DNase and regulated the DNase activity in vitro. (C) 2002 Elsevier Science (USA). All rights reserved.
Relation:	CLINICAL GENETICS 61(3):218-221
Appears in Collections:	[China Medical University Hospital] Jurnal articles

Files in This Item:

There are no files associated with this item.

Loading...