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ISSN
1672-9145
Acta Biochim Biophys Sin
2005, 37(3): 181–185
CN 31-1940/Q
Critical Role of Cys168 in Noggin Protein’s Biological Function
Wei-Dong LIU, Xiang-Ling FENG, Cai-Ping REN, Jian-Ling SHI, Xu-Yu
YANG, Ming ZHAO, Liang ZHOU, Ke LAN, and Kai-Tai
YAO*
Cancer Research Institute, Central South University, Changsha
410078, China
Abstract Previous studies have
indicated that noggin exerts its neural inducing effect by binding and antagonizing
bone morphogenetic protein 4 (BMP4). In order to further clarify the
relationship between the structure and the function of noggin, and elucidate
the possible mechanism responsible for noggin-BMP4 interaction, we generated
three noggin mutants, C168S, C174S and C197S, by using a site-directed
mutagenesis method. Ectopic expression of wild-type (WT) noggin, C174S or
C197S, in Xenopus animal caps (ACs) by mRNA injection converted the
explants (prospective ectoderm) into neural tissue, as indicated by the
neural-like morphology and expression of the neural cell adhesion molecule (NCAM)
in the ACs. In contrast, ACs expressing C168S suffered an epidermal fate
similar to the control caps. Similarly, among the three mutants, only C168S
lost the dorsalizing function. These studies highlight the critical role played
by Cys168 in noggin’s biological activities. It probably participates in the
formation of an intermolecular disulfide bridge.
Key words noggin; site-directed
mutagenesis; neural induction; dorsalizing
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Received: November 8, 2004 Accepted: January 17,
2005
This work was supported by a grant from Joint Research Scheme
Project of National Natural Science Foundation of China and the Hong Kong
Research Grants Council (No. 39910161994)
*Corresponding
author: Tel, 86-731-4805451; Fax, 86-731-4360094; E-mail, [email protected]