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THE MOLECULAR-BASIS OF THE UNDULATED PAX-1 MUTATION
Author(s): CHALEPAKIS G, FRITSCH R, FICKENSCHER H, DEUTSCH U, GOULDING M, GRUSS P
Source: CELL    Volume: 66    Issue: 5    Pages: 873-884    Published: SEP 6 1991  
Times Cited: 227     References: 55     
Abstract: The murine paired box gene Pax-1 has been associated with the mouse developmental mutant undulated (un), which exhibits malformations in the vertebral column. In un mice, a point mutation leading to a Gly-Ser exchange in a conserved part of the paired domain of Pax-1 is present. Here we show that Pax-1 encodes a DNA-binding protein with transcriptional activating properties. The DNA-binding specificity of the Pax-1 protein has been extensively analyzed in gel shift assays, and in conjunction with binding interference experiments, a DNA-binding core motif was defined. Comparison of the DNA-binding properties of wild-type and un Pax-1 proteins demonstrates that the Gly-Ser replacement at position 15 within the paired domain dramatically decreases the DNA-binding affinity of the un Pax-1 protein and alters its DNA-binding specificity. These results decipher the molecular basis of the un mutation.
Document Type: Article
Language: English
Reprint Address: CHALEPAKIS, G (reprint author), MAX PLANCK INST BIOPHYS CHEM, DEPT MOLEC CELL BIOL, W-3400 GOTTINGEN, GERMANY
Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: GE460
ISSN: 0092-8674
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