Kinetic analysis of Drosophila Vnd protein containing homeodomain with its target sequence

Title
Kinetic analysis of Drosophila Vnd protein containing homeodomain with its target sequence
Author(s)
유시욱
Keywords
SURFACE-PLASMON RESONANCE; VND/NK-2 HOMEODOMAIN; DNA-BINDING; NK-2 HOMEODOMAIN; COMPLEX; GENE; SPECTROSCOPY; SPECIFICITY; MUTATIONS; ACTIVATOR
Issue Date
201006
Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
Citation
BMB REPORTS, v.43, no.6, pp.407 - 412
Abstract
Homeodomain (HD) is a highly conserved DNA-binding domain composed of helix-turn-helix motif. Drosophila Vnd (Ventral nervous system defective) containing HD acts as a regulator to either enhance or suppress gene expression upon binding to its target sequence. In this study, kinetic analysis of Vnd binding to DNA was performed. The result demonstrates that DNA-binding affinity Of the recombinant protein containing HD and NK2-specific domain (NK2-SD) was higher than that of the full-length Vnd. 16 access whether phosphorylation sites within HD and NK2-SD affect the interaction of the protein with the target sequence; alanine substitutions were introduced. The result shows that S631A mutation within NK2-SD does not contribute significantly to the DNA-binding affinity. However, S571A and T600A mutations within HD showed lower affinity for DNA binding. In addition, DNA-binding analysis using embryonic nuclear protein also demonstrates that Vnd interacts with other nuclear proteins, suggesting the existence of Vnd as a complex. [BMB reports 2010; 43(6): 407-412]
URI
http://hdl.handle.net/YU.REPOSITORY/22317http://dx.doi.org/10.5483/BMBRep.2010.43.6.407
ISSN
1976-6696
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교육대학원 > 교육대학원 > Articles
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