Differential DNA binding properties of three human homeodomain proteins
نویسندگان
چکیده
منابع مشابه
Differential DNA binding properties of three human homeodomain proteins.
The products of three human homeobox containing (HOX) genes, 2C, 3C and 4B, were produced in insect cells using the Baculovirus expression system and purified to near homogeneity. In this system we observed that the DNA binding forms of the three proteins are not glycosylated. HOX 3C and 4B are phosphorylated in insect cells, while HOX 2C is not. The three HOX proteins bind to a DNA sequence kn...
متن کاملRecognition models to predict DNA-binding specificities of homeodomain proteins
MOTIVATION Recognition models for protein-DNA interactions, which allow the prediction of specificity for a DNA-binding domain based only on its sequence or the alteration of specificity through rational design, have long been a goal of computational biology. There has been some progress in constructing useful models, especially for C(2)H(2) zinc finger proteins, but it remains a challenging pr...
متن کاملDNA binding properties of the purified Antennapedia homeodomain.
The in vitro DNA binding properties of a purified 68-amino acid Antennapedia homeodomain (Antp HD) peptide have been analyzed. Equilibrium and kinetic binding studies showed that stable DNA-protein complexes are formed with a Kd of 1.6 x 10(-9) M and 1.8 x 10(-10) M, respectively. Heterodimer analysis led to the conclusion that Antp HD interacts in vitro as a monomer with the DNA target sites u...
متن کاملDNA-binding properties of ARID family proteins
The ARID (A-T Rich Interaction Domain) is a helix-turn-helix motif-based DNA-binding domain, conserved in all eukaryotes and diagnostic of a family that includes 15 distinct human proteins with important roles in development, tissue-specific gene expression and proliferation control. The 15 human ARID family proteins can be divided into seven subfamilies based on the degree of sequence identity...
متن کاملDNA-binding properties of nuclear matrix proteins.
Mouse nuclear matrix proteins, examined by a filter assay, were found to bind to DNA. There was no preference for homologous mouse compared to heterologous E. coli DNA. Competition assays showed a preference for AT-rich DNA and of the 4 single-stranded homopolymers there was a preference for poly(dT). These observations are consistent with the possibility that the matrix may play a role in the ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 1992
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/20.17.4465