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Positively charged residues at the N-terminal arm of the homeodomain are required for efficient DNA binding by homeodomain-leucine zipper proteins

Autor: C M, Palena, A E, Tron, C W, Bertoncini, D H, Gonzalez, R L, Chan

Publikováno v: Journal of molecular biology. 308(1)

Plant homeodomain-leucine zipper proteins, unlike most animal homeodomains, bind DNA efficiently only as dimers. In the present work, we report that the deletion of the homeodomain N-terminal arm (first nine residues) of the homeodomain-leucine zippe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::81d4a8a891695ecea72c92e5a47d9c55
https://pubmed.ncbi.nlm.nih.gov/11302705

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A monomer-dimer equilibrium modulates the interaction of the sunflower homeodomain leucine-zipper protein Hahb-4 with DNA

Autor: C M, Palena, D H, Gonzalez, R L, Chan

Publikováno v: The Biochemical journal. 341

We have analysed the interaction of the sunflower homeodomain leucine-zipper (Hd-Zip) protein Hahb-4 with DNA. The complete Hd-Zip domain from Hahb-4 was able to select specific sequences from a random oligonucleotide mixture that contained a 9-bp co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9a6899e40dfed799645d7b502432cc4c
https://pubmed.ncbi.nlm.nih.gov/10377247

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