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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 [PDF]

open access: yesJournal of Molecular Biology, 2001
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 zipper ...
Carlos W. Bertoncini   +2 more
exaly   +2 more sources
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Purification of the proline-rich homeodomain protein

Journal of Chromatography B, 2003
The proline-rich homeodomain protein (PRH), also known as Hex, is a transcriptional repressor expressed in a variety of cell types. The PRH protein contains a proline-rich N-terminal domain that can repress transcription when attached to a heterologous DNA binding domain, a central homeodomain that mediates sequence-specific DNA binding, and an acidic ...
Butcher, AJ, Gaston, K, Jayaraman, P-S
openaire   +2 more sources

Target genes of homeodomain proteins

BioEssays, 1999
Homeodomain proteins are transcription factors that share a related DNA binding domain, the homeodomain. This class of proteins was first recognized in the fruitfly Drosophila melanogaster where they cause homeotic transformations such as a fly with four wings instead of two (Lewis EB. A gene complex controlling segmentation in Drosophila.
openaire   +2 more sources

LIM homeodomain proteins and associated partners: Then and now

2021
The field of molecular embryology started around 1990 by identifying new genes and analyzing their functions in early vertebrate embryogenesis. Those genes encode transcription factors, signaling molecules, their regulators, etc. Most of those genes are relatively highly expressed in specific regions or exhibit dramatic phenotypes when ectopically ...
Yuuri, Yasuoka, Masanori, Taira
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Homeodomain Proteins

1998
Abstract As described in Chapter 3, homeodomain proteins are transcription factors that are characterized by the presence of a 60-amino-acid DNA binding domain. The structure of the homeodomain consists of a flexible amino-terminal arm followed by three a helices (Fig.
openaire   +1 more source

DNA Wrapping and Distortion by an Oligomeric Homeodomain Protein

Journal of Molecular Biology, 2008
Many transcription factors alter DNA or chromatin structure. Changes in chromatin structure are often brought about by the recruitment of chromatin-binding proteins, chromatin-modifying proteins, or other transcription co-activator or co-repressor proteins.
Williams, H, Jayaraman, P-S, Gaston, K
openaire   +3 more sources

A Role for the HOXB7 Homeodomain Protein in DNA Repair

Cancer Research, 2007
Abstract Homeobox genes encode transcription factors which function in body axis patterning in the developing embryo. Recent evidence suggests that the maintenance of specific HOX expression patterns is necessary for regulating the homeostasis of adult tissues as well.
Ethel, Rubin   +12 more
openaire   +2 more sources

Expression of homeodomain protein CDX2 in gallbladder carcinomas

Journal of Cancer Research and Clinical Oncology, 2005
Caudal-related homeobox protein CDX2 plays an important role in the regulation of cell proliferation and differentiation of the intestinal epithelium. CDX2 is associated with intestinal metaplasia and carcinomas of the stomach, but the role of CDX2 in gallbladder carcinogenesis remains unknown.We analyzed the expression of CDX2 and intestinal apomucin ...
Xiang-Song, Wu   +9 more
openaire   +2 more sources

Identification of the Transactivating Region of the Homeodomain Protein, Hex

Journal of Biochemistry, 2004
The homeodomain-containing protein Hex acts as an activator as well as a repressor of transcription in animals. While its repression domain has been mapped to the amino-terminal region, the activation domain has never been identified. Here, we show that the homeodomain and the acidic carboxyl-terminal region are necessary for full activation of the ...
Shinya, Kasamatsu   +8 more
openaire   +2 more sources

Homeodomain Proteins in Pancreas Development

2001
The pancreas derives from the upper, duodenal part of the foregut via a dorsal and ventral protrusion of the epithelium directly posterior to the developing stomach, and in the mouse, the early pancreatic buds become evident on embryonic day 9 (e9) (Figure 1). The part of the gut from which the pancreas originates becomes committed to a pancreatic fate
Ulf Ahlgren, Helena Edlund
openaire   +1 more source

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