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PMID: 1497674 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

A homology domain shared between Drosophila optomotor-blind and mouse Brachyury is involved in DNA binding.

Biochemical and biophysical research communications ·Vol. 186 ·No. 2 ·1992-07-31 ·Pages 918-25

Pflugfelder GO, Roth H, Poeck B

Abstract

The distribution of sequence elements divides the optomotor-blind protein into three regions and is suggestive of a transcriptional regulatory role of this protein. The central region of Omb is homologous to the N-terminal half of the Brachyury protein. The conserved domain of Omb is here shown to possess general DNA binding affinity but has no significant similarity to recognized DNA binding motifs.

MeSH Terms
Amino Acid Sequence Animals Cloning, Molecular DNA/genetics,isolation & purification DNA-Binding Proteins/genetics Drosophila/genetics Drosophila Proteins Fetal Proteins/genetics Mice Molecular Sequence Data Nerve Tissue Proteins/genetics Sequence Homology, Nucleic Acid T-Box Domain Proteins
Chemicals
DNA-Binding Proteins Drosophila Proteins Fetal Proteins Nerve Tissue Proteins T-Box Domain Proteins bi protein, Drosophila DNA Brachyury protein
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Pflugfelder G O
Theodor-Boveri-Institut, Lehrstuhl für Genetik, Würzburg, Germany.
Roth H
Poeck B
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1992-07-31
Pages
918-25
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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