Extreme evolutionary conservation of QM, a novel c-Jun associated transcription factor

Farmer, A. A., Loftus, T. M., Mills, A. A., Sato, K. Y., Neill, J. D., Tron, T., Yang, M., Trumpower, B. L., Stanbridge, E. J. (1994) Extreme evolutionary conservation of QM, a novel c-Jun associated transcription factor. Human Molecular Genetics, 3 (5). pp. 723-728. ISSN 09646906 (ISSN)

URL: http://www.ncbi.nlm.nih.gov/pubmed/8081358
DOI: 10.1093/hmg/3.5.723

Abstract

QM is a 214 amino acid polypeptide, encoded by a gene (DXS648) in Xq28, that contains a high percentage of charged amino acids and has been found to bind c-Jun and DNA. Searches of the GenBank database revealed no matches between QM and any other known transcription factors. However, we and others have isolated QM homologs from a diverse array of eukaryotes. Alignment of these sequences indicated a high degree of conservation throughout the first 175 residues of the protein and revealed several interesting features. Most notable is the considerable conservation of charged amino acids within specific regions of the protein. Secondary structure analysis suggests that two of these regions form amphipathic α-helices, one basic and one acidic. A third conserved charged domain, comprising the N-terminal 30 amino acids, is both basic and proline rich. The rate of sequence divergence of the various homologs was found to be slow (of the order of 1% change every 22 million years), consistent with a critical role for QM in eukaryotic cells. A role for QM as a novel class of transcription regulatory protein is suggested.

Item Type: Paper
Uncontrolled Keywords: proline transcription factor amino acid sequence amino terminal sequence article chromosome Xq genetic conservation human nonhuman priority journal protein secondary structure Animal Chromosome Mapping Comparative Study DNA-Binding Proteins Eukaryotic Cells Evolution Invertebrates Molecular Sequence Data Multigene Family Mutation Phylogeny Plants Protein Structure, Tertiary Proto-Oncogene Proteins c-jun Saccharomyces cerevisiae Sequence Alignment Sequence Homology, Amino Acid Species Specificity Support, Non-U.S. Gov't Support, U.S. Gov't, Non-P.H.S. Support, U.S. Gov't, P.H.S. Transcription Factors Vertebrates X Chromosome Eukaryota
Subjects: diseases & disorders > cancer
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
diseases & disorders
bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function
organism description > animal > mammal > primates > hominids > human
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
CSHL Authors:
Communities: CSHL labs > Mills lab
Depositing User: Matt Covey
Date: 1994
Date Deposited: 11 Mar 2013 20:52
Last Modified: 11 Mar 2013 20:52
Related URLs:
URI: http://repository.cshl.edu/id/eprint/27753

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving