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© 1994 Oxford University Press

OTHER

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

Andrew A. Farmer, Thomas M. Loftus, Alea A. Mills, Kevin Y. Sato, John D. Neill{dagger}, Thierry Tron2, Meijia Yang2, Bernard L. Trumpower2 and Eric J. Stanbridge*

Department of Mcrobiology and Molecular Genetics, University of Califomia lrvine, College of Medicine lrvine, CA 92715 1Pioneer Hi-Bred International, Inc. Department of Biotechnology Research, Johnston, IA 50131 2Department of Biochemistry, Dartmouth Medical School Hanover, NH 03755, USA

*To whom correspondence should be addressed

Received December 7, 1993; Accepted March 9, 1994

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 amphlpathlc a-hellces, one basic and one acidic. A third conserved charged domain, comprising the N-termlnal 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 eukaryotlc cells. A role for as a novel class of transcription regulatory protein is suggested.

{dagger}Present address: United States Deparment of Agriculture, National Animal Disease Center, 2300 Dayton Avenue, PO Box 70, Ames, JA 50010, USA


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