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Nucleic Acids Research, 1993, Vol. 21, No. 7 1643-1646
© 1993

MOLECULAR BIOLOGY

Isolation and characterization of cDNA clones encoding the Drosophila homolog of the HMG-box SSRP family that recognizes specific DNA structures

Suzanne L. Bruhn*, David E. Housman1 and Stephen J. Lippard

Department of Chemistry, Massachusetts Institute of Technology Cambridge, MA 02139, USA 1Department of Biology, Massachusetts Institute of Technology Cambridge, MA 02139, USA

* To whom correspondence should be addressed at: Harvard Medical School, Department of Genetics, Boston, MA 02115, USA

Received October 1, 1992. Revised February 3, 1993. Accepted February 3, 1993.

Recently an HMG-box protein denoted SSRP1, for structure-specific recognition protein 1, has been discovered which binds to specific DNA structural elements such as the bent, unwound conformations that occur upon the formation of intrastrand crosslinks by the anticancer drug cisplatin. The SSRP family includes the mouse protein T160, which recognizes recombination signal sequences. In order to delineate functional domains more clearly, a homolog of SSRP1 was cloned from Drosophila melanogaster. This homolog maps to polytene region 60A (1–4) and shares 54% identity with human SSRP1. Comparison of the predicted amino acid sequences among SSRP family members reveals 48% identity, with structural conservation in the carboxy terminus of the HMG box as well as domains of highly charged residues, interestingly, however, the most highly conserved regions of the protein are in the less well understood amino terminus, strongly suggesting that this portion of the protein is critical for its function.


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