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Nucleic Acids Research, Vol 26, Issue 5 1160-1166, Copyright © 1998 by Oxford University Press

ARTICLES

cDNA cloning, recombinant expression and characterization of polypetides with exceptional DNA affinity

P Nehls, T Keck, R Greferath, E Spiess, T Glaser, K Rothbarth, H Stammer and D Werner
German Cancer Research Center, Division Biochemistry of the Cell (0225) and Biomedical Ultrastructure Research Unit (0195), D-69120 Heidelberg, Germany.

Polypeptides remaining tightly associated with isolated genomic DNA are of interest with respect to their potential involvement in the topological organization and/or function of genomic DNA. Such residual DNA-polypeptide complexes were used for raising monoclonal antibodies by in vitro immunization. Screening of a murine lambdagt11 cDNA library with these antibodies released a positive cDNA (MC1D) encoding a 16 kDa polypeptide. The cloned homologous human cDNA (HC1D) was identified in the dbest data base by partial sequence comparison, and it was sequenced full length. The cDNA-derived amino acid sequences comprise nuclear location signals but none of the known DNA-binding motifs. However, the recombinantly expressed proteins show in vitro DNA binding affinities. A polyclonal antiserum to the recombinant MC1D protein immunostains sub-nuclear structures, and it detects a residual 16 kDa polypeptide on western blots of DNA digests. These results support the conclusion that the cloned cDNAs reflect mRNAs encoding one of the chemically-resistant polypeptides which can be detected in isolated genomic DNA by sensitive techniques, e.g. by125Iodine labeling and SDS- PAGE.
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