| First Author | Nehls P | Year | 1998 |
| Journal | Nucleic Acids Res | Volume | 26 |
| Issue | 5 | Pages | 1160-6 |
| PubMed ID | 9469821 | Mgi Jnum | J:46576 |
| Mgi Id | MGI:1201325 | Doi | 10.1093/nar/26.5.1160 |
| Citation | Nehls P, et al. (1998) cDNA cloning, recombinant expression and characterization of polypetides with exceptional DNA affinity. Nucleic Acids Res 26(5):1160-6 |
| abstractText | 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. |
