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Nucleic Acids Research, 1993, Vol. 21, No. 18 4363-4368
© 1993

MOLECULAR BIOLOGY

A topoisomerase II-like protein is part of an inducible DNA-binding protein complex that binds 5' of an immunoglobulin promoter

Carol F. Webb, Kenton L. Eneff and Fred H. Drake1

Oklahoma Medical Research Foundation, Department of Immunobiology and Cancer Oklahoma City, OK 73104 1SmithKline Beecham Oharmaceuticals, Department of Cellular Biochemistry King of Prussia, PA 19406, USA

Received March 29, 1993. Revised August 6, 1993. Accepted August 6, 1993.

We previously Identified a B cell-specific protein-DNA complex 5' of an Immunoglobulin n heavy chain promoter. The sequences to which this protein complex bound were required for induction of immunoglobulin mRNA levels with interleukln-5 + antigen. Further studies identified a second sequence 5' of these regulatory sequences that bound to both the nuclear matrix and to a similar lnterleukin-5 + antigen inducible protein complex. Therefore, we sought to Identify the putative regulatory proteins that comprised this DNA-blnding complex. In this study, we have used anti-topoisomerase II antibodies to demonstrate that one of the proteins found In the lnterleukin-5 + antigen inducible complexes is serologically related to topoisomerase II. To our knowledge, this Is the first report where a topoisomerase II related protein participates In an inducible mobility shifted protein-DNA complex. These data suggest a model In which the enhanced immunoglobulin gene transcription observed after treatment with Interleukln-5 + antigen might be explained by the Induction of a protein complex that acts to relieve torsional stress along the gene.


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