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

• Published in: Nucleic acids research Vol. 21; no. 18; pp. 4363 - 4368
• Main Authors: Webb, Carol F., Eneff, Kenton L., Drake, Fred H.
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 11-09-1993
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Antibodies - immunology; Antibody Specificity; Antigens - immunology; B-Lymphocytes - metabolism; Binding and carrier proteins; Biological and medical sciences; Cell Line; DNA Topoisomerases, Type II - metabolism; DNA-Binding Proteins - metabolism; Fundamental and applied biological sciences. Psychology; Immunoglobulin mu-Chains - genetics; Interleukin-5 - pharmacology; Molecular Sequence Data; Promoter Regions, Genetic; Proteins; RNA, Messenger - metabolism; Topoisomerase II Inhibitors; DNA topoisomerase (ATP-hydrolysing); Immunoglobulins; Interleukin 5; Enzyme; Transcription promoter; Analog; heavy-Peptide chain; Variable region; Cytokine; DNA binding protein; Molecular interaction; B-Lymphocyte
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/21.18.4363

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.