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Interaction between human topoisomerase I and a novel RING finger/arginine-serine protein.

ABSTRACT: The N-terminus of human topoisomerase I participates in the binding of this enzyme to helicases and other proteins. Using the N-terminal 250 amino acids of human topoisomerase I and a yeast two-hybrid/ in vitro binding screen, a novel arginine-serine-rich peptide was identified as a human topoisomerase I-binding protein. The corresponding full-length protein, named topors, contains a consensus RING zinc finger domain and nuclear localization signals in addition to the arginine-serine-rich region. The RING finger domain of topors is homologous to a similar domain in a family of viral proteins that are involved in the regulation of viral transcription. When expressed in HeLa cells as a green fluorescent protein fusion, topors localizes in the nucleus in a punctate pattern and co-immunoprecipitates with topoisomerase I. These data suggest that topors is involved in trans-cription, possibly recruiting topoisomerase I to RNA polymerase II transcriptional complexes.

SUBMITTER: Haluska P

PROVIDER: S-EPMC148458 | biostudies-other | 1999 Jun

REPOSITORIES: biostudies-other

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Interaction between human topoisomerase I and a novel RING finger/arginine-serine protein.

Haluska P P Saleem A A Rasheed Z Z Ahmed F F Su E W EW Liu L F LF Rubin E H EH

Nucleic acids research 19990601 12

The N-terminus of human topoisomerase I participates in the binding of this enzyme to helicases and other proteins. Using the N-terminal 250 amino acids of human topoisomerase I and a yeast two-hybrid/ in vitro binding screen, a novel arginine-serine-rich peptide was identified as a human topoisomerase I-binding protein. The corresponding full-length protein, named topors, contains a consensus RING zinc finger domain and nuclear localization signals in addition to the arginine-serine-rich region ...[more]

PMID: 10352183

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