TY - JOUR
T1 - Interaction between human topoisomerase I and a novel RING finger/arginine-serine protein
AU - Haluska, Paul
AU - Saleem, Ahamed
AU - Rasheed, Zeshaan
AU - Ahmed, Farheena
AU - Su, Emily W.
AU - Liu, Leroy F.
AU - Rubin, Eric H.
N1 - Funding Information:
We thank Drs Brian Pollack and Sidney Pestka for the Jak1 two-hybrid vector, Drs Steven Ward and Daniel Medina for assistance with fluorescent microscopy and Dr William Hait for reading the manuscript. This work was supported by US Public Health Service grant CA70981, awarded by the National Cancer Institute.
PY - 1999/6/15
Y1 - 1999/6/15
N2 - 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 transcription, possibly recruiting topoisomerase I to RNA polymerase II transcriptional complexes.
AB - 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 transcription, possibly recruiting topoisomerase I to RNA polymerase II transcriptional complexes.
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U2 - 10.1093/nar/27.12.2538
DO - 10.1093/nar/27.12.2538
M3 - Article
C2 - 10352183
AN - SCOPUS:0345298272
SN - 0305-1048
VL - 27
SP - 2538
EP - 2544
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 12
ER -