The phosphoCTD-interacting domain of Topoisomerase I.

Journal Article (Journal Article)

The N-terminal domain (NTD) of Drosophila melanogaster (Dm) Topoisomerase I has been shown to bind to RNA polymerase II, but the domain of RNAPII with which it interacts is not known. Using bacterially-expressed fusion proteins carrying all or half of the NTDs of Dm and human (Homo sapiens, Hs) Topo I, we demonstrate that the N-terminal half of each NTD binds directly to the hyperphosphorylated C-terminal repeat domain (phosphoCTD) of the largest RNAPII subunit, Rpb1. Thus, the amino terminal segment of metazoan Topo I (1-157 for Dm and 1-114 for Hs) contains a novel phosphoCTD-interacting domain that we designate the Topo I-Rpb1 interacting (TRI) domain. The long-known in vivo association of Topo I with active genes presumably can be attributed, wholly or in part, to the TRI domain-mediated binding of Topo I to the phosphoCTD of transcribing RNAPII.

Full Text

Duke Authors

Cited Authors

  • Wu, J; Phatnani, HP; Hsieh, T-S; Greenleaf, AL

Published Date

  • June 18, 2010

Published In

Volume / Issue

  • 397 / 1

Start / End Page

  • 117 - 119

PubMed ID

  • 20493173

Pubmed Central ID

  • PMC2900466

Electronic International Standard Serial Number (EISSN)

  • 1090-2104

Digital Object Identifier (DOI)

  • 10.1016/j.bbrc.2010.05.081


  • eng

Conference Location

  • United States