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
Language
- eng
Conference Location
- United States