BLM and RMI1 Alleviate RPA Inhibition of TopoIIIa Decatenase Activity

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BLM and RMI1 Alleviate RPA Inhibition of TopoIIIa Decatenase Activity. / Yang, Jay; Bachrati, Csanad Z; Hickson, Ian D; Brown, Grant W.

In: P L o S One, Vol. 7, No. 7, 07.2012, p. e41208.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Yang, J, Bachrati, CZ, Hickson, ID & Brown, GW 2012, 'BLM and RMI1 Alleviate RPA Inhibition of TopoIIIa Decatenase Activity', P L o S One, vol. 7, no. 7, pp. e41208. https://doi.org/10.1371/journal.pone.0041208

APA

Yang, J., Bachrati, C. Z., Hickson, I. D., & Brown, G. W. (2012). BLM and RMI1 Alleviate RPA Inhibition of TopoIIIa Decatenase Activity. P L o S One, 7(7), e41208. https://doi.org/10.1371/journal.pone.0041208

Vancouver

Yang J, Bachrati CZ, Hickson ID, Brown GW. BLM and RMI1 Alleviate RPA Inhibition of TopoIIIa Decatenase Activity. P L o S One. 2012 Jul;7(7):e41208. https://doi.org/10.1371/journal.pone.0041208

Author

Yang, Jay ; Bachrati, Csanad Z ; Hickson, Ian D ; Brown, Grant W. / BLM and RMI1 Alleviate RPA Inhibition of TopoIIIa Decatenase Activity. In: P L o S One. 2012 ; Vol. 7, No. 7. pp. e41208.

Bibtex

@article{1e5241b05b244e8ba96d9161f9dd68f4,
title = "BLM and RMI1 Alleviate RPA Inhibition of TopoIIIa Decatenase Activity",
abstract = "RPA is a single-stranded DNA binding protein that physically associates with the BLM complex. RPA stimulates BLM helicase activity as well as the double Holliday junction dissolution activity of the BLM-topoisomerase IIIa complex. We investigated the effect of RPA on the ssDNA decatenase activity of topoisomerase IIIa. We found that RPA and other ssDNA binding proteins inhibit decatenation by topoisomerase IIIa. Complex formation between BLM, TopoIIIa, and RMI1 ablates inhibition of decatenation by ssDNA binding proteins. Together, these data indicate that inhibition by RPA does not involve species-specific interactions between RPA and BLM-TopoIIIa-RMI1, which contrasts with RPA modulation of double Holliday junction dissolution. We propose that topoisomerase IIIa and RPA compete to bind to single-stranded regions of catenanes. Interactions with BLM and RMI1 enhance toposiomerase IIIa activity, promoting decatenation in the presence of RPA.",
author = "Jay Yang and Bachrati, {Csanad Z} and Hickson, {Ian D} and Brown, {Grant W}",
year = "2012",
month = jul,
doi = "10.1371/journal.pone.0041208",
language = "English",
volume = "7",
pages = "e41208",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "7",

}

RIS

TY - JOUR

T1 - BLM and RMI1 Alleviate RPA Inhibition of TopoIIIa Decatenase Activity

AU - Yang, Jay

AU - Bachrati, Csanad Z

AU - Hickson, Ian D

AU - Brown, Grant W

PY - 2012/7

Y1 - 2012/7

N2 - RPA is a single-stranded DNA binding protein that physically associates with the BLM complex. RPA stimulates BLM helicase activity as well as the double Holliday junction dissolution activity of the BLM-topoisomerase IIIa complex. We investigated the effect of RPA on the ssDNA decatenase activity of topoisomerase IIIa. We found that RPA and other ssDNA binding proteins inhibit decatenation by topoisomerase IIIa. Complex formation between BLM, TopoIIIa, and RMI1 ablates inhibition of decatenation by ssDNA binding proteins. Together, these data indicate that inhibition by RPA does not involve species-specific interactions between RPA and BLM-TopoIIIa-RMI1, which contrasts with RPA modulation of double Holliday junction dissolution. We propose that topoisomerase IIIa and RPA compete to bind to single-stranded regions of catenanes. Interactions with BLM and RMI1 enhance toposiomerase IIIa activity, promoting decatenation in the presence of RPA.

AB - RPA is a single-stranded DNA binding protein that physically associates with the BLM complex. RPA stimulates BLM helicase activity as well as the double Holliday junction dissolution activity of the BLM-topoisomerase IIIa complex. We investigated the effect of RPA on the ssDNA decatenase activity of topoisomerase IIIa. We found that RPA and other ssDNA binding proteins inhibit decatenation by topoisomerase IIIa. Complex formation between BLM, TopoIIIa, and RMI1 ablates inhibition of decatenation by ssDNA binding proteins. Together, these data indicate that inhibition by RPA does not involve species-specific interactions between RPA and BLM-TopoIIIa-RMI1, which contrasts with RPA modulation of double Holliday junction dissolution. We propose that topoisomerase IIIa and RPA compete to bind to single-stranded regions of catenanes. Interactions with BLM and RMI1 enhance toposiomerase IIIa activity, promoting decatenation in the presence of RPA.

U2 - 10.1371/journal.pone.0041208

DO - 10.1371/journal.pone.0041208

M3 - Journal article

C2 - 22911760

VL - 7

SP - e41208

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 7

ER -

ID: 40802314