Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures

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

Standard

Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures. / Chatterjee, Sujoy; Zagelbaum, Jennifer; Savitsky, Pavel; Sturzenegger, Andreas; Huttner, Diana; Janscak, Pavel; Hickson, Ian D; Gileadi, Opher; Rothenberg, Eli.

In: Nature Communications, Vol. 5, 5556, 24.11.2014, p. 1-12.

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

Harvard

Chatterjee, S, Zagelbaum, J, Savitsky, P, Sturzenegger, A, Huttner, D, Janscak, P, Hickson, ID, Gileadi, O & Rothenberg, E 2014, 'Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures', Nature Communications, vol. 5, 5556, pp. 1-12. https://doi.org/10.1038/ncomms6556

APA

Chatterjee, S., Zagelbaum, J., Savitsky, P., Sturzenegger, A., Huttner, D., Janscak, P., Hickson, I. D., Gileadi, O., & Rothenberg, E. (2014). Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures. Nature Communications, 5, 1-12. [5556]. https://doi.org/10.1038/ncomms6556

Vancouver

Chatterjee S, Zagelbaum J, Savitsky P, Sturzenegger A, Huttner D, Janscak P et al. Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures. Nature Communications. 2014 Nov 24;5:1-12. 5556. https://doi.org/10.1038/ncomms6556

Author

Chatterjee, Sujoy ; Zagelbaum, Jennifer ; Savitsky, Pavel ; Sturzenegger, Andreas ; Huttner, Diana ; Janscak, Pavel ; Hickson, Ian D ; Gileadi, Opher ; Rothenberg, Eli. / Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures. In: Nature Communications. 2014 ; Vol. 5. pp. 1-12.

Bibtex

@article{0052e292247e46dbaa181bc7b3a05561,
title = "Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures",
abstract = "Bloom syndrome is an autosomal recessive disorder caused by mutations in the RecQ family helicase BLM that is associated with growth retardation and predisposition to cancer. BLM helicase has a high specificity for non-canonical G-quadruplex (G4) DNA structures, which are formed by G-rich DNA strands and play an important role in the maintenance of genomic integrity. Here we used single-molecule FRET to define the mechanism of interaction of BLM helicase with intra-stranded G4 structures. We show that the activity of BLM is substrate dependent, and highly regulated by a short-strand DNA (ssDNA) segment that separates the G4 motif from double-stranded DNA. We demonstrate cooperativity between the RQC and HRDC domains of BLM during binding and unfolding of the G4 structure, where the RQC domain interaction with G4 is stabilized by HRDC binding to ssDNA. We present a model that proposes a unique role for G4 structures in modulating the activity of DNA processing enzymes.",
author = "Sujoy Chatterjee and Jennifer Zagelbaum and Pavel Savitsky and Andreas Sturzenegger and Diana Huttner and Pavel Janscak and Hickson, {Ian D} and Opher Gileadi and Eli Rothenberg",
year = "2014",
month = nov,
day = "24",
doi = "10.1038/ncomms6556",
language = "English",
volume = "5",
pages = "1--12",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures

AU - Chatterjee, Sujoy

AU - Zagelbaum, Jennifer

AU - Savitsky, Pavel

AU - Sturzenegger, Andreas

AU - Huttner, Diana

AU - Janscak, Pavel

AU - Hickson, Ian D

AU - Gileadi, Opher

AU - Rothenberg, Eli

PY - 2014/11/24

Y1 - 2014/11/24

N2 - Bloom syndrome is an autosomal recessive disorder caused by mutations in the RecQ family helicase BLM that is associated with growth retardation and predisposition to cancer. BLM helicase has a high specificity for non-canonical G-quadruplex (G4) DNA structures, which are formed by G-rich DNA strands and play an important role in the maintenance of genomic integrity. Here we used single-molecule FRET to define the mechanism of interaction of BLM helicase with intra-stranded G4 structures. We show that the activity of BLM is substrate dependent, and highly regulated by a short-strand DNA (ssDNA) segment that separates the G4 motif from double-stranded DNA. We demonstrate cooperativity between the RQC and HRDC domains of BLM during binding and unfolding of the G4 structure, where the RQC domain interaction with G4 is stabilized by HRDC binding to ssDNA. We present a model that proposes a unique role for G4 structures in modulating the activity of DNA processing enzymes.

AB - Bloom syndrome is an autosomal recessive disorder caused by mutations in the RecQ family helicase BLM that is associated with growth retardation and predisposition to cancer. BLM helicase has a high specificity for non-canonical G-quadruplex (G4) DNA structures, which are formed by G-rich DNA strands and play an important role in the maintenance of genomic integrity. Here we used single-molecule FRET to define the mechanism of interaction of BLM helicase with intra-stranded G4 structures. We show that the activity of BLM is substrate dependent, and highly regulated by a short-strand DNA (ssDNA) segment that separates the G4 motif from double-stranded DNA. We demonstrate cooperativity between the RQC and HRDC domains of BLM during binding and unfolding of the G4 structure, where the RQC domain interaction with G4 is stabilized by HRDC binding to ssDNA. We present a model that proposes a unique role for G4 structures in modulating the activity of DNA processing enzymes.

U2 - 10.1038/ncomms6556

DO - 10.1038/ncomms6556

M3 - Journal article

C2 - 25418155

VL - 5

SP - 1

EP - 12

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 5556

ER -

ID: 129810223