Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2

Research output: Contribution to journalJournal articleResearchpeer-review

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Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2. / Kenchappa, Chandra; Heiðarsson, Pétur Orri; Kragelund, Birthe; Garrett, Roger; Poulsen, Flemming.

In: Nucleic Acids Research, Vol. 41, No. 5, 2013, p. 3424-3435.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Kenchappa, C, Heiðarsson, PO, Kragelund, B, Garrett, R & Poulsen, F 2013, 'Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2' Nucleic Acids Research, vol. 41, no. 5, pp. 3424-3435. https://doi.org/10.1093/nar/gks1465

APA

Kenchappa, C., Heiðarsson, P. O., Kragelund, B., Garrett, R., & Poulsen, F. (2013). Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2. Nucleic Acids Research, 41(5), 3424-3435. https://doi.org/10.1093/nar/gks1465

Vancouver

Kenchappa C, Heiðarsson PO, Kragelund B, Garrett R, Poulsen F. Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2. Nucleic Acids Research. 2013;41(5):3424-3435. https://doi.org/10.1093/nar/gks1465

Author

Kenchappa, Chandra ; Heiðarsson, Pétur Orri ; Kragelund, Birthe ; Garrett, Roger ; Poulsen, Flemming. / Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2. In: Nucleic Acids Research. 2013 ; Vol. 41, No. 5. pp. 3424-3435.

Bibtex

@article{47b19ef410694ab0913d90b5fd5cd69e,
title = "Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2",
abstract = "Clustered regularly interspaced short palindromic repeats (CRISPR) form the basis of diverse adaptive immune systems directed primarily against invading genetic elements of archaea and bacteria. Cbp1 of the crenarchaeal thermoacidophilic order Sulfolobales, carrying three imperfect repeats, binds specifically to CRISPR DNA repeats and has been implicated in facilitating production of long transcripts from CRISPR loci. Here, a second related class of CRISPR DNA repeat-binding protein, denoted Cbp2, is characterized that contains two imperfect repeats and is found amongst members of the crenarchaeal thermoneutrophilic order Desulfurococcales. DNA repeat-binding properties of the Hyperthermus butylicus protein Cbp2(Hb) were characterized and its three-dimensional structure was determined by NMR spectroscopy. The two repeats generate helix-turn-helix structures separated by a basic linker that is implicated in facilitating high affinity DNA binding of Cbp2 by tethering the two domains. Structural studies on mutant proteins provide support for Cys(7) and Cys(28) enhancing high thermal stability of Cbp2(Hb) through disulphide bridge formation. Consistent with their proposed CRISPR transcriptional regulatory role, Cbp2(Hb) and, by inference, other Cbp1 and Cbp2 proteins are closely related in structure to homeodomain proteins with linked helix-turn-helix (HTH) domains, in particular the paired domain Pax and Myb family proteins that are involved in eukaryal transcriptional regulation.",
author = "Chandra Kenchappa and Hei{\dh}arsson, {P{\'e}tur Orri} and Birthe Kragelund and Roger Garrett and Flemming Poulsen",
year = "2013",
doi = "10.1093/nar/gks1465",
language = "English",
volume = "41",
pages = "3424--3435",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "5",

}

RIS

TY - JOUR

T1 - Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2

AU - Kenchappa, Chandra

AU - Heiðarsson, Pétur Orri

AU - Kragelund, Birthe

AU - Garrett, Roger

AU - Poulsen, Flemming

PY - 2013

Y1 - 2013

N2 - Clustered regularly interspaced short palindromic repeats (CRISPR) form the basis of diverse adaptive immune systems directed primarily against invading genetic elements of archaea and bacteria. Cbp1 of the crenarchaeal thermoacidophilic order Sulfolobales, carrying three imperfect repeats, binds specifically to CRISPR DNA repeats and has been implicated in facilitating production of long transcripts from CRISPR loci. Here, a second related class of CRISPR DNA repeat-binding protein, denoted Cbp2, is characterized that contains two imperfect repeats and is found amongst members of the crenarchaeal thermoneutrophilic order Desulfurococcales. DNA repeat-binding properties of the Hyperthermus butylicus protein Cbp2(Hb) were characterized and its three-dimensional structure was determined by NMR spectroscopy. The two repeats generate helix-turn-helix structures separated by a basic linker that is implicated in facilitating high affinity DNA binding of Cbp2 by tethering the two domains. Structural studies on mutant proteins provide support for Cys(7) and Cys(28) enhancing high thermal stability of Cbp2(Hb) through disulphide bridge formation. Consistent with their proposed CRISPR transcriptional regulatory role, Cbp2(Hb) and, by inference, other Cbp1 and Cbp2 proteins are closely related in structure to homeodomain proteins with linked helix-turn-helix (HTH) domains, in particular the paired domain Pax and Myb family proteins that are involved in eukaryal transcriptional regulation.

AB - Clustered regularly interspaced short palindromic repeats (CRISPR) form the basis of diverse adaptive immune systems directed primarily against invading genetic elements of archaea and bacteria. Cbp1 of the crenarchaeal thermoacidophilic order Sulfolobales, carrying three imperfect repeats, binds specifically to CRISPR DNA repeats and has been implicated in facilitating production of long transcripts from CRISPR loci. Here, a second related class of CRISPR DNA repeat-binding protein, denoted Cbp2, is characterized that contains two imperfect repeats and is found amongst members of the crenarchaeal thermoneutrophilic order Desulfurococcales. DNA repeat-binding properties of the Hyperthermus butylicus protein Cbp2(Hb) were characterized and its three-dimensional structure was determined by NMR spectroscopy. The two repeats generate helix-turn-helix structures separated by a basic linker that is implicated in facilitating high affinity DNA binding of Cbp2 by tethering the two domains. Structural studies on mutant proteins provide support for Cys(7) and Cys(28) enhancing high thermal stability of Cbp2(Hb) through disulphide bridge formation. Consistent with their proposed CRISPR transcriptional regulatory role, Cbp2(Hb) and, by inference, other Cbp1 and Cbp2 proteins are closely related in structure to homeodomain proteins with linked helix-turn-helix (HTH) domains, in particular the paired domain Pax and Myb family proteins that are involved in eukaryal transcriptional regulation.

U2 - 10.1093/nar/gks1465

DO - 10.1093/nar/gks1465

M3 - Journal article

VL - 41

SP - 3424

EP - 3435

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 5

ER -

ID: 44022715