Identification of a minimal functional linker in human topoisomerase I by domain swapping with Cre recombinase

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Identification of a minimal functional linker in human topoisomerase I by domain swapping with Cre recombinase. / Hougaard, Rikke Frøhlich; Juul, Sissel; Vinther, Maria ; Veigaard, Christopher; Hede, Marianne S.; Andersen, Félicie Faucon.

I: Biochemistry, Bind 47, Nr. 27, 2008, s. 7127-7136.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Bibtex

@article{378de2d054cc11dd917a000ea68e967b,

title = "Identification of a minimal functional linker in human topoisomerase I by domain swapping with Cre recombinase",

abstract = "Cellular forms of type IB topoisomerases distinguish themselves from their viral counterparts and the tyrosine recombinases to which they are closely related by having rather extensive N-terminal and linker domains. The functions and necessity of these domains are not yet fully unraveled. In this study we replace 86 amino acids including the linker domain of the cellular type IB topoisomerase, human topoisomerase I, with four, six, or eight amino acids from the corresponding short loop region in Cre recombinase. In vitro characterization of the resulting chimeras, denoted Cropos, reveals that six amino acids from the Cre linker loop constitute the minimal length of a functional linker in human topoisomerase I.",

author = "Hougaard, {Rikke Fr{\o}hlich} and Sissel Juul and Maria Vinther and Christopher Veigaard and Hede, {Marianne S.} and Andersen, {F{\'e}licie Faucon}",

year = "2008",

doi = "10.1021/bi800031k",

language = "English",

volume = "47",

pages = "7127--7136",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "ACS Publications",

number = "27",

}

RIS

TY - JOUR

T1 - Identification of a minimal functional linker in human topoisomerase I by domain swapping with Cre recombinase

AU - Hougaard, Rikke Frøhlich

AU - Juul, Sissel

AU - Vinther, Maria

AU - Veigaard, Christopher

AU - Hede, Marianne S.

AU - Andersen, Félicie Faucon

PY - 2008

Y1 - 2008

N2 - Cellular forms of type IB topoisomerases distinguish themselves from their viral counterparts and the tyrosine recombinases to which they are closely related by having rather extensive N-terminal and linker domains. The functions and necessity of these domains are not yet fully unraveled. In this study we replace 86 amino acids including the linker domain of the cellular type IB topoisomerase, human topoisomerase I, with four, six, or eight amino acids from the corresponding short loop region in Cre recombinase. In vitro characterization of the resulting chimeras, denoted Cropos, reveals that six amino acids from the Cre linker loop constitute the minimal length of a functional linker in human topoisomerase I.

AB - Cellular forms of type IB topoisomerases distinguish themselves from their viral counterparts and the tyrosine recombinases to which they are closely related by having rather extensive N-terminal and linker domains. The functions and necessity of these domains are not yet fully unraveled. In this study we replace 86 amino acids including the linker domain of the cellular type IB topoisomerase, human topoisomerase I, with four, six, or eight amino acids from the corresponding short loop region in Cre recombinase. In vitro characterization of the resulting chimeras, denoted Cropos, reveals that six amino acids from the Cre linker loop constitute the minimal length of a functional linker in human topoisomerase I.

U2 - 10.1021/bi800031k

DO - 10.1021/bi800031k

M3 - Journal article

C2 - 18553933

VL - 47

SP - 7127

EP - 7136

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 27

ER -