Activity of coliphage HK022 excisionase (Xis) in the absence of DNA binding

Pnina Gottfried; Nava Silberstein; Ezra Yagil; Mikhail Kolot

doi:10.1016/S0014-5793(03)00512-X

Activity of coliphage HK022 excisionase (Xis) in the absence of DNA binding

Pnina Gottfried, Nava Silberstein, Ezra Yagil, Mikhail Kolot^*

^*Corresponding author for this work

Biochemistry Molecular Biology

Research output: Contribution to journal › Article › peer-review

Abstract

A mutated excisionase (Xis) protein of coliphage HK022 whose single Cys residue was replaced by Ser does not bind to its two tandem binding sites (X1, X2) on the P arm of attR. Despite its DNA-binding inability the protein showed 30% excision activity of the wild type Xis both in vitro and in vivo. This partial activity is attributed to the interaction of Xis with integrase that is retained in the mutant protein. This protein-protein interaction occurs in the absence of DNA binding.

Original language	English
Pages (from-to)	133-138
Number of pages	6
Journal	FEBS Letters
Volume	545
Issue number	2-3
DOIs	https://doi.org/10.1016/S0014-5793(03)00512-X
State	Published - 19 Jun 2003

Keywords

Bacteriophage HK022
DNA-protein interaction
Excisionase
Fluorescence resonance energy transfer
Protein-protein interaction
Site-specific recombination

Access to Document

10.1016/S0014-5793(03)00512-X

Cite this

@article{afaa7c2db7934a46a45a2e8ff68dbf29,

title = "Activity of coliphage HK022 excisionase (Xis) in the absence of DNA binding",

abstract = "A mutated excisionase (Xis) protein of coliphage HK022 whose single Cys residue was replaced by Ser does not bind to its two tandem binding sites (X1, X2) on the P arm of attR. Despite its DNA-binding inability the protein showed 30% excision activity of the wild type Xis both in vitro and in vivo. This partial activity is attributed to the interaction of Xis with integrase that is retained in the mutant protein. This protein-protein interaction occurs in the absence of DNA binding.",

keywords = "Bacteriophage HK022, DNA-protein interaction, Excisionase, Fluorescence resonance energy transfer, Protein-protein interaction, Site-specific recombination",

author = "Pnina Gottfried and Nava Silberstein and Ezra Yagil and Mikhail Kolot",

note = "Funding Information: Ehud Gazit and two anonymous reviewers improved the manuscript, Carol Robertson and Howard Nash gave us IHF and Reid Johnson sent us the fis mutant. The Israel Science Foundation founded by the Academy of Sciences and Humanities supported this work (Grant 637/02).",

year = "2003",

month = jun,

day = "19",

doi = "10.1016/S0014-5793(03)00512-X",

language = "אנגלית",

volume = "545",

pages = "133--138",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Wiley-Blackwell",

number = "2-3",

}

TY - JOUR

T1 - Activity of coliphage HK022 excisionase (Xis) in the absence of DNA binding

AU - Gottfried, Pnina

AU - Silberstein, Nava

AU - Yagil, Ezra

AU - Kolot, Mikhail

N1 - Funding Information: Ehud Gazit and two anonymous reviewers improved the manuscript, Carol Robertson and Howard Nash gave us IHF and Reid Johnson sent us the fis mutant. The Israel Science Foundation founded by the Academy of Sciences and Humanities supported this work (Grant 637/02).

PY - 2003/6/19

Y1 - 2003/6/19

N2 - A mutated excisionase (Xis) protein of coliphage HK022 whose single Cys residue was replaced by Ser does not bind to its two tandem binding sites (X1, X2) on the P arm of attR. Despite its DNA-binding inability the protein showed 30% excision activity of the wild type Xis both in vitro and in vivo. This partial activity is attributed to the interaction of Xis with integrase that is retained in the mutant protein. This protein-protein interaction occurs in the absence of DNA binding.

AB - A mutated excisionase (Xis) protein of coliphage HK022 whose single Cys residue was replaced by Ser does not bind to its two tandem binding sites (X1, X2) on the P arm of attR. Despite its DNA-binding inability the protein showed 30% excision activity of the wild type Xis both in vitro and in vivo. This partial activity is attributed to the interaction of Xis with integrase that is retained in the mutant protein. This protein-protein interaction occurs in the absence of DNA binding.

KW - Bacteriophage HK022

KW - DNA-protein interaction

KW - Excisionase

KW - Fluorescence resonance energy transfer

KW - Protein-protein interaction

KW - Site-specific recombination

UR - http://www.scopus.com/inward/record.url?scp=0038540684&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(03)00512-X

DO - 10.1016/S0014-5793(03)00512-X

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

AN - SCOPUS:0038540684

SN - 0014-5793

VL - 545

SP - 133

EP - 138

JO - FEBS Letters

JF - FEBS Letters

IS - 2-3

ER -

Activity of coliphage HK022 excisionase (Xis) in the absence of DNA binding

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this