Structural basis of the bacteriophage TP901‐1 CI repressor dimerization and interaction with DNA

Kim Krighaar Rasmussen; Anders Kokkenborg Varming; Simon N. Schmidt; Kristian Erik Høpfner Frandsen; Peter Waaben Thulstrup; Malene Ringkjøbing Jensen; Leila Lo Leggio

doi:10.1002/1873-3468.13060

Structural basis of the bacteriophage TP901‐1 CI repressor dimerization and interaction with DNA

Kim Krighaar Rasmussen, Anders Kokkenborg Varming, Simon N. Schmidt, Kristian Erik Høpfner Frandsen, Peter Waaben Thulstrup, Malene Ringkjøbing Jensen, Leila Lo Leggio

2 Citationer (Scopus)

55 Downloads (Pure)

Abstract

Temperate bacteriophages are known for their bistability, which in TP901-1 is controlled by two proteins, CI and MOR. Clear 1 repressor (CI) is hexameric and binds three palindromic operator sites via an N-terminal helix-turn-helix domain (NTD). A dimeric form, such as the truncated CI∆58 investigated here, is necessary for high-affinity binding to DNA. The crystal structure of the dimerization region (CTD₁) is determined here, showing that it forms a pair of helical hooks. This newly determined structure is used together with the known crystal structure of the CI-NTD and small angle X-ray scattering data, to determine the solution structure of CI∆58 in complex with a palindromic operator site, showing that the two NTDs bind on opposing sides of the DNA helix.

Originalsprog	Engelsk
Tidsskrift	F E B S Letters
Vol/bind	592
Udgave nummer	10
Sider (fra-til)	1738-1750
Antal sider	13
ISSN	0014-5793
DOI	https://doi.org/10.1002/1873-3468.13060
Status	Udgivet - maj 2018

Adgang til dokumentet

10.1002/1873-3468.13060

Rasmussen_et_al_2018_preprintwithSIIndsendt manuskript, 3,8 MBLicens: Andet
1873-3468.13060Forlagets udgivne version, 961 KB

Citationsformater

@article{b33293134ec945f3a92ef2885f54bc3d,

title = "Structural basis of the bacteriophage TP901‐1 CI repressor dimerization and interaction with DNA",

abstract = "Temperate bacteriophages are known for their bistability, which in TP901-1 is controlled by two proteins, CI and MOR. Clear 1 repressor (CI) is hexameric and binds three palindromic operator sites via an N-terminal helix-turn-helix domain (NTD). A dimeric form, such as the truncated CI∆58 investigated here, is necessary for high-affinity binding to DNA. The crystal structure of the dimerization region (CTD1) is determined here, showing that it forms a pair of helical hooks. This newly determined structure is used together with the known crystal structure of the CI-NTD and small angle X-ray scattering data, to determine the solution structure of CI∆58 in complex with a palindromic operator site, showing that the two NTDs bind on opposing sides of the DNA helix.",

author = "Rasmussen, {Kim Krighaar} and Varming, {Anders Kokkenborg} and Schmidt, {Simon N.} and Frandsen, {Kristian Erik H{\o}pfner} and Thulstrup, {Peter Waaben} and Jensen, {Malene Ringkj{\o}bing} and {Lo Leggio}, Leila",

year = "2018",

month = may,

doi = "10.1002/1873-3468.13060",

language = "English",

volume = "592",

pages = "1738--1750",

journal = "F E B S Letters",

issn = "0014-5793",

publisher = "JohnWiley & Sons Ltd",

number = "10",

}

TY - JOUR

T1 - Structural basis of the bacteriophage TP901‐1 CI repressor dimerization and interaction with DNA

AU - Rasmussen, Kim Krighaar

AU - Varming, Anders Kokkenborg

AU - Schmidt, Simon N.

AU - Frandsen, Kristian Erik Høpfner

AU - Thulstrup, Peter Waaben

AU - Jensen, Malene Ringkjøbing

AU - Lo Leggio, Leila

PY - 2018/5

Y1 - 2018/5

N2 - Temperate bacteriophages are known for their bistability, which in TP901-1 is controlled by two proteins, CI and MOR. Clear 1 repressor (CI) is hexameric and binds three palindromic operator sites via an N-terminal helix-turn-helix domain (NTD). A dimeric form, such as the truncated CI∆58 investigated here, is necessary for high-affinity binding to DNA. The crystal structure of the dimerization region (CTD1) is determined here, showing that it forms a pair of helical hooks. This newly determined structure is used together with the known crystal structure of the CI-NTD and small angle X-ray scattering data, to determine the solution structure of CI∆58 in complex with a palindromic operator site, showing that the two NTDs bind on opposing sides of the DNA helix.

AB - Temperate bacteriophages are known for their bistability, which in TP901-1 is controlled by two proteins, CI and MOR. Clear 1 repressor (CI) is hexameric and binds three palindromic operator sites via an N-terminal helix-turn-helix domain (NTD). A dimeric form, such as the truncated CI∆58 investigated here, is necessary for high-affinity binding to DNA. The crystal structure of the dimerization region (CTD1) is determined here, showing that it forms a pair of helical hooks. This newly determined structure is used together with the known crystal structure of the CI-NTD and small angle X-ray scattering data, to determine the solution structure of CI∆58 in complex with a palindromic operator site, showing that the two NTDs bind on opposing sides of the DNA helix.

U2 - 10.1002/1873-3468.13060

DO - 10.1002/1873-3468.13060

M3 - Letter

C2 - 29683476

SN - 0014-5793

VL - 592

SP - 1738

EP - 1750

JO - F E B S Letters

JF - F E B S Letters

IS - 10

ER -

Structural basis of the bacteriophage TP901‐1 CI repressor dimerization and interaction with DNA

Abstract

Adgang til dokumentet

Fingeraftryk

Citationsformater