Crystal structure and interactions of the PAS repeat region of the Drosophila clock protein PERIOD

Ozkan Yildiz; Masao Doi; Irene Yujnovsky; Luca Cardone; Alex Berndt; Sven Hennig; Sabrina Schulze; Claus Urbanke; Paolo Sassone-Corsi; Eva Wolf

doi:10.1016/j.molcel.2004.11.022

Crystal structure and interactions of the PAS repeat region of the Drosophila clock protein PERIOD

Ozkan Yildiz
, Masao Doi
, Irene Yujnovsky
, Luca Cardone
, Alex Berndt
, Sven Hennig
, Sabrina Schulze
, Claus Urbanke
, Paolo Sassone-Corsi
, Eva Wolf

AIMMS

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

PERIOD proteins are central components of the Drosophila and mammalian circadian clock. Their function is controlled by daily changes in synthesis, cellular localization, phosphorylation, degradation, as well as specific interactions with other clock components. Here we present the crystal structure of a Drosophila PERIOD (dPER) fragment comprising two tandemly organized PAS (PER-ARNT-SIM) domains (PAS-A and PAS-B) and two additional C-terminal alpha helices (alphaE and alphaF). Our analysis reveals a noncrystallographic dPER dimer mediated by intermolecular interactions of PAS-A with PAS-B and helix alphaF. We show that alphaF is essential for dPER homodimerization and that the PAS-A-alphaF interaction plays a crucial role in dPER clock function, as it is affected by the 29 hr long-period perL mutation.

Original language	English
Pages (from-to)	69-82
Number of pages	14
Journal	Molecular Cell
Volume	17
Issue number	1
DOIs	https://doi.org/10.1016/j.molcel.2004.11.022
Publication status	Published - 7 Jan 2005

Keywords

Amino Acid Sequence
Animals
Circadian Rhythm
Crystallography, X-Ray
Dimerization
Drosophila
Drosophila Proteins
Models, Molecular
Molecular Sequence Data
Mutation
Nuclear Proteins
Period Circadian Proteins
Protein Structure, Quaternary
Protein Structure, Tertiary
Repetitive Sequences, Amino Acid
Sequence Homology, Amino Acid
Static Electricity
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

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10.1016/j.molcel.2004.11.022

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title = "Crystal structure and interactions of the PAS repeat region of the Drosophila clock protein PERIOD",

abstract = "PERIOD proteins are central components of the Drosophila and mammalian circadian clock. Their function is controlled by daily changes in synthesis, cellular localization, phosphorylation, degradation, as well as specific interactions with other clock components. Here we present the crystal structure of a Drosophila PERIOD (dPER) fragment comprising two tandemly organized PAS (PER-ARNT-SIM) domains (PAS-A and PAS-B) and two additional C-terminal alpha helices (alphaE and alphaF). Our analysis reveals a noncrystallographic dPER dimer mediated by intermolecular interactions of PAS-A with PAS-B and helix alphaF. We show that alphaF is essential for dPER homodimerization and that the PAS-A-alphaF interaction plays a crucial role in dPER clock function, as it is affected by the 29 hr long-period perL mutation.",

keywords = "Amino Acid Sequence, Animals, Circadian Rhythm, Crystallography, X-Ray, Dimerization, Drosophila, Drosophila Proteins, Models, Molecular, Molecular Sequence Data, Mutation, Nuclear Proteins, Period Circadian Proteins, Protein Structure, Quaternary, Protein Structure, Tertiary, Repetitive Sequences, Amino Acid, Sequence Homology, Amino Acid, Static Electricity, Comparative Study, Journal Article, Research Support, Non-U.S. Gov't",

author = "Ozkan Yildiz and Masao Doi and Irene Yujnovsky and Luca Cardone and Alex Berndt and Sven Hennig and Sabrina Schulze and Claus Urbanke and Paolo Sassone-Corsi and Eva Wolf",

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T1 - Crystal structure and interactions of the PAS repeat region of the Drosophila clock protein PERIOD

AU - Yildiz, Ozkan

AU - Doi, Masao

AU - Yujnovsky, Irene

AU - Cardone, Luca

AU - Berndt, Alex

AU - Hennig, Sven

AU - Schulze, Sabrina

AU - Urbanke, Claus

AU - Sassone-Corsi, Paolo

AU - Wolf, Eva

PY - 2005/1/7

Y1 - 2005/1/7

N2 - PERIOD proteins are central components of the Drosophila and mammalian circadian clock. Their function is controlled by daily changes in synthesis, cellular localization, phosphorylation, degradation, as well as specific interactions with other clock components. Here we present the crystal structure of a Drosophila PERIOD (dPER) fragment comprising two tandemly organized PAS (PER-ARNT-SIM) domains (PAS-A and PAS-B) and two additional C-terminal alpha helices (alphaE and alphaF). Our analysis reveals a noncrystallographic dPER dimer mediated by intermolecular interactions of PAS-A with PAS-B and helix alphaF. We show that alphaF is essential for dPER homodimerization and that the PAS-A-alphaF interaction plays a crucial role in dPER clock function, as it is affected by the 29 hr long-period perL mutation.

AB - PERIOD proteins are central components of the Drosophila and mammalian circadian clock. Their function is controlled by daily changes in synthesis, cellular localization, phosphorylation, degradation, as well as specific interactions with other clock components. Here we present the crystal structure of a Drosophila PERIOD (dPER) fragment comprising two tandemly organized PAS (PER-ARNT-SIM) domains (PAS-A and PAS-B) and two additional C-terminal alpha helices (alphaE and alphaF). Our analysis reveals a noncrystallographic dPER dimer mediated by intermolecular interactions of PAS-A with PAS-B and helix alphaF. We show that alphaF is essential for dPER homodimerization and that the PAS-A-alphaF interaction plays a crucial role in dPER clock function, as it is affected by the 29 hr long-period perL mutation.

KW - Amino Acid Sequence

KW - Animals

KW - Circadian Rhythm

KW - Crystallography, X-Ray

KW - Dimerization

KW - Drosophila

KW - Drosophila Proteins

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Mutation

KW - Nuclear Proteins

KW - Period Circadian Proteins

KW - Protein Structure, Quaternary

KW - Protein Structure, Tertiary

KW - Repetitive Sequences, Amino Acid

KW - Sequence Homology, Amino Acid

KW - Static Electricity

KW - Comparative Study

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1016/j.molcel.2004.11.022

DO - 10.1016/j.molcel.2004.11.022

M3 - Article

C2 - 15629718

SN - 1097-2765

VL - 17

SP - 69

EP - 82

JO - Molecular Cell

JF - Molecular Cell

IS - 1

ER -

Crystal structure and interactions of the PAS repeat region of the Drosophila clock protein PERIOD

Abstract

Keywords

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