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

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

Research output: Contribution to journalArticlepeer-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 α helices (αE and αF). Our analysis reveals a noncrystallographic dPER dimer mediated by intermolecular interactions of PAS-A with PAS-B and helix αF. We show that αF is essential for dPER homodimerization and that the PAS-A-αF interaction plays a crucial role in dPER clock function, as it is affected by the 29 hr long-period perL mutation.

Original languageEnglish
Pages (from-to)69-82
Number of pages14
JournalMolecular Cell
Volume17
Issue number1
DOIs
Publication statusPublished - Jan 7 2005

ASJC Scopus subject areas

  • Molecular Biology

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