PAS is a dimerization domain common to Drosophila period and several transcription factors

Huang, Z. J., Edery, I., Rosbash, M. (1993) PAS is a dimerization domain common to Drosophila period and several transcription factors. Nature, 364 (6434). pp. 259-62. ISSN 0028-0836 (Print)0028-0836

URL: http://www.ncbi.nlm.nih.gov/pubmed/8391649
DOI: 10.1038/364259a0

Abstract

Mutations in the period gene product (PER) can shorten or lengthen the circadian rhythms of Drosophila melanogaster, but its biochemical activity has not been established. PER contains a motif of approximately 270 amino acids whose function is unknown (termed PAS) and which is also present in three transcription factors of the basic-helix-loop-helix (bHLH) type, in the D. melanogaster single-minded gene product (SIM), and in both subunits of the mammalian dioxin receptor complex. We show here that the PER PAS functions in vitro as a novel protein dimerization motif and that it can mediate associations between different members of the PAS protein family. The dimerization efficiency is decreased by several missense mutations in the PAS domain, including the original perL mutation, which lengthens circadian periods from 24 h to 29 h (ref. 1). The results indicate that the PAS domain may function as a dimerization domain in both SIM and the dioxin receptor complex, and that PER may regulate circadian gene transcription partly by interacting with the PAS domain of bHLH--PAS-containing transcription factors.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Animals Cross-Linking Reagents DNA/metabolism DNA-Binding Proteins/genetics/metabolism Drosophila Proteins Drosophila melanogaster Humans Molecular Sequence Data Mutation Nuclear Proteins/*chemistry/genetics Peptide Fragments/*chemistry/genetics Period Circadian Proteins Precipitin Tests Protein Binding Protein Conformation Proteins/chemistry Receptors, Aryl Hydrocarbon Receptors, Drug/chemistry Transcription Factors/*chemistry/genetics
Subjects: organism description > animal > insect > Drosophila
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
CSHL Authors:
Communities: CSHL labs > Huang lab
Depositing User: Matt Covey
Date Deposited: 05 Jun 2014 20:41
Last Modified: 05 Jun 2014 20:41
Related URLs:
URI: http://repository.cshl.edu/id/eprint/30193

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