Proteome analysis of the circadian clock protein PERIOD2

Gul H., Selvi S., Yilmaz F., Ozcelik G., Olfaz-Aslan S., Yazan S., ...Daha Fazla

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, cilt.90, ss.1315-1330, 2022 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 90
  • Basım Tarihi: 2022
  • Doi Numarası: 10.1002/prot.26314
  • Dergi Adı: PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Agricultural & Environmental Science Database, BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, EMBASE, Food Science & Technology Abstracts, INSPEC, MEDLINE, Veterinary Science Database
  • Sayfa Sayıları: ss.1315-1330
  • Anahtar Kelimeler: BioID, circadian clock, PERIOD2, protein-protein interactions, proteomics, CANCER, RHYTHM, CRYPTOCHROME, EXPRESSION, COMPONENTS, MECHANISM, DYNAMICS, GENETICS, ADHESION, BINDING
  • İstanbul Üniversitesi Adresli: Evet

Özet

Circadian rhythms are a series of endogenous autonomous 24-h oscillations generated by the circadian clock. At the molecular level, the circadian clock is based on a transcription-translation feedback loop, in which BMAL1 and CLOCK transcription factors of the positive arm activate the expression of CRYPTOCHROME (CRY) and PERIOD (PER) genes of the negative arm as well as the circadian clock-regulated genes. There are three PER proteins, of which PER2 shows the strongest oscillation at both stability and cellular localization level. Protein-protein interactions (PPIs) or interactome of the circadian clock proteins have been investigated using classical methods such as two-dimensional gel electrophoresis, immunoprecipitation-coupled mass spectrometry, and yeast-two hybrid assay where the dynamic and weak interactions are difficult to catch. To identify the interactome of PER2 we have adopted proximity-dependent labeling with biotin and mass spectrometry-based identification of labeled proteins (BioID). In addition to known interactions with such as CRY1 and CRY2, we have identified several new PPIs for PER2 and confirmed some of them using co-immunoprecipitation technique. This study characterizes the PER2 protein interactions in depth, and it also implies that using a fast BioID method with miniTurbo or TurboID coupled to other major circadian clock proteins might uncover other interactors in the clock that have yet to be discovered.