Abstract

BackgroundThe plant circadian clock has at its core a feedback loop that includes TIMING OF CAB2 EXPRESSION 1 (TOC1). This protein has an as of yet unknown biochemical activity. It has been noted that the extreme amino-terminus of this protein is distantly related in sequence to response regulators (RR), and thus TOC1 is a member of the so-called pseudo response regulator (PRR) family. As well, the extreme carboxy-terminus has a small sequence stretch related to the other PRRs and CONSTANS (CO)-like proteins, and this peptide stretch has been termed the CCT (for CONSTANS, CONSTANS-LIKE, TOC1) domain.MethodsTo extend further our understanding of the TOC1 protein, we performed a ROSETTA structural prediction on TOC1 orthologues from four plant species. Phylogenetic interpretations assisted in model construction.ResultsFrom our models, we suggest that TOC1 is a three-domain protein: TOC1 has an amino-terminal signaling-domain related to response receivers, a carboxy-terminal domain that could participate both in metal binding and in transcriptional regulation, and a linker domain that connects the two.ConclusionThe models we present should prove useful in future hypothesis-driven biochemical analyses to test the predictions that TOC1 is a multi-domain signaling component of the plant circadian clock.

Highlights

  • The plant circadian clock has at its core a feedback loop that includes TIMING OF CAB2 EXPRESSION 1 (TOC1)

  • Dominant outputs include the oscillation of free-cytosolic calcium (Ca2+) [1], which are generated from cADPR-derived signals [2], and the rhythmic accumulation of around 10% of all transcripts [2,3,4,5,6]

  • Out-group sequences were the paralogues of the pseudo response regulator (PRR) family, which are PRR3/5/7/9 from Arabidopsis, and from rice (Oryza sativa), OsPRR37 and OsPRR73, OsPRR59 and OsPRR95 [23,34]

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Summary

Results

We suggest that TOC1 is a three-domain protein: TOC1 has an aminoterminal signaling-domain related to response receivers, a carboxy-terminal domain that could participate both in metal binding and in transcriptional regulation, and a linker domain that connects the two

Background
Methods
Results and discussion
31. Alexandrov NN
64. Zhang Y
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