Inner clock: Biologists research the mechanism of an auxiliary clock

November 17, 2017

In December, the Nobel Prize for Medicine and Physiology will be awarded for the identification of genes that control the inner clock. The honoured academics examined fruit flies to determine the biorhythm. Biochemist Professor Dr. Dorothee Staiger of Bielefeld University has been researching the inner clock of plants for twenty years. Her team has now published a new study in the research journal Genome Biology. One finding: not only the inner clock, but also a protein acting as an "auxiliary clock" ensures that recurring routines take place in the cells.

"The inner clock ensures that a plant adapts its metabolism to the environment in good time," says Dorothee Staiger. "Thus enabling it to directly use the first rays of the sun for photosynthesis, for example, and produce carbohydrates."

As the Nobel Prize winners have shown, individual genes in the genome of plants, animals and humans control the inner clock. Messenger molecules - messenger RNAs - are produced on these genes at a certain time of day. These molecules start the formation of clock proteins, which in turn reach their highest concentration at a fixed time of day.

Clock proteins switch their own genes on and off at 24-hour intervals. They are therefore responsible for their own rhythm. The clock proteins also ensure that other genes in the cell are active at the best possible time of day. They initiate different processes at certain times of the day: from opening the flowers and defending against pathogens in plants to the sleep-wake rhythm in humans.

Now Staiger and her team have examined another part of the inner clock in detail, using the model plant Arabidopsis thaliana (thale cress). During the process, they found an "auxiliary clock" - a protein called "AtGRP7". "Interestingly, the AtGRP7 protein behaves almost like a clock protein - it influences its own 24-hour rhythm," says Dr. Tino Köster. "As a result, the amount of AtGRP7 protein rises during the day and falls again at night." Köster and his colleague Katja Meyer are the lead authors of the study.

According to the researchers, a daily recurring cycle that can be divided into three phases is responsible for this. "In the first phase, the protein binds to its own messenger RNA and breaks it down at night. In the second phase, the reduction in messenger RNA causes less of the AtGRP7 protein to be formed. In the third phase, the diminished amount of protein ensures that new messenger RNA can form again. "This marks the beginning of the cycle all over again," says Katja Meyer, who is doing her doctorate in Staiger's "RNA Biology and Molecular Physiology" research team. The scientific work of both Meyer and Tino Köster was funded by the German Academic Scholarship Foundation for several years.

A new finding of the study is that the protein not only binds to its own messenger RNA, but is also capable of blocking a lot of other messenger RNAs in the cell. For this, Staiger's team and their cooperation partners at the University Halle-Wittenberg had to find all the messenger RNAs in the cells of the plants on which the protein is located. In addition, the biologists subjected the plant to irradiation with ultraviolet light for about two minutes. This results in the messenger RNAs bonding firmly with the protein. They then isolated the protein and identified the RNAs bound to it by means of high-throughput sequencing. This new method is called iCLIP. It was originally developed for animal cell cultures. "For the new study, we were the world's first research team to apply the iCLIP method to whole plants," says Dorothee Staiger.

In a further step, the researchers examined what the protein does with the bound messenger RNAs in the cell. For the analysis, the researchers artificially increased the amount of the AtGRP7 protein in several plants and examined the effects of this on the messenger RNAs. "We were able to show that an increased amount of AtGRP7 can disrupt the rhythm of some messenger RNAs. This means AtGRP7 acts as an auxiliary clock, mediating between the inner clock and the messenger RNAs dependent on the time of day," says Katja Meyer.

The study was funded by the German Research Foundation (DFG) and serves basic research. "Our aim is to understand the basic interrelationships in nature," says Staiger. "In this case, we learn how the inner clock ensures that further smaller clocks are set in motion. And we learn which strategies plants use to adapt to changing environmental conditions."
Original publication:

Katja Meyer, Tino Köster, Christine Nolte, Claus Weinholdt, Martin Lewinski, Ivo Grosse and Dorothee Staiger: Adaptation of iCLIP to plants determines the binding landscape of the clock-regulated RNA-binding protein AtGRP7. Genome Biology,, published on 31 October 2017.

Further information:

The research team:


Professor Dr. Dorothee Staiger, Bielefeld University
Faculty of Biology
Phone: +49 521 106-5609

Bielefeld University

Related Protein Articles from Brightsurf:

The protein dress of a neuron
New method marks proteins and reveals the receptors in which neurons are dressed

Memory protein
When UC Santa Barbara materials scientist Omar Saleh and graduate student Ian Morgan sought to understand the mechanical behaviors of disordered proteins in the lab, they expected that after being stretched, one particular model protein would snap back instantaneously, like a rubber band.

Diets high in protein, particularly plant protein, linked to lower risk of death
Diets high in protein, particularly plant protein, are associated with a lower risk of death from any cause, finds an analysis of the latest evidence published by The BMJ today.

A new understanding of protein movement
A team of UD engineers has uncovered the role of surface diffusion in protein transport, which could aid biopharmaceutical processing.

A new biotinylation enzyme for analyzing protein-protein interactions
Proteins play roles by interacting with various other proteins. Therefore, interaction analysis is an indispensable technique for studying the function of proteins.

Substituting the next-best protein
Children born with Duchenne muscular dystrophy have a mutation in the X-chromosome gene that would normally code for dystrophin, a protein that provides structural integrity to skeletal muscles.

A direct protein-to-protein binding couples cell survival to cell proliferation
The regulators of apoptosis watch over cell replication and the decision to enter the cell cycle.

A protein that controls inflammation
A study by the research team of Prof. Geert van Loo (VIB-UGent Center for Inflammation Research) has unraveled a critical molecular mechanism behind autoimmune and inflammatory diseases such as rheumatoid arthritis, Crohn's disease, and psoriasis.

Resurrecting ancient protein partners reveals origin of protein regulation
After reconstructing the ancient forms of two cellular proteins, scientists discovered the earliest known instance of a complex form of protein regulation.

Sensing protein wellbeing
The folding state of the proteins in live cells often reflect the cell's general health.

Read More: Protein News and Protein Current Events is a participant in the Amazon Services LLC Associates Program, an affiliate advertising program designed to provide a means for sites to earn advertising fees by advertising and linking to