Shuji Akiyama

This paper traces the molecular shape evolution of KaiC, a circadian clock protein, showing it evolved from an asymmetric hexamer to a compact symmetric hexamer and a dodecamer over 3.1 billion years.

The paper identifies amino acid residues in KaiC that regulate temperature compensation through local and non-local interactions affecting ATPase activity.

This paper identifies the 322nd residue of KaiC as a third period-tuning site, showing that mutations at this site can alter circadian period length through effects on ATPase activity.

The paper investigates the evolutionary origin of self-sustained Kai protein circadian oscillators in cyanobacteria by analyzing ancestral Kai proteins and their functional and structural development.

This study identifies the autoinhibition mechanism of KaiC priming phosphorylation and shows how KaiA relieves this inhibition by altering R385 interactions.