A 41,000 M(r) polypeptide of Chlorella exhibits a circadian rhythm in its synthesis and possesses characteristic features of a putative essential clock protein as was proposed by the coupled translation-membrane model. Purification of this polypeptide and a microsequencing analysis yielded a N-terminal sequence of 35 amino acids that showed no homology to known sequences that were thought to be involved in circadian rhythm such as the per gene of Drosophila and the frq gene of Neurospora. However, strong homology was observed to 3-phosphoglycerate kinase (PGK) of different organisms. The highest homology (83%) of this Chlorella sequence was found with the PGK of wheat chloroplast. PGK activity and the 41,000 M(r) polypeptide co-purified through differential centrifugation and gel filtration. These data, and comparison with the physical properties of other known PGK molecules, support the conclusion that the 41,000 M(r) polypeptide of Chlorella, a candidate for a putative essential clock protein, is 3-phosphoglycerate kinase.
On the molecular mechanism of the circadian clock. The 41,000 M(r) clock protein of Chlorella was identified as 3-phosphoglycerate kinase
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O.J. Walla, E.J. de Groot, M. Schweiger; On the molecular mechanism of the circadian clock. The 41,000 M(r) clock protein of Chlorella was identified as 3-phosphoglycerate kinase. J Cell Sci 1 February 1994; 107 (2): 719–726. doi: https://doi.org/10.1242/jcs.107.2.719
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