On the molecular mechanism of the circadian clock: The 41,000 <i>M</i>r clock protein of <i>Chlorella</i> was identified as 3-phosphoglycerate kinase

Walla, O.J.; Groot, E.J. de; Schweiger, Manfred

doi:10.1242/jcs.107.2.719

Cited by 9 publications

(1 citation statement)

References 59 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Studies based on Y 9 mutants of E. gracilis have shown that the expression of this enzyme is influenced by light [213], although little is known about the molecular basis and function of this expression. Intriguingly, Chlorella chloroplast PGK exhibits circadian expression and appears to be an essential clock protein [214]. It would be interesting to study the physiological significance of a possible circadian regulation of PGK in E. gracilis .…”

Section: Phosphoglycerate Kinase In Protistsmentioning

confidence: 99%

Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea

et al. 2020

View full text Add to dashboard Cite

Phosphoglycerate kinase (PGK) is a glycolytic enzyme that is well conserved among the three domains of life. PGK is usually a monomeric enzyme of about 45 kDa that catalyses one of the two ATP-producing reactions in the glycolytic pathway, through the conversion of 1,3-bisphosphoglycerate (1,3BPGA) to 3-phosphoglycerate (3PGA). It also participates in gluconeogenesis, catalysing the opposite reaction to produce 1,3BPGA and ADP. Like most other glycolytic enzymes, PGK has also been catalogued as a moonlighting protein, due to its involvement in different functions not associated with energy metabolism, which include pathogenesis, interaction with nucleic acids, tumorigenesis progression, cell death and viral replication. In this review, we have highlighted the overall aspects of this enzyme, such as its structure, reaction kinetics, activity regulation and possible moonlighting functions in different protistan organisms, especially both free-living and parasitic Kinetoplastea. Our analysis of the genomes of different kinetoplastids revealed the presence of open-reading frames (ORFs) for multiple PGK isoforms in several species. Some of these ORFs code for unusually large PGKs. The products appear to contain additional structural domains fused to the PGK domain. A striking aspect is that some of these PGK isoforms are predicted to be catalytically inactive enzymes or ‘dead’ enzymes. The roles of PGKs in kinetoplastid parasites are analysed, and the apparent significance of the PGK gene duplication that gave rise to the different isoforms and their expression in Trypanosoma cruzi is discussed.

show abstract

Section: Phosphoglycerate Kinase In Protistsmentioning

confidence: 99%

Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea

et al. 2020

View full text Add to dashboard Cite

show abstract

Circadian Rhythmicity: Is the “Biological Clock” Hardware or Software?

Lüttge

2003

Progress in Botany

View full text Add to dashboard Cite

Regulation and molecular structure of a circadian oscillating protein located in the cell membrane of the prokaryote Synechococcus RF-1

Chen

Chien

Huang

1996

Planta

View full text Add to dashboard Cite

When a light/light-adapted culture of Synechococcus RF-1 is exposed to a diurnal light/dark regimen, the synthesis of more than ten of its polypeptides is known to become entrained to a circadian oscillating pattern which persists for some time under free-running conditions. One of the circadian oscillating polypeptides, COP23, was found to be located in the cell membrane. The rate of COP23 synthesis is controlled at the transcription level. In addition to the protein synthesis rate, the content of COP23 also exhibited a circadian rhythm. Pulse labeling with [35S]methionine revealed that COP23 was relatively stable in an arrhythmic culture. However, the exposure of Synechococcus RF-1 to a light/dark regimen induced not only a circadian synthesis rhythm, but also a rapid degradation of COP23 protein at a defined period of time. The induction of rapid protein degradation was prevented by the presence of chloramphenicol. The gene encoding the COP23 polypeptide has been cloned and sequenced. The amino acid sequence derived from the open-reading frame revealed that a signal peptide (28 amino acids) does not appear to be part of the mature COP23. The mature COP23 does not have a membrane-associated segment, and it is suggested to be a peripheral molecule. With respect to their DNA base sequence and protein amino acid sequence, none of the proteins documented in the EMBL and PC/Gene data bases are significantly homologous with the COP23 molecule.

show abstract

On the molecular mechanism of the circadian clock: The 41,000 Mr clock protein of Chlorella was identified as 3-phosphoglycerate kinase

Cited by 9 publications

References 59 publications

Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea

Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea

Circadian Rhythmicity: Is the “Biological Clock” Hardware or Software?

Regulation and molecular structure of a circadian oscillating protein located in the cell membrane of the prokaryote Synechococcus RF-1

Contact Info

Product

Resources

About