PGK1 cDNA ORF clone, Saccharomyces cerevisiae S288C

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

The complete DNA sequence of yeast chromosome III.
Oliver SG, van der Aart QJ, Agostoni-Carbone ML, Aigle M, Alberghina L, Alexandraki D, Antoine G, Anwar R, Ballesta JP, Benit P
Nature357(6373)38-46(1992 May)

Overexpression of PGK1 restored normal ageing and suppress apoptotic phenotypes of the mutant.
Title: PGK1, the gene encoding the glycolitic enzyme phosphoglycerate kinase, acts as a multicopy suppressor of apoptotic phenotypes in S. cerevisiae.

The stability curve reveals the existence of two stable, folded conformers with an abrupt conformational transition occurring at 24 degrees C.
Title: Thermodynamic analysis of the nondenaturational conformational change of baker's yeast phosphoglycerate kinase at 24 degrees C.

Data suggest that proteolysis occurs from the globally unfolded state of E. coli phosphoglycerate kinase, but upon unfolding of only the C-domain in the Saccharomyces enzyme, with the N-domain remaining folded and consequently resistant to cleavage.
Title: Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability.

Misfolding of the domains within the complete protein is synchronized indicating that domain-domain interactions direct the misfolding and amyloid formation mechanism.
Title: Domain interactions direct misfolding and amyloid formation of yeast phosphoglycerate kinase.

A thermodynamic transition intermediate was observed in the pressure-denaturation; the C-terminal domain carrying all the Trp residues seemed to exert structural changes at relatively lower pressure
Title: Pressure-temperature-induced denaturation of yeast phosphoglycerate kinase, a double-domain protein.