Evidence for control of nitrogen metabolism by a START-dependent mechanism in Saccharomyces cerevisiae.
It is generally thought that cell growth and metabolism regulate cell division and not vice versa. Here, we examined Saccharomyces cerevisiae cells growing under conditions of continuous culture in a chemostat. We found that loss of G1 cyclins, or inactivation of the cyclin-dependent kinase Cdc28p, reduced the activity of glutamate synthase (Glt1p), a key enzyme in nitrogen assimilation. We also present evidence indicating that the G1 cyclin-dependent control of Glt1p may involve Jem1p, a DnaJ-type chaperone. Our results suggest that completion of START may be linked to nitrogen metabolism.
Bryan
B A
BA
Department of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, TX 77843, USA.
McGrew
E
E
Lu
Y
Y
Polymenis
M
M
D001483:Base Sequence; D017489:CDC28 Protein Kinase, S cerevisiae / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism; D002453:Cell Cycle / Q000502:physiology; D016213:Cyclins / Q000235:genetics / Q000378:metabolism; D004271:DNA, Fungal / Q000235:genetics; D016193:G1 Phase / Q000502:physiology; D005800:Genes, Fungal; D005970:Glutamate Synthase / Q000235:genetics / Q000378:metabolism; D009584:Nitrogen / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism
C082719:CLN1 protein, S cerevisiae; C082721:CLN2 protein, S cerevisiae; D016213:Cyclins; D004271:DNA, Fungal; D029701:Saccharomyces cerevisiae Proteins; D005970:Glutamate Synthase; D017489:CDC28 Protein Kinase, S cerevisiae; D009584:Nitrogen