Depression of Saccharomyces cerevisiae invasive growth on non-glucose carbon sources requires the Snf1 kinase.
Haploid Saccharomyces cerevisiae cells growing on media lacking glucose but containing high concentrations of carbon sources such as fructose, galactose, raffinose, and ethanol exhibit enhanced agar invasion. These carbon sources also promote diploid filamentous growth in response to nitrogen starvation. The enhanced invasive and filamentous growth phenotypes are suppressed by the addition of glucose to the media and require the Snf1 kinase. Mutations in the PGI1 and GND1 genes encoding carbon source utilization enzymes confer enhanced invasive growth that is unaffected by glucose but requires active Snf1. Carbon source does not modulate FLO11 flocculin expression, but enhanced polarized bud site selection is necessary for invasion on certain carbon sources. Interestingly, deletion of SNF1 blocks invasion without affecting bud site selection. Snf1 is also required for formation of spokes and hubs in multicellular mats. To examine glucose repression of invasive growth more broadly, we performed genome-wide microarray expression analysis in wild-type cells growing on glucose and galactose, and snf1 Delta cells on galactose. SNF1 probably mediates glucose repression of multiple genes potentially involved in invasive and filamentous growth. FLO11-independent cell-cell attachment, cell wall integrity, and/or polarized growth are affected by carbon source metabolism. In addition, derepression of cell cycle genes and signalling via the cAMP-PKA pathway appears to depend upon SNF1 activity during growth on galactose.
Department of Chemical Engineering, University of Wisconsin, Madison, Madison, WI 53706, USA.
Sean P
SP
Palecek
Archita S
AS
Parikh
Joon H
JH
Huh
Stephen J
SJ
Kron
D002244:Carbon / Q000378:metabolism; D002448:Cell Adhesion; D018797:Cell Cycle Proteins / Q000096:biosynthesis / Q000235:genetics; D016764:Cell Polarity; D002473:Cell Wall / Q000648:ultrastructure; D003470:Culture Media / Q000737:chemistry / Q000494:pharmacology; D000242:Cyclic AMP / Q000502:physiology; D000431:Ethanol / Q000494:pharmacology; D015966:Gene Expression Regulation, Fungal / Q000187:drug effects; D005956:Glucose-6-Phosphate Isomerase / Q000096:biosynthesis / Q000235:genetics; D005990:Glycerol / Q000494:pharmacology; D006601:Hexoses / Q000494:pharmacology; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000096:biosynthesis / Q000235:genetics; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000502:physiology*; D011887:Raffinose / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology / Q000235:genetics / Q000254:growth & development* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000502:physiology*; D015290:Second Messenger Systems / Q000187:drug effects
D018797:Cell Cycle Proteins; D003470:Culture Media; C110690:FLO11 protein, S cerevisiae; D006601:Hexoses; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D029701:Saccharomyces cerevisiae Proteins; D000431:Ethanol; D002244:Carbon; D000242:Cyclic AMP; C071570:SNF1-related protein kinases; D017346:Protein Serine-Threonine Kinases; D005956:Glucose-6-Phosphate Isomerase; D011887:Raffinose; D005990:Glycerol