The protein encoded by SAC6, a gene that can mutate to suppress a temperature-sensitive defect in the yeast actin gene, has been identified as a 67-kilodalton actin-binding protein (ABP 67) that associates with all identifiable actin structures. This finding demonstrates the in vivo functional importance of the actin-ABP 67 interaction previously established in vitro and illustrates the use of suppressor analysis to identify physically interacting proteins.

https://science.sciencemag.org/content/sci/243/4888/231.full.pdf

A yeast actin-binding protein is encoded by SAC6, a gene found by suppression of an actin mutation.

A temperature-sensitive mutant, sec34-2, is defective in the late stages of endoplasmic reticulum (ER)-to-Golgi transport. A high-copy suppressor screen that uses thesec34-2 mutant has resulted in ...

High-Copy Suppressor Analysis Reveals a Physical Interaction between Sec34p and Sec35p, a Protein Implicated in Vesicle Docking

In the Saccharomyces cerevisiae glycolytic pathway, 11 enzymes catalyze the stepwise conversion of glucose to two molecules of ethanol plus two CO₂ molecules. In the highly crowded cytoplasm, this pathway would be very inefficient if it were dependent on substrate/enzyme diffusion. Therefore, the existence of a multi-enzymatic glycolytic complex has been suggested. This complex probably uses the cytoskeleton to stabilize the interaction of the various enzymes. Here, the role of filamentous actin (F-actin) in stabilization of a putative glycolytic metabolon is reported. Experiments were performed in isolated enzyme/actin mixtures, cytoplasmic extracts and permeabilized yeast cells. Polymerization of actin was promoted using phalloidin or inhibited using cytochalasin D or latrunculin. The polymeric filamentous F-actin, but not the monomeric globular G-actin, stabilized both the interaction of isolated glycolytic pathway enzyme mixtures and the whole fermentation pathway, leading to higher fermentation activity. The associated complexes were resistant against inhibition as a result of viscosity (promoted by the disaccharide trehalose) or inactivation (using specific enzyme antibodies). In S. cerevisiae, a glycolytic metabolon appear to assemble in association with F-actin. In this complex, fermentation activity is enhanced and enzymes are partially protected against inhibition by trehalose or by antibodies.

https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/febs.12387

A glycolytic metabolon in Saccharomyces cerevisiae is stabilized by F‐actin

Proteins involved in vesicular transport and membrane fusion.

CP1 (encoded by CEP1 ) is a Saccharomyces cerevisiae chromatin protein that binds a DNA element conserved in centromeres and in the 5′-flanking DNA of methionine biosynthetic ( MET ) genes. Strains lacking CP1 are defective in chromosome segregation and MET gene transcription, leading to the hypothesis that CP1 plays a general role in assembling higher order chromatin structures at genomic sites where it is bound. A screen for mutations synthetically lethal with a cep1 null allele yielded five recessive csl ( cep1 synthetic lethal) mutations, each defining a unique complementation group. Four of the five mutations synergistically increased the loss rate of marker chromosomes carrying a centromere lacking the CP1 binding site, suggesting that the cep1 synthetic lethality was due to chromosome segregation defects. Three of these four CSL genes were subsequently found to be known or imputed kinetochore genes: CEP3, NDC10 , and CSE4 . The fourth, CSL4 , corresponded to ORF YNL232w on chromosome XIV , and was found to be essential. A human cDNA was identified that encoded a protein homologous to Csl4 and that complemented the csl4-1 mutation. The results are consistent with the view that the major cellular role of CP1 is to safeguard the biochemical integrity of the kinetochore.

/pdf/mutations-synthetically-lethal-with-cep1-target-s-cerevisiae-3momkw2tb7.pdf

Mutations Synthetically Lethal with cep1 Target S. cerevisiae Kinetochore Components

Why study the cytoskeleton in yeast

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Why study the cytoskeleton in yeast