scholarly journals Flocculation of Saccharomyces cerevisiae is dependent on activation of Slt2 and Rlm1 regulated by the cell wall integrity pathway

2019 ◽  
Vol 112 (4) ◽  
pp. 1350-1369 ◽  
Author(s):  
Santhosh Kumar Sariki ◽  
Ramesh Kumawat ◽  
Vikash Singh ◽  
Raghuvir Singh Tomar
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Cell Wall Integrity ◽  
Cell Wall Integrity Pathway

Pneumocystis carinii BCK1 Complements the Saccharomyces cerevisiae Cell Wall Integrity Pathway

2003 ◽  
Vol 50 (s1) ◽  
pp. 676-677 ◽  
Author(s):  
PAWAN K. VOHRA ◽  
THEODORE J. KOTTOM ◽  
ANDREW H. LIMPER ◽  
CHARLES F. THOMAS
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Pneumocystis Carinii ◽  
Cell Wall Integrity ◽  
Cell Wall Integrity Pathway

scholarly journals Mpt5p, a Stress Tolerance- and Lifespan-Promoting PUF Protein in Saccharomyces cerevisiae, Acts Upstream of the Cell Wall Integrity Pathway

2006 ◽  
Vol 6 (2) ◽  
pp. 262-270 ◽  
Author(s):  
Mark S. Stewart ◽  
Sue Ann Krause ◽  
Josephine McGhie ◽  
Joseph V. Gray
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Life Span ◽  
Stress Tolerance ◽  
Synthetic Medium ◽  
Cell Wall Integrity ◽  
Puf Proteins ◽  
Downstream Target ◽  
Cell Wall Integrity Pathway ◽  
Puf Protein

ABSTRACT Pumilio family (PUF) proteins affect specific genes by binding to, and inhibiting the translation or stability of, their transcripts. The PUF domain is required and sufficient for this function. One Saccharomyces cerevisiae PUF protein, Mpt5p (also called Puf5p or Uth4p), promotes stress tolerance and replicative life span (the maximum number of doublings a mother cell can undergo before entering into senescence) by an unknown mechanism thought to partly overlap with, but to be independent of, the cell wall integrity (CWI) pathway. Here, we found that mpt5Δ mutants also display a short chronological life span (the time cells stay alive in saturated cultures in synthetic medium), a defect that is suppressed by activation of CWI signaling. We found that Mpt5p is an upstream activator of the CWI pathway: mpt5Δ mutants display the appropriate phenotypes and genetic interactions, display low basal activity of the pathway, and are defective in activation of the pathway upon thermal stress. A set of mRNAs that specifically bind to Mpt5p was recently reported. One such putative target, LRG1, encodes a GTPase-activating protein for Rho1p that directly links Mpt5p to CWI signaling: Lrg1p inhibits CWI signaling, LRG1 mRNA contains a consensus Mpt5p-binding site in its putative 3′ untranslated region, loss of Lrg1p suppresses the temperature sensitivity and CWI signaling defects of mpt5Δ mutants, and LRG1 mRNA abundance is inhibited by Mpt5p. We conclude that Mpt5p is required for normal replicative and chronological life spans and that the CWI pathway is a key and direct downstream target of this PUF protein.

scholarly journals Cell fusion in yeast is negatively regulated by components of the cell wall integrity pathway

2019 ◽  
Vol 30 (4) ◽  
pp. 441-452 ◽  
Author(s):  
Allison E. Hall ◽  
Mark D. Rose
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Death ◽  
Cell Wall ◽  
Yeast Cell ◽  
Cell Fusion ◽  
Cell Walls ◽  
Cell Wall Integrity ◽  
Fusion Genes ◽  
Cell Wall Degradation ◽  
Cell Wall Integrity Pathway

During mating, Saccharomyces cerevisiae cells must degrade the intervening cell wall to allow fusion of the partners. Because improper timing or location of cell wall degradation would cause lysis, the initiation of cell fusion must be highly regulated. Here, we find that yeast cell fusion is negatively regulated by components of the cell wall integrity (CWI) pathway. Loss of the cell wall sensor, MID2, specifically causes “mating-induced death” after pheromone exposure. Mating-induced death is suppressed by mutations in cell fusion genes ( FUS1, FUS2, RVS161, CDC42), implying that mid2Δ cells die from premature fusion without a partner. Consistent with premature fusion, mid2Δ shmoos had thinner cell walls and lysed at the shmoo tip. Normally, Cdc42p colocalizes with Fus2p to form a focus only when mating cells are in contact (prezygotes) and colocalization is required for cell fusion. However, Cdc42p was aberrantly colocalized with Fus2p to form a focus in mid2Δ shmoos. A hyperactive allele of the CWI kinase Pkc1p ( PKC1*) caused decreased cell fusion and Cdc42p localization in prezygotes. In shmoos, PKC1* increased Cdc42p localization; however, it was not colocalized with Fus2p or associated with cell death. We conclude that Mid2p and Pkc1p negatively regulate cell fusion via Cdc42p and Fus2p.

scholarly journals Quercetin Protects Saccharomyces cerevisiae against Oxidative Stress by Inducing Trehalose Biosynthesis and the Cell Wall Integrity Pathway

PLoS ONE ◽  
2012 ◽  
Vol 7 (9) ◽  
pp. e45494 ◽  
Author(s):  
Rita Vilaça ◽  
Vanda Mendes ◽  
Marta Vaz Mendes ◽  
Laura Carreto ◽  
Maria Amélia Amorim ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Cell Wall Integrity ◽  
Cell Wall Integrity Pathway ◽  
Trehalose Biosynthesis

Low temperature highlights the functional role of the cell wall integrity pathway in the regulation of growth in Saccharomyces cerevisiae

2012 ◽  
Vol 446 (3) ◽  
pp. 477-488 ◽  
Author(s):  
Isaac Córcoles-Sáez ◽  
Lídia Ballester-Tomas ◽  
Maria A. de la Torre-Ruiz ◽  
Jose A. Prieto ◽  
Francisca Randez-Gil
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Low Temperatures ◽  
Cell Wall Integrity ◽  
Target Of Rapamycin ◽  
Cold Sensitivity ◽  
Cold Response ◽  
Response Component ◽  
Cell Wall Integrity Pathway ◽  
Mutant Cells

Unlike other stresses, the physiological significance and molecular mechanisms involved in the yeast cold response are largely unknown. In the present study, we show that the CWI (cell wall integrity) pathway plays an important role in the growth of Saccharomyces cerevisiae at low temperatures. Cells lacking the Wsc1p (wall integrity and stress response component 1) membrane sensor or the MAPKs (mitogen-activated protein kinases) Bck1p (bypass of C kinase 1), Mkk (Mapk kinase) 1p/Mkk2p or Slt2p (suppressor of lyt2) exhibited cold sensitivity. However, there was no evidence of either a cold-provoked perturbation of the cell wall or a differential cold expression program mediated by Slt2p. The results of the present study suggest that Slt2p is activated by different inputs in response to nutrient signals and mediates growth control through TORC1 (target of rapamycin 1 complex)–Sch9p (suppressor of cdc25) and PKA (protein kinase A) at low temperatures. We found that absence of TOR1 (target of rapamycin 1) causes cold sensitivity, whereas a ras2Δ mutant shows increased cold growth. Lack of Sch9p alleviates the phenotype of slt2Δ and bck1Δ mutant cells, as well as attenuation of PKA activity by overexpression of BCY1 (bypass of cyclase mutations 1). Interestingly, swi4Δ mutant cells display cold sensitivity, but the phenotype is neither mediated by the Slt2p-regulated induction of Swi4p (switching deficient 4)-responsive promoters nor influenced by osmotic stabilization. Hence, cold signalling through the CWI pathway has distinct features and might mediate still unknown effectors and targets.

scholarly journals The interaction of Slt2 MAP kinase with Knr4 is necessary for signalling through the cell wall integrity pathway in Saccharomyces cerevisiae

2003 ◽  
Vol 49 (1) ◽  
pp. 23-35 ◽  
Author(s):  
Helene Martin-Yken ◽  
Adilia Dagkessamanskaia ◽  
Fadi Basmaji ◽  
Arnaud Lagorce ◽  
Jean Francois
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Map Kinase ◽  
Cell Wall Integrity ◽  
Cell Wall Integrity Pathway

Saccharomyces cerevisiae YCRO17c/CWH43encodes a putative sensor/transporter protein upstream of theBCK2branch of the PKC1-dependent cell wall integrity pathway

Yeast ◽  
2001 ◽  
Vol 18 (9) ◽  
pp. 827-840 ◽  
Author(s):  
Helene Martin-Yken ◽  
Adilia Dagkessamanskaia ◽  
Piet De Groot ◽  
Arthur Ram ◽  
Frans Klis ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Cell Wall Integrity ◽  
Transporter Protein ◽  
Cell Wall Integrity Pathway ◽  
Dependent Cell
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