scholarly journals Role of Cell Cycle-regulated Expression in the Localized Incorporation of Cell Wall Proteins in Yeast

2006 ◽  
Vol 17 (7) ◽  
pp. 3267-3280 ◽  
Author(s):  
Gertien J. Smits ◽  
Laura R. Schenkman ◽  
Stanley Brul ◽  
John R. Pringle ◽  
Frans M. Klis
Keyword(s):  
Cell Cycle ◽  
Cell Wall ◽  
Mechanical Damage ◽  
Cell Wall Proteins ◽  
Functional Interaction ◽  
Promoter Regions ◽  
Septum Formation ◽  
Regulated Expression ◽  
Mother Cells

The yeast cell wall is an essential organelle that protects the cell from mechanical damage and antimicrobial peptides, participates in cell recognition and adhesion, and is important for the generation and maintenance of normal cell shape. We studied the localization of three covalently bound cell wall proteins in Saccharomyces cerevisiae. Tip1p was found only in mother cells, whereas Cwp2p was incorporated in small-to-medium–sized buds. When the promoter regions of TIP1 and CWP2 (responsible for transcription in early G1and S/G2phases, respectively) were exchanged, the localization patterns of Tip1p and Cwp2p were reversed, indicating that the localization of cell wall proteins can be completely determined by the timing of transcription during the cell cycle. The third protein, Cwp1p, was incorporated into the birth scar, where it remained for several generations. However, we could not detect any role of Cwp1p in strengthening the birth scar wall or any functional interaction with the proteins that mark the birth scar pole as a potential future budding site. Promoter-exchange experiments showed that expression in S/G2phase is necessary but not sufficient for the normal localization of Cwp1p. Studies of mutants in which septum formation is perturbed indicate that the normal asymmetric localization of Cwp1p also depends on the normal timing of septum formation, composition of the septum, or both.

scholarly journals EGFR-ERK induced activation of GRHL1 promotes cell cycle progression by up-regulating cell cycle related genes in lung cancer

2021 ◽  
Vol 12 (5) ◽  
Author(s):  
Yiming He ◽  
Mingxi Gan ◽  
Yanan Wang ◽  
Tong Huang ◽  
Jianbin Wang ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Cell Cycle ◽  
Cell Cycle Progression ◽  
Potential Role ◽  
Target Genes ◽  
Nuclear Translocation ◽  
Phosphorylation Site ◽  
Promoter Regions ◽  
Cycle Progression

AbstractGrainyhead-like 1 (GRHL1) is a transcription factor involved in embryonic development. However, little is known about the biological functions of GRHL1 in cancer. In this study, we found that GRHL1 was upregulated in non-small cell lung cancer (NSCLC) and correlated with poor survival of patients. GRHL1 overexpression promoted the proliferation of NSCLC cells and knocking down GRHL1 inhibited the proliferation. RNA sequencing showed that a series of cell cycle-related genes were altered when knocking down GRHL1. We further demonstrated that GRHL1 could regulate the expression of cell cycle-related genes by binding to the promoter regions and increasing the transcription of the target genes. Besides, we also found that EGF stimulation could activate GRHL1 and promoted its nuclear translocation. We identified the key phosphorylation site at Ser76 on GRHL1 that is regulated by the EGFR-ERK axis. Taken together, these findings elucidate a new function of GRHL1 on regulating the cell cycle progression and point out the potential role of GRHL1 as a drug target in NSCLC.

scholarly journals Immunoreactive cell wall proteins of Clostridium difficile identified by human sera

2008 ◽  
Vol 57 (6) ◽  
pp. 750-756 ◽  
Author(s):  
Anne Wright ◽  
Denise Drudy ◽  
Lorraine Kyne ◽  
Katherine Brown ◽  
Neil F. Fairweather
Keyword(s):  
Cell Wall ◽  
Clostridium Difficile ◽  
Cell Wall Proteins ◽  
Hospital Outbreak ◽  
Human Sera ◽  
Potential Vaccine ◽  
Immunogenic Proteins ◽  
Susceptible Populations ◽  
Developed World

Clostridium difficile is a leading cause of nosocomial infection in the developed world, causing antibiotic-associated disease in susceptible populations. The identity of immunogenic proteins is important in understanding the pathogenesis of disease and in the design of vaccines. This study analysed the sera of six patients infected during a hospital outbreak of a C. difficile ribotype 017 strain. Using a proteomics-based approach, cell wall proteins were separated by two-dimensional PAGE, and immunoreactive proteins were revealed by reaction with patient sera. The identity of immunoreactive proteins was established by MS. Forty-two different proteins were identified in total. All patient sera reacted with at least one component of the surface-layer protein (SLP), four reacted with both components (high- and low-molecular-mass SLPs), and five reacted with one other cell wall protein, suggesting that these are immunodominant antigens. The role of these proteins as potential vaccine candidates and their roles in pathogenesis deserve further study.

scholarly journals Involvement of Sortase Anchoring of Cell Wall Proteins in Biofilm Formation by Streptococcusmutans

2005 ◽  
Vol 73 (6) ◽  
pp. 3773-3777 ◽  
Author(s):  
Céline M. Lévesque ◽  
Elena Voronejskaia ◽  
Yi-Chen Cathy Huang ◽  
Richard W. Mair ◽  
Richard P. Ellen ◽  
...  
Keyword(s):  
Cell Wall ◽  
Biofilm Formation ◽  
Cell Wall Proteins ◽  
Planktonic Cells ◽  
Genes Encoding

ABSTRACT Streptococcus mutans is one of the best-known biofilm-forming organisms associated with humans. We investigated the role of the sortase gene (srtA) in monospecies biofilm formation and observed that inactivation of srtA caused a decrease in biofilm formation. Genes encoding three putative sortase-dependent proteins were also found to be up-regulated in biofilms versus planktonic cells and mutations in these genes resulted in reduced biofilm biomass.

scholarly journals Functional Interaction Between the PKC1 Pathway and CDC31 Network of SPB Duplication Genes

Genetics ◽  
2000 ◽  
Vol 155 (4) ◽  
pp. 1543-1559 ◽  
Author(s):  
Waheeda Khalfan ◽  
Irena Ivanovska ◽  
Mark D Rose
Keyword(s):  
Cell Cycle ◽  
Cell Wall ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Genetic Interactions ◽  
Genetic Screens ◽  
Functional Interaction ◽  
Cycle Arrest ◽  
Pole Body ◽  
Synthetically Lethal

Abstract The earliest known step in yeast spindle pole body (SPB) duplication requires Cdc31p and Kar1p, two physically interacting SPB components, and Dsk2p and Rad23p, a pair of ubiquitin-like proteins. Components of the PKC1 pathway were found to interact with these SPB duplication genes in two independent genetic screens. Initially, SLG1 and PKC1 were obtained as high-copy suppressors of dsk2Δ rad23Δ and a mutation in MPK1 was synthetically lethal with kar1-Δ17. Subsequently, we demonstrated extensive genetic interactions between the PKC1 pathway and the SPB duplication mutants that affect Cdc31p function. The genetic interactions are unlikely to be related to the cell-wall integrity function of the PKC1 pathway because the SPB mutants did not exhibit cell-wall defects. Overexpression of multiple PKC1 pathway components suppressed the G2/M arrest of the SPB duplication mutants and mutations in MPK1 exacerbated the cell cycle arrest of kar1-Δ17, suggesting a role for the PKC1 pathway in SPB duplication. We also found that mutations in SPC110, which encodes a major SPB component, showed genetic interactions with both CDC31 and the PKC1 pathway. In support of the model that the PKC1 pathway regulates SPB duplication, one of the phosphorylated forms of Spc110p was absent in pkc1 and mpk1Δ mutants.

Role of cell wall topography in conjugation of Schizosaccharomyces pombe

1975 ◽  
Vol 21 (9) ◽  
pp. 1399-1405 ◽  
Author(s):  
Eva Streiblová ◽  
A. Wolf
Keyword(s):  
Cell Cycle ◽  
Cell Wall ◽  
Schizosaccharomyces Pombe ◽  
Cycle Duration ◽  
Cell Cycle Duration ◽  
Morphological Criteria ◽  
The Moment

The surface of the zygotes of Schizosaccharomyces pombe was studied by observing fluorescence following primulin treatment. Conjugation occurred only at the poles. Competence to fuse was independent of actual pole growth and pole ontogeny (old or new pole). The cells were competent to fuse throughout the first three-quarters of the cell cycle. Morphological criteria indicate that cell pairs are not synchronized at the moment of fusion. The length of the G1 phases of individual conjugating cells apparently ranges from 0.1 to 0.7 of the cell cycle duration.

scholarly journals Localization of Synthesis of β1,6-Glucan inSaccharomyces cerevisiae

1999 ◽  
Vol 181 (24) ◽  
pp. 7414-7420 ◽  
Author(s):  
Roy C. Montijn ◽  
Edwin Vink ◽  
Wally H. Müller ◽  
Arie J. Verkleij ◽  
Herman Van Den Ende ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Surface ◽  
Glycoside Hydrolases ◽  
Restrictive Temperature ◽  
Secretory Vesicles ◽  
Cell Wall Proteins ◽  
Hydrophobic Cluster Analysis ◽  
Hydrophobic Cluster ◽  
Alternative Function

ABSTRACT β1,6-Glucan is a key component of the yeast cell wall, interconnecting cell wall proteins, β1,3-glucan, and chitin. It has been postulated that the synthesis of β1,6-glucan begins in the endoplasmic reticulum with the formation of protein-bound primer structures and that these primer structures are extended in the Golgi complex by two putative glucosyltransferases that are functionally redundant, Kre6 and Skn1. This is followed by maturation steps at the cell surface and by coupling to other cell wall macromolecules. We have reinvestigated the role of Kre6 and Skn1 in the biogenesis of β1,6-glucan. Using hydrophobic cluster analysis, we found that Kre6 and Skn1 show significant similarities to family 16 glycoside hydrolases but not to nucleotide diphospho-sugar glycosyltransferases, indicating that they are glucosyl hydrolases or transglucosylases instead of genuine glucosyltransferases. Next, using immunogold labeling, we tried to visualize intracellular β1,6-glucan in cryofixed sec1-1 cells which had accumulated secretory vesicles at the restrictive temperature. No intracellular labeling was observed, but the cell surface was heavily labeled. Consistent with this, we could detect substantial amounts of β1,6-glucan in isolated plasma membrane-derived microsomes but not in post-Golgi secretory vesicles. Taken together, our data indicate that the synthesis of β1,6-glucan takes place largely at the cell surface. An alternative function for Kre6 and Skn1 is discussed.

Yeast flocculation—the role of cell wall proteins

1994 ◽  
Vol 2 (1-3) ◽  
pp. 159-164 ◽  
Author(s):  
P. Moradas-Ferreira ◽  
P.A. Fernandes ◽  
M.J. Costa
Keyword(s):  
Cell Wall ◽  
Cell Wall Proteins ◽  
Yeast Flocculation

scholarly journals Extracellular cell wall β(1,3)glucan is required to couple septation to actomyosin ring contraction

2013 ◽  
Vol 203 (2) ◽  
pp. 265-282 ◽  
Author(s):  
Javier Muñoz ◽  
Juan Carlos G. Cortés ◽  
Matthias Sipiczki ◽  
Mariona Ramos ◽  
José Angel Clemente-Ramos ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Animal Cells ◽  
Contractile Ring ◽  
Septum Formation ◽  
Main Cell ◽  
Primary Septum ◽  
Pulling Forces

Cytokinesis has been extensively studied in different models, but the role of the extracellular cell wall is less understood. Here we studied this process in fission yeast. The essential protein Bgs4 synthesizes the main cell wall β(1,3)glucan. We show that Bgs4-derived β(1,3)glucan is required for correct and stable actomyosin ring positioning in the cell middle, before the start of septum formation and anchorage to the cell wall. Consequently, β(1,3)glucan loss generated ring sliding, oblique positioned rings and septa, misdirected septum synthesis indicative of relaxed rings, and uncoupling between a fast ring and membrane ingression and slow septum synthesis, suggesting that cytokinesis can progress with defective septum pushing and/or ring pulling forces. Moreover, Bgs4-derived β(1,3)glucan is essential for secondary septum formation and correct primary septum completion. Therefore, our results show that extracellular β(1,3)glucan is required for cytokinesis to connect the cell wall with the plasma membrane and for contractile ring function, as proposed for the equivalent extracellular matrix in animal cells.

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