Enhanced surface display efficiency of β-glucosidase in Saccharomyces cerevisiae by disruption of cell wall protein-encoding genes YGP1 and CWP2

2021 ◽  
pp. 108305
Author(s):  
Jantima Arnthong ◽  
Jatupong Ponjarat ◽  
Piyada Bussadee ◽  
Pacharawan Deenarn ◽  
Parichat Prommana ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Surface Display ◽  
Cell Wall Protein ◽  
Protein Encoding ◽  
Encoding Genes ◽  
Enhanced Surface

scholarly journals Monitoring expression of yeast cell wall protein-encoding genes in response to high hydrostatic pressure

2014 ◽  
Vol 8 (S4) ◽  
Author(s):  
Tassia Nati ◽  
Fernanda Bravim ◽  
Jimmy Soares ◽  
Mainã Mantovanelli Mota ◽  
James Riley Broach ◽  
...  
Keyword(s):  
Cell Wall ◽  
Hydrostatic Pressure ◽  
Yeast Cell ◽  
High Hydrostatic Pressure ◽  
Cell Wall Protein ◽  
Yeast Cell Wall ◽  
Protein Encoding ◽  
Encoding Genes

scholarly journals Transcription of multiple cell wall protein-encoding genes inSaccharomyces cerevisiaeis differentially regulated during the cell cycle

1998 ◽  
Vol 161 (2) ◽  
pp. 345-349 ◽  
Author(s):  
L.Heleen P Caro ◽  
Gertien J Smits ◽  
Piet Egmond ◽  
John W Chapman ◽  
Frans M Klis
Keyword(s):  
Cell Cycle ◽  
Cell Wall ◽  
Cell Wall Protein ◽  
Protein Encoding ◽  
Multiple Cell ◽  
Encoding Genes

scholarly journals Cell Surface Expression of Bacterial Esterase A by Saccharomyces cerevisiae and Its Enhancement by Constitutive Activation of the Cellular Unfolded Protein Response

2006 ◽  
Vol 72 (11) ◽  
pp. 7140-7147 ◽  
Author(s):  
Frank Breinig ◽  
Björn Diehl ◽  
Sabrina Rau ◽  
Christian Zimmer ◽  
Helmut Schwab ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Cell Surface ◽  
Surface Display ◽  
Cell Surface Display ◽  
Constitutive Activation ◽  
Unfolded Protein ◽  
Yeast Cell Surface ◽  
Protein Response

ABSTRACT Yeast cell surface display is a powerful tool for expression and immobilization of biocatalytically active proteins on a unicellular eukaryote. Here bacterial carboxylesterase EstA from Burkholderia gladioli was covalently anchored into the cell wall of Saccharomyces cerevisiae by in-frame fusion to the endogenous yeast proteins Kre1p, Cwp2p, and Flo1p. When p-nitrophenyl acetate was used as a substrate, the esterase specific activities of yeast expressing the protein fusions were 103 mU mg−1 protein for Kre1/EstA/Cwp2p and 72 mU mg−1 protein for Kre1/EstA/Flo1p. In vivo cell wall targeting was confirmed by esterase solubilization after laminarinase treatment and immunofluorescence microscopy. EstA expression resulted in cell wall-associated esterase activities of 2.72 U mg−1 protein for Kre1/EstA/Cwp2p and 1.27 U mg−1 protein for Kre1/EstA/Flo1p. Furthermore, esterase display on the yeast cell surface enabled the cells to effectively grow on the esterase-dependent carbon source glycerol triacetate (Triacetin). In the case of Kre1/EstA/Flo1p, in vivo maturation within the yeast secretory pathway and final incorporation into the wall were further enhanced when there was constitutive activation of the unfolded protein response pathway. Our results demonstrate that esterase cell surface display in yeast, which, as shown here, is remarkably more effective than EstA surface display in Escherichia coli, can be further optimized by activating the protein folding machinery in the eukaryotic secretion pathway.

scholarly journals Phylogenetic origin and transcriptional regulation at the post-diauxic phase of SPI1, in Saccharomyces cerevisiae

2012 ◽  
Vol 17 (3) ◽  
Author(s):  
Fernando Cardona ◽  
Marcel.Lí Olmo ◽  
Agustín Aranda
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Transcriptional Regulation ◽  
Stationary Phases ◽  
Cell Wall Protein ◽  
Null Mutant ◽  
Common Features ◽  
A Cell ◽  
Phylogenetic Origin ◽  
Pka Pathway

AbstractThe gene SPI1, of Saccharomyces cerevisiae, encodes a cell wall protein that is induced in several stress conditions, particularly in the postdiauxic and stationary phases of growth. It has a paralogue, SED1, which shows some common features in expression regulation and in the null mutant phenotype. In this work we have identified homologues in other species of yeasts and filamentous fungi, and we have also elucidated some aspects of the origin of SPI1, by duplication and diversification of SED1. In terms of regulation, we have found that the expression in the post-diauxic phase is regulated by genes related to the PKA pathway and stress response (MSN2/4, YAK1, POP2, SOK2, PHD1, and PHO84) and by genes involved in the PKC pathway (WSC2, PKC1, and MPK1).

scholarly journals Characterization of Phosphopantetheinyl Hydrolase from Mycobacterium tuberculosis

2021 ◽  
Author(s):  
Shilpika Pandey ◽  
Amrita Singh ◽  
Guangli Yang ◽  
Felipe B. d’Andrea ◽  
Xiuju Jiang ◽  
...  
Keyword(s):  
Infectious Disease ◽  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Posttranslational Modification ◽  
Content Type ◽  
Protein Encoding ◽  
And Function ◽  
Encoding Genes

Tuberculosis (TB), caused by Mycobacterium tuberculosis , was the leading cause of death from an infectious disease before COVID, yet the in vivo essentiality and function of many of the protein-encoding genes expressed by M. tuberculosis are not known. We biochemically characterize M. tuberculosis ’s phosphopantetheinyl hydrolase, PptH, a protein unique to mycobacteria that removes an essential posttranslational modification on proteins involved in synthesis of lipids important for the bacterium’s cell wall and virulence.

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