Amino acid divergence between the CHS domain contributes to the different intracellular behaviour of Family II fungal chitin synthases in Saccharomyces cerevisiae

Jiménez, Cristina; Sacristán, Carlos; Roncero, M. Isabel G.; Roncero, César

doi:10.1016/j.fgb.2010.08.013

Cited by 7 publications

(4 citation statements)

References 47 publications

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“…Such analysis could be related to the effect of the CSM deletion on the reduction of the nonzymogenic activity (which accounted for less than 10% of the total chitin synthase activity). This activity, quantified without trypsin at pH 8 and in the presence of Co ϩ2 and Ni ϩ2 (22), was reduced in the single and double ⌬csm mutants (data not shown), suggested that the differential effect of cations seen on chitin synthase activities in yeast (49) was also found in filamentous fungi.…”

Section: Complexity Of the Chitin Synthase Family In Filamentous Fungimentioning

confidence: 92%

Chitin Synthases with a Myosin Motor-Like Domain Control the Resistance of Aspergillus fumigatus to Echinocandins

Jiménez‐Ortigosa

Aimanianda

Muszkieta

et al. 2012

Antimicrob Agents Chemother

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dAspergillus fumigatus has two chitin synthases (CSMA and CSMB) with a myosin motor-like domain (MMD) arranged in a head-to-head configuration. To understand the function of these chitin synthases, single and double csm mutant strains were constructed and analyzed. Although there was a slight reduction in mycelial growth of the mutants, the total chitin synthase activity and the cell wall chitin content were similar in the mycelium of all of the mutants and the parental strain. In the conidia, chitin content in the ⌬csmA strain cell wall was less than half the amount found in the parental strain. In contrast, the ⌬csmB mutant strain and, unexpectedly, the ⌬csmA/⌬csmB mutant strain did not show any modification of chitin content in their conidial cell walls. In contrast to the hydrophobic conidia of the parental strain, conidia of all of the csm mutants were hydrophilic due to the presence of an amorphous material covering the hydrophobic surface-rodlet layer. The deletion of CSM genes also resulted in an increased susceptibility of resting and germinating conidia to echinocandins. These results show that the deletion of the CSMA and CSMB genes induced a significant disorganization of the cell wall structure, even though they contribute only weakly to the overall cell wall chitin synthesis.

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Section: Complexity Of the Chitin Synthase Family In Filamentous Fungimentioning

confidence: 92%

Chitin Synthases with a Myosin Motor-Like Domain Control the Resistance of Aspergillus fumigatus to Echinocandins

Jiménez‐Ortigosa

Aimanianda

Muszkieta

et al. 2012

Antimicrob Agents Chemother

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“…Yeast's chitin synthases are predicted to have three to five transmembrane helices toward their C termini, and Chs3 likely has two more transmembrane domains nearer its N terminus (Jimenez et al 2010;Merzendorfer 2011). Amino acid residues important for catalysis lie in a large cytoplasmic domain containing the signature sequences QXXEY, EDRXL, and QXRRW (Nagahashi et al 1995;Saxena et al 1995;Cos et al 1998;Yabe et al 1998;Ruiz-Herrera et al 2002;Merzendorfer 2011).…”

Section: Biosynthesis Of Wall Components At the Plasma Membranementioning

confidence: 99%

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

2012

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The wall gives a Saccharomyces cerevisiae cell its osmotic integrity; defines cell shape during budding growth, mating, sporulation, and pseudohypha formation; and presents adhesive glycoproteins to other yeast cells. The wall consists of b1,3-and b1,6-glucans, a small amount of chitin, and many different proteins that may bear N-and O-linked glycans and a glycolipid anchor. These components become cross-linked in various ways to form higher-order complexes. Wall composition and degree of cross-linking vary during growth and development and change in response to cell wall stress. This article reviews wall biogenesis in vegetative cells, covering the structure of wall components and how they are cross-linked; the biosynthesis of N-and O-linked glycans, glycosylphosphatidylinositol membrane anchors, b1,3-and b1,6-linked glucans, and chitin; the reactions that cross-link wall components; and the possible functions of enzymatic and nonenzymatic cell wall proteins. TABLE OF CONTENTS Abstract 775Introduction 777

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“…CSIII is only modestly zymogenic, because trypsin treatment only increases activity by a factor of 1.7. Moreover, increases in the levels of Chs3 at the PM have been correlated with higher basal activities and increases in chitin synthesis [15,24]. Therefore it can be assumed that CSIII basal activity correspond with the actual levels of chitin synthase in vivo.…”

Section: The Physiological Relevance Of Cs Measurementsmentioning

confidence: 99%

Monitoring Chitin Deposition During Septum Assembly in Budding Yeast

Arcones

Roncero

2016

Methods in Molecular Biology

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The synthesis of the septum is a critical step during cytokinesis in the fungal cell. Moreover, in Saccharomyces cerevisiae septum assembly depends mostly on the proper synthesis and deposition of chitin and, accordingly, on the timely regulation of chitin synthases. In this chapter, we will see how to follow chitin synthesis by two complementary approaches: monitoring chitin deposition in vivo at the septum by calcofluor staining and fluorescence microscopy, and measuring the chitin synthase activities responsible for this synthesis.

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Amino acid divergence between the CHS domain contributes to the different intracellular behaviour of Family II fungal chitin synthases in Saccharomyces cerevisiae

Cited by 7 publications

References 47 publications

Chitin Synthases with a Myosin Motor-Like Domain Control the Resistance of Aspergillus fumigatus to Echinocandins

Chitin Synthases with a Myosin Motor-Like Domain Control the Resistance of Aspergillus fumigatus to Echinocandins

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

Monitoring Chitin Deposition During Septum Assembly in Budding Yeast

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