Altered expression of chitin synthetase activity and biochemical changes in the cell wall in a developmental mutant ofPhycomyces

1988 ◽  
Vol 26 (11-12) ◽  
pp. 717-732 ◽  
Author(s):  
Elvia Ruiz-Flores ◽  
Everardo Lopez-Romero ◽  
Arturo Flores-Carreon ◽  
Felix Gutierrez-Corona
Keyword(s):  
Cell Wall ◽  
Biochemical Changes ◽  
Synthetase Activity ◽  
Altered Expression ◽  
Chitin Synthetase ◽  
Developmental Mutant

Altered expression of chitin synthetase activity and biochemical changes in the cell wall in a developmental mutant ofPhycomyces

1988 ◽  
Vol 26 (11-12) ◽  
pp. 717-732
Author(s):  
Elvia Ruiz-Flores ◽  
Everardo Lopez-Romero ◽  
Arturo Flores-Carreon ◽  
Felix Gutierrez-Corona
Keyword(s):  
Cell Wall ◽  
Biochemical Changes ◽  
Synthetase Activity ◽  
Altered Expression ◽  
Chitin Synthetase ◽  
Developmental Mutant

Chitin synthetase activity in a developmental mutant of Phycomyces blakesleeanus

1990 ◽  
Vol 58 (2) ◽  
pp. 67-72 ◽  
Author(s):  
E. Ruiz-Flores ◽  
E. Lopez-Romero ◽  
F. Gutierrez-Corona
Keyword(s):  
Synthetase Activity ◽  
Phycomyces Blakesleeanus ◽  
Chitin Synthetase ◽  
Developmental Mutant

scholarly journals Characterization of LtsA from Rhodococcus erythropolis, an Enzyme with Glutamine Amidotransferase Activity

2005 ◽  
Vol 187 (8) ◽  
pp. 2582-2591 ◽  
Author(s):  
Yasuo Mitani ◽  
XianYing Meng ◽  
Yoichi Kamagata ◽  
Tomohiro Tamura
Keyword(s):  
Cell Wall ◽  
Culture Media ◽  
Rhodococcus Erythropolis ◽  
Mycolic Acid ◽  
Site Directed Mutagenesis ◽  
Host Cells ◽  
Wall Structure ◽  
Synthetase Activity ◽  
Glutamine Amidotransferase ◽  
Glutaminase Activity

ABSTRACT The nocardioform actinomycete Rhodococcus erythropolis has a characteristic cell wall structure. The cell wall is composed of arabinogalactan and mycolic acid and is highly resistant to the cell wall-lytic activity of lysozyme (muramidase). In order to improve the isolation of recombinant proteins from R. erythropolis host cells (N. Nakashima and T. Tamura, Biotechnol. Bioeng. 86:136-148, 2004), we isolated two mutants, L-65 and L-88, which are susceptible to lysozyme treatment. The lysozyme sensitivity of the mutants was complemented by expression of Corynebacterium glutamicum ltsA, which codes for an enzyme with glutamine amidotransferase activity that results from coupling of two reactions (a glutaminase activity and a synthetase activity). The lysozyme sensitivity of the mutants was also complemented by ltsA homologues from Bacillus subtilis and Mycobacterium tuberculosis, but the homologues from Streptomyces coelicolor and Escherichia coli did not complement the sensitivity. This result suggests that only certain LtsA homologues can confer lysozyme resistance. Wild-type recombinant LtsA from R. erythropolis showed glutaminase activity, but the LtsA enzymes from the L-88 and L-65 mutants displayed drastically reduced activity. Interestingly, an ltsA disruptant mutant, which expressed the mutated LtsA, changed from lysozyme sensitive to lysozyme resistant when NH4Cl was added into the culture media. The glutaminase activity of the LtsA mutants inactivated by site-directed mutagenesis was also restored by addition of NH4Cl, indicating that NH3 can be used as an amide donor molecule. Taken together, these results suggest that LtsA is critically involved in mediating lysozyme resistance in R. erythropolis cells.

scholarly journals AFM combined to ATR-FTIR reveals Candida cell wall changes under caspofungin treatment

Nanoscale ◽  
2017 ◽  
Vol 9 (36) ◽  
pp. 13731-13738 ◽  
Author(s):  
Fabienne Quilès ◽  
Isabelle Accoceberry ◽  
Célia Couzigou ◽  
Grégory Francius ◽  
Thierry Noël ◽  
...  
Keyword(s):  
Cell Wall ◽  
Vibrational Spectroscopy ◽  
Biochemical Changes

AFM was combined to vibrational spectroscopy to decipher morphological, mechanical and biochemical changes induced by caspofungin treatment onCandida.

Transcriptome profiling of aSaccharomyces cerevisiaemutant with a constitutively activated Ras/cAMP pathway

2003 ◽  
Vol 16 (1) ◽  
pp. 107-118 ◽  
Author(s):  
D. L. Jones ◽  
J. Petty ◽  
D. C. Hoyle ◽  
A. Hayes ◽  
E. Ragni ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cell Wall ◽  
Microarray Analysis ◽  
Cellular Response ◽  
Ribosome Biogenesis ◽  
Biological Significance ◽  
Altered Expression ◽  
Wall Functions ◽  
Constitutive Activation ◽  
Camp Pathway

Often changes in gene expression levels have been considered significant only when above/below some arbitrarily chosen threshold. We investigated the effect of applying a purely statistical approach to microarray analysis and demonstrated that small changes in gene expression have biological significance. Whole genome microarray analysis of a pde2Δ mutant, constructed in the Saccharomyces cerevisiae reference strain FY23, revealed altered expression of ∼11% of protein encoding genes. The mutant, characterized by constitutive activation of the Ras/cAMP pathway, has increased sensitivity to stress, reduced ability to assimilate nonfermentable carbon sources, and some cell wall integrity defects. Applying the Munich Information Centre for Protein Sequences (MIPS) functional categories revealed increased expression of genes related to ribosome biogenesis and downregulation of genes in the cell rescue, defense, cell death and aging category, suggesting a decreased response to stress conditions. A reduced level of gene expression in the unfolded protein response pathway (UPR) was observed. Cell wall genes whose expression was affected by this mutation were also identified. Several of the cAMP-responsive orphan genes, upon further investigation, revealed cell wall functions; others had previously unidentified phenotypes assigned to them. This investigation provides a statistical global transcriptome analysis of the cellular response to constitutive activation of the Ras/cAMP pathway.

Synthesis of Cell Wall Microfibrils in vitro by a "Soluble" Chitin Synthetase from Mucor rouxii

Science ◽  
1974 ◽  
Vol 186 (4161) ◽  
pp. 357-359 ◽  
Author(s):  
J. Ruiz-Herrera ◽  
S. Bartnicki-Garcia
Keyword(s):  
Cell Wall ◽  
Mucor Rouxii ◽  
Chitin Synthetase
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