scholarly journals Cellobionic acid utilization: from Neurospora crassa to Saccharomyces cerevisiae

2015 ◽  
Vol 8 (1) ◽  
Author(s):  
Xin Li ◽  
Kulika Chomvong ◽  
Vivian Yaci Yu ◽  
Julie M Liang ◽  
Yuping Lin ◽  
...  
1994 ◽  
Vol 269 (26) ◽  
pp. 17705-17712
Author(s):  
S.K. Mahanty ◽  
U.S. Rao ◽  
R.A. Nicholas ◽  
G.A. Scarborough

Genetics ◽  
2001 ◽  
Vol 157 (3) ◽  
pp. 1067-1075 ◽  
Author(s):  
Laura E Bean ◽  
William H Dvorachek ◽  
Edward L Braun ◽  
Allison Errett ◽  
Gregory S Saenz ◽  
...  

AbstractWe report the analysis of a 36-kbp region of the Neurospora crassa genome, which contains homologs of two closely linked stationary phase genes, SNZ1 and SNO1, from Saccharomyces cerevisiae. Homologs of SNZ1 encode extremely highly conserved proteins that have been implicated in pyridoxine (vitamin B6) metabolism in the filamentous fungi Cercospora nicotianae and in Aspergillus nidulans. In N. crassa, SNZ and SNO homologs map to the region occupied by pdx-1 (pyridoxine requiring), a gene that has been known for several decades, but which was not sequenced previously. In this study, pyridoxine-requiring mutants of N. crassa were found to possess mutations that disrupt conserved regions in either the SNZ or SNO homolog. Previously, nearly all of these mutants were classified as pdx-1. However, one mutant with a disrupted SNO homolog was at one time designated pdx-2. It now appears appropriate to reserve the pdx-1 designation for the N. crassa SNZ homolog and pdx-2 for the SNO homolog. We further report annotation of the entire 36,030-bp region, which contains at least 12 protein coding genes, supporting a previous conclusion of high gene densities (12,000-13,000 total genes) for N. crassa. Among genes in this region other than SNZ and SNO homologs, there was no evidence of shared function. Four of the genes in this region appear to have been lost from the S. cerevisiae lineage.


1994 ◽  
Vol 41 (4) ◽  
pp. 467-471 ◽  
Author(s):  
A Dzikowska ◽  
J P Le Caer ◽  
P Jonczyk ◽  
P Wëgleński

Arginase (EC 3.5.3.1) of Aspergillus nidulans, the enzyme which enables the fungus to use arginine as the sole nitrogen source was purified to homogeneity. Molecular mass of the purified arginase subunit is 40 kDa and is similar to that reported for the Neurospora crassa (38.3 kDa) and Saccharomyces cerevisiae (39 kDa) enzymes. The native molecular mass of arginase is 125 kDa. The subunit/native molecular mass ratio suggests a trimeric form of the protein. The arginase protein was cleaved and partially sequenced. Two out of the six polypeptides sequenced show a high degree of homology to conserved domains in arginases from other species.


1992 ◽  
Vol 157 (4) ◽  
pp. 305-310 ◽  
Author(s):  
Ralf Kneer ◽  
Toni M. Kutchan ◽  
Andreas Hochberger ◽  
Meinhart H. Zenk

2011 ◽  
Vol 77 (16) ◽  
pp. 5822-5825 ◽  
Author(s):  
Suk-Jin Ha ◽  
Qiaosi Wei ◽  
Soo Rin Kim ◽  
Jonathan M. Galazka ◽  
Jamie Cate ◽  
...  

ABSTRACTWe demonstrate improved ethanol yield and productivity through cofermentation of cellobiose and galactose by an engineeredSaccharomyces cerevisiaestrain expressing genes coding for cellodextrin transporter (cdt-1) and intracellular β-glucosidase (gh1-1) fromNeurospora crassa. Simultaneous fermentation of cellobiose and galactose can be applied to producing biofuels from hydrolysates of marine plant biomass.


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