Format

Send to

Choose Destination
J Agric Food Chem. 2017 Mar 1;65(8):1641-1648. doi: 10.1021/acs.jafc.6b05348. Epub 2017 Feb 16.

Mutant Potential Ubiquitination Sites in Dur3p Enhance the Urea and Ethyl Carbamate Reduction in a Model Rice Wine System.

Author information

1
Key Laboratory of Industrial Biotechnology, Ministry of Education and School of Biotechnology, Jiangnan University , 1800 Lihu Road, Wuxi, Jiangsu 214122, China.
2
Zhejiang Guyuelongshan Shaoxing Wine Company , 13 Yangjiang Road, Shaoxing, Zhejiang 312099, China.

Abstract

Ubiquitination can significantly affect the endocytosis and degradation of plasma membrane proteins. Here, the ubiquitination of a Saccharomyces cerevisiae urea plasma membrane transporter (Dur3p) was altered. Two potential ubiquitination sites, lysine residues K556 and K571, of Dur3p were predicted and replaced by arginine, and the effects of these mutations on urea utilization and formation under different nitrogen conditions were investigated. Compared with Dur3p, the Dur3pK556R mutant showed a 20.1% decrease in ubiquitination level in yeast nitrogen base medium containing urea and glutamine. It also exhibited a >75.8% decrease in urea formation in yeast extract-peptone-dextrose medium and 41.3 and 55.4% decreases in urea and ethyl carbamate formation (a known carcinogen), respectively, in a model rice wine system. The results presented here show that the mutation of Dur3p ubiquitination sites could significantly affect urea utilization and formation. Modifying the ubiquitination of specific transporters might have promising applications in rationally engineering S. cerevisiae strains to efficiently use specific nitrogen sources.

KEYWORDS:

nitrogen catabolite repression; nitrogen sources; post-translational modifications; site-directed mutagenesis; urea transporter

PMID:
28185458
DOI:
10.1021/acs.jafc.6b05348
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for American Chemical Society
Loading ...
Support Center