Journal
FUNGAL GENETICS AND BIOLOGY
Volume 80, Issue -, Pages 10-18Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.fgb.2015.04.016
Keywords
Neurospora crassa; Nitrate reductase; Recombinant protein expression; Strep-tag (R); Post-translational modification
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Funding
- Deutsche Forschungsgemeinschaft [FOR 1220 PROTRAIN]
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We established an expression and purification procedure for recombinant protein production in Neurospora crassa (N. crassa). This Strep-tag (R) based system was successfully used for purifying recombinant N. crassa nitrate reductase (NR), whose enzymatic activity was compared to recombinant N. crassa NR purified from Escherichia coil. The purity of the two different NR preparations was similar but NR purified from N. crassa showed a significantly higher nitrate turnover rate. Two phosphorylation sites were identified for NR purified from the endogenous expression system. We conclude that homologous expression of N. crassa NR yields a higher active enzyme and propose that NR phosphorylation causes enhanced enzymatic activity. (C) 2015 Elsevier Inc. All rights reserved.
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