PROTEOMIC CHANGES OF RECOMBINANT YEAST: PHARMACO-INDUSTRIAL POTENTIAL

Abstract

The original yeast strain Hansenula anomala 2340 was implanted by low-energy nitrogen ion (N+) to obtain the mutant strain N6076. The mutant strain produced a red quinone compound, not synthesized by the parent strain. Two-dimensional fluorescence difference gel electrophoresis (2-D DIGE) and mass spectrometry (MS) were utilized to analyze the protein profile of the mutant strain N6076. The proteome changes were compared to those of the original strain to assess the amount of change that the metabolic pathways underwent in the mutant strain. The results indicated the detection of 57 different expressed proteins (P< 0.05) when the N6076 mutant strain was cultured in the liquid medium for 96 h as compared to that of the original strain. Of these different expressed protein spots, 27 were upregulated, and 30 were down-regulated. Also, 56 protein spots were identified with the aid of MALDI-TOF and tandem (TOF-TOF) MS. The protein score confidence interval (CI) of the protein profiling in the down-regulated protein spots 273 and 1294 were 81.371% and 12.864%, respectively, by bioinformatic analysis. This probably points to the fact that the irradiation by N+ contributed to the mutation of these two proteins.