Anuscript; available in PMC 2016 April 02.Galv et al. EJG is supported by Conacyt M ico CB-2011-01-166241 and INFR-2012-01-187757. RG is supported by Conacyt M ico, I020/193/10 FON.INST.-29-10. GB is supported by NIH grant R01 GM066018.PageAuthor Manuscript Author Manuscript Author Manuscript Author ManuscriptExperiments had been performed at the University of Pittsburgh, USA and Cinvestav-Sur, M ico City. Conception and early experiments: TPR and EJG who also designed, performed and analyzed the electrophysiological data. EJG and GB wrote the manuscript. RG, GGL and EL performed the IHC experiments. All of the authors study and agreed the interpretation from the final results.
bs_bs_bannerMinireview Arginase-1/ARG1 Protein Purity & Documentation histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicumRobert K. Kulis-Horn, Marcus Persicke and J n Kalinowski Centrum f Biotechnologie, Universit Bielefeld, Universit sstra 27, 33615 Bielefeld, Germany. SummaryL-Histidine biosynthesis is definitely an ancient metabolic pathway present in bacteria, archaea, reduced eukaryotes, and plants. For decades L-histidine biosynthesis has been studied mostly in Escherichia coli and Salmonella typhimurium, revealing fundamental regulatory processes in bacteria. Moreover, inside the final 15 years this pathway has been also investigated intensively inside the industrial amino acid-producing bacterium Corynebacterium glutamicum, revealing similarities to E. coli and S. typhimurium, as well as differences. This overview summarizes the present understanding of L-histidine biosynthesis in C. glutamicum. The genes involved and corresponding enzymes are described, in distinct focusing around the imidazoleglycerol-phosphate synthase (HisFH) plus the histidinol-phosphate phosphatase (HisN). The transcriptional organization of his genes in C. glutamicum can also be reported, such as the 4 histidine operons and their promoters. Information of transcriptional regulation in the course of stringent response and by histidine itself is summarized plus a translational regulation mechanism is discussed, as well as clues about a histidine transport system. Finally, we go over the potential of using this information to make or boost C. glutamicum strains for the industrial L-histidine production.Introduction Corynebacterium glutamicum is actually a well-established microorganism for biotechnological applications. While it has been engineered for the production of numerous fine chemicals like succinate (IL-7 Protein Formulation Litsanov et al., 2012) or isobutanol (Blombach et al., 2011), it can be nonetheless primarily employed for the production of L-amino acids (Becker and Wittmann, 2012). By far the most crucial amino acids are L-glutamate (flavour enhancer) and L-lysine (feed additive) according to production scales (Becker and Wittmann, 2011). In addition, you can find also efforts to create effective producers for other amino acids like L-leucine, L-serine, and L-methionine. These efforts are supported by a detailed insight into the corresponding amino acid biosynthetic pathways and their regulation in C. glutamicum and have been summarized in many testimonials or book chapters (Eggeling and Bott, 2005; Wendisch, 2007; Blombach and Seibold, 2010; Brinkrolf et al., 2010). However, to date there’s no critique offered about L-histidine biosynthesis and its regulation within this amino acid-producing microorganism. Here, we intend to summarize the existing understanding on histidine biosynthesis, its regulation and attempts for application in C. glutamicum. The published information are discusse.