| Literature DB >> 17221198 |
Ayman El Fiki1, Gamal El Metabteb, Carmen Bellebna, Thomas Wartmann, Rüdiger Bode, Gerd Gellissen, Gotthard Kunze.
Abstract
The yeast Arxula adeninivorans provides an attractive expression platform and can be exploited as gene source for biotechnologically interesting proteins. In the following study, a striking example for the combination of both aspects is presented. The transaldolase-encoding A. adeninivorans ATAL gene, including its promoter and terminator elements, was isolated and characterized. The gene includes a coding sequence of 963 bp encoding a putative 321 amino acid protein of 35.0 kDa. The enzyme characteristics analyzed from isolates of native strains and recombinant strains overexpressing the ATAL gene revealed a molecular mass of ca. 140 kDa corresponding to a tetrameric structure, a pH optimum of ca. 5.5, and a temperature optimum of 20 degrees C. The preferred substrates for the enzyme include D-erythrose-4-phosphate and D-fructose-6-phosphate, whereas D-glyceraldehyde is not converted. The ATAL expression level under salt-free conditions was observed to increase in media supplemented with 5% NaCl rendering the ATAL promoter attractive for moderate heterologous gene expression under high-salt conditions. Its suitability was assessed for the expression of a human serum albumin (HSA) reporter gene.Entities:
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Year: 2007 PMID: 17221198 DOI: 10.1007/s00253-006-0785-8
Source DB: PubMed Journal: Appl Microbiol Biotechnol ISSN: 0175-7598 Impact factor: 4.813