title: Expression of Mycoplasma proteins carrying an affinity tag in M. pneumoniae allows rapid purification and circumvents problems related to the aberrant genetic code.
abstract: In Mycoplasma pneumoniae and several other mollicutes, the UGA opal codon specifies tryptophan rather than a translation stop. This often makes it difficult to express Mycoplasma proteins in heterologous hosts. In this work, we demonstrate that mollicute proteins can be fused to an affinity tag and be expressed directly in M. pneumoniae. The protein can then be purified by affinity chromatography and be used for biochemical or any other desired analysis.
authors.affiliation: Department of General Microbiology, Institute of Microbiology and Genetics, Georg-August University Göttingen, Grisebachstr. 8, D-37077 Göttingen, Germany.
authors.forename: Sebastian R
authors.initials: SR
authors.lastname: Schmidl
authors.forename: Claudine
authors.initials: C
authors.lastname: Hames
authors.forename: Jörg
authors.initials: J
authors.lastname: Stülke
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity; D018388:Codon, Terminator / Q000235:genetics; D005815:Genetic Code / Q000235:genetics*; D009174:Mycoplasma / Q000235:genetics*; D009177:Mycoplasma pneumoniae / Q000235:genetics*; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D018388:Codon, Terminator; D011994:Recombinant Proteins