title: Cloning, expression and purification of SmpB from Mycobacterium tuberculosis.
abstract: SmpB, a small tmRNA binding protein, is essential for trans-translation. 6His and FLAG tagged SmpB was cloned from Mycobacterium tuberculosis H37Rv. It was expressed in Escherichia coli using the T7 promoter-polymerase system. Anti-FLAG M2 agarose was used for its purification. Mycobacterial SmpB copurifies with other proteins. We identified elongation factor EF-Tu in the purified SmpB preparations.
authors.affiliation: Department of Medical Microbiology and Immunobiology, University of Szeged, PO Box 427, H-6701 Szeged, Szeged, Hungary.
authors.forename: L
authors.initials: L
authors.lastname: Kovács
authors.forename: Klára
authors.initials: K
authors.lastname: Megyeri
authors.forename: Anna
authors.initials: A
authors.lastname: Juhász
authors.forename: Anikó
authors.initials: A
authors.lastname: Zaja
authors.forename: A
authors.initials: A
authors.lastname: Miczák
mesh_terms: D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D009169:Mycobacterium tuberculosis / Q000235:genetics* / Q000378:metabolism; D010444:Peptide Elongation Factor Tu / Q000378:metabolism; D012329:RNA, Bacterial / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D012329:RNA, Bacterial; D016601:RNA-Binding Proteins; C430328:small protein B; C096222:tmRNA; D010444:Peptide Elongation Factor Tu