title: High-level expression of soluble recombinant RNase P protein from Escherichia coli.
abstract: We have expressed recombinant RNase P protein from Escherichia coli in high yield. A hexahistidine sequence at the amino terminus allowed protein purification in a single step. Mass spectrometry confirmed the molecular weight of the purified protein and indicated a purity of > 95%. Protein functionality was demonstrated by reconstitution of active holoenzyme.
authors.affiliation: Syva Company, Palo Alto, California 94304, USA.
authors.forename: R
authors.initials: R
authors.lastname: Rivera-León
authors.forename: C J
authors.initials: CJ
authors.lastname: Green
authors.forename: B S
authors.initials: BS
authors.lastname: Vold
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D004722:Endoribonucleases / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins; D012323:RNA Processing, Post-Transcriptional; D016337:RNA, Catalytic / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification; D012354:RNA, Transfer, His / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification; D043262:Ribonuclease P
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D016337:RNA, Catalytic; D012354:RNA, Transfer, His; D011994:Recombinant Proteins; D004722:Endoribonucleases; D043262:Ribonuclease P; C470865:ribonuclease P, E coli