High-level expression of soluble recombinant RNase P protein from Escherichia coli.
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.
Rivera-León
R
R
Syva Company, Palo Alto, California 94304, USA.
Green
C J
CJ
Vold
B S
BS
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
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