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PMID:7730292

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Citation

Rivera-León, R, Green, CJ and Vold, BS (1995) High-level expression of soluble recombinant RNase P protein from Escherichia coli. J. Bacteriol. 177:2564-6

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.

Links

PubMed PMC176919

Keywords

Bacterial Proteins/biosynthesis; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Cloning, Molecular; Endoribonucleases/biosynthesis; Endoribonucleases/genetics; Endoribonucleases/isolation & purification; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; RNA Processing, Post-Transcriptional; RNA, Catalytic/biosynthesis; RNA, Catalytic/genetics; RNA, Catalytic/isolation & purification; RNA, Transfer, His/metabolism; Recombinant Proteins/biosynthesis; Recombinant Proteins/isolation & purification; Ribonuclease P

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status


See also

References

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