title: Protein-protein fusion catalyzed by sortase A.
abstract: Chimeric proteins boast widespread use in areas ranging from cell biology to drug delivery. Post-translational protein fusion using the bacterial transpeptidase sortase A provides an attractive alternative when traditional gene fusion fails. We describe use of this enzyme for in vitro protein ligation and report the successful fusion of 10 pairs of protein domains with preserved functionality--demonstrating the robust and facile nature of this reaction.
authors.affiliation: Department of Physics, Harvard University, Cambridge, Massachusetts, United States of America.
authors.forename: David A
authors.initials: DA
authors.lastname: Levary
authors.forename: Ranganath
authors.initials: R
authors.lastname: Parthasarathy
authors.forename: Eric T
authors.initials: ET
authors.lastname: Boder
authors.forename: Margaret E
authors.initials: ME
authors.lastname: Ackerman
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019881:Aminoacyltransferases / Q000737:chemistry / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D055162:Biocatalysis; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D057809:HEK293 Cells; D006801:Humans; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D019881:Aminoacyltransferases; C120542:sortase A; D003546:Cysteine Endopeptidases