title: Protein splicing of the three Pyrococcus abyssi ribonucleotide reductase inteins.
abstract: An intein is a polypeptide that interrupts the functional domains of a protein, called the exteins. The intein can facilitate its own excision from the exteins, concomitant with the ligation of the exteins, in a process called protein splicing. The alpha subunit of the ribonucleotide reductase of the extreme thermophile Pyrococcus abyssi is interrupted by three inteins in separate insertion sites. Each intein can facilitate protein splicing when over-expressed in Escherichia coli, with affinity domains serving as the exteins. The influence of the N-terminal flanking residue on the efficiency of splicing is specific to each intein. Each intein has a different downstream nucleophilic residue, and cannot tolerate substitution to a residue of lesser or equal nucleophilicity. The influence of the conserved penultimate His also differs between the inteins.
authors: Department of Chemistry, College of the Holy Cross, Worcester, MA 01610, USA.
authors: Adam M
authors: AM
authors: Kerrigan
authors: Taryn L
authors: TL
authors: Powers
authors: Deirdre M
authors: DM
authors: Dorval
authors: Julie N
authors: JN
authors: Reitter
authors: Kenneth V
authors: KV
authors: Mills
mesh_terms: D047668:Inteins; D019154:Protein Splicing; D043903:Pyrococcus abyssi / Q000201:enzymology*; D012264:Ribonucleotide Reductases / Q000378:metabolism*
chemical_list: D012264:Ribonucleotide Reductases