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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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kerrigan AM,Powers TL,Dorval DM,Reitter JN,Mills KV

doi

10.1016/j.bbrc.2009.06.145

subject

Has Abstract

pub_date

2009-09-11 00:00:00

pages

153-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)01312-6

journal_volume

387

pub_type

杂志文章

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