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. Author manuscript; available in PMC: 2011 Oct 15.
Published in final edited form as: Cell. 2010 Oct 15;143(2):191–200. doi: 10.1016/j.cell.2010.09.031

Table 1.

Split-inteins commonly used for PTSa

Sizeb Half-
life c
(min)
Comments
IntN IntC
Naturally split inteins
Ssp DnaE 123 36 35–175 One of the better studied and broadly used split inteins. Requires three native extein residues (Cys-Phe-Asn) at the C-terminal junction. IntC is accessible to SPPSd.
Npu DnaE e 102 36 ~1 Most efficient split intein described so far. Active with a broad set of residues at the splicing junction. IntC is accessible to SPPS.

Artificially split inteins
Mtu RecA 105 38 60–120 Reconstitution of the active intein requires co-refolding of previously denatured fragments.
Sce VMA 184 55 6 Requires induced fragment complementation by auxiliary dimerization domains. Has been used to control protein function in conditional protein splicing systems in vivo and in vitro.
Ssp DnaB-S0 f 104 47 12 Active under native conditions. Ser-Gly required at the N-terminal junction.
Ssp DnaB-S1 f 11 143 280 The short IntN is amenable to SPPS and has been used for the labeling of protein N-termini. Same sequence requirements than as DnaB-S0.
Ssp GyrB-S11 f 150 6 170 Active under native conditions. Ser-Ala-Asp used at the N-terminal junction.
a

Ssp: Synechotcystis sp.; Npu: Nostoc punctiforme; Sce: Saccharomyces cerevisiae; Mtu: Mycobacterium tuberculosis. (Mootz, 2009) and references therein.

b

Number of residues.

c

Half-lives calculated from reported first order rate constants.

d

Solid-phase peptide synthesis.

e

Artificial variants of the Npu DnaE, with shorter IntC (15 and 6 residues), have been designed by shifting the split site closer to the C-terminus.

f

S0, S1 and S11 indicate the site at which the intein is split. S0 corresponds to the split site of naturally split inteins.

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