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. 2011 Aug 8;286(39):34440–34447. doi: 10.1074/jbc.M111.277350

TABLE 3.

Contributions of individual mutations to the splicing efficiency at the insertion site 2 in the KanR protein

Mutant inteins Mutationsa Splicing efficiency
%
WT 0
    WT-1 A(−1)G 7

M3 D24G I58T 0
    M3-3 A(−)G D24G I58T 65

M30 A(−)G D24G I58T S18P S107A S122P H143R 98
    M30-6 S18P 0
    M30-7 S107A 0
    M30-8 S122P 0
    M30-9 H143R 0
    M30-1 D24G I58T S18P S107A S122P H143R 71
    M30-2 D24G I58T S18P 22
    M30-3 D24G I58T H143R 38
    M30-4 S18P S107A S122P H143R 15
    M30-5 S107A S122P H143R 6

M86 D24G I58T S18P S107A S122P H143R S114P P142L 93
    M86-1 S18P S107A S122P H143R S114P P142L 11
    M86-2 S107A S122P H143R S114P P142L 20
    M86-3 D24G I58T H143R P142L 0
    M86-4 D24G I58T S107A S114P 0
    M86-5 D24G I58T S107A 0
    M86-6 D24G I58T S114P 0

a The A(−1)G mutation is in the KanR sequence at the position immediately before the intein; all other mutations are relative to the wild type sequence of the Ssp DnaB mini-intein.