Skip to main content
. 1999 Mar 30;96(7):3562–3567. doi: 10.1073/pnas.96.7.3562

Table 1.

Sequences of active PurN heterodimers

Number N-terminal fragment C-terminal fragment Relative doubling time*
A46 1–72NQ MLGS63–212 1.2 ± 0.1
A36 1–65 MLGS63–212 1.3
A37 1–69VTS MGS63–212 1.3
A43 1–62 MGS63–212 1.3
A47 1–80GVAR M63–212 1.3
A42 1–62 MGS63–212 1.4 ± 0.2
A35 1–74 M63–212 1.4
A38 1–66LTS MLGF63–212 1.4
A39 1–72QRS MLGS63–212 1.5
A44 1–61 MLGS63–212 1.5
A34 1–63LTS M63–212 1.5
B31 1–113 M112–112 1.2
B15 1–114LTS M114–212 1.2
B30 1–112LTS M109–212 1.3
B13 1–111 M114–212 1.4 ± 0.3
B18 1–111 M107–212 1.6
B28 1–118TS M112–212 2.7
B27 1–112A M112–212 5.7
B17 1–112RS M114–212 6.1
WT control 1–212 0.98 ± 0.06
WT control 1–212 1.0 ± 0.02

The amino acid sequences were determined from the DNA sequence of the purN gene fragments. Because proteolytic processing of the fragments may occur (e.g. to shorten overlapping sequences), the exact amino acid sequence of active PurN heterodimers may differ. 

*

The growth rate in minimal media of auxotrophic strain TX680F′ expressing the heterodimers was determined (see Materials and Methods). The doubling time during exponential growth is expressed relative to that of TX680F′ cells expressing the wild-type monomer from phagemid pDIM-C6. TX680F′ bearing control plasmids without any purN gene or with only one gene fragment showed no growth.