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. 2014 Sep 8;289(44):30343–30354. doi: 10.1074/jbc.M114.598656

TABLE 4.

Features of the purified PilF complexes and phenotypes of the T. thermophilus pilF mutants

NA, not applicable.

Strain/protein Zinc per hexamera ATPase activityb Complex formationc Thermostabilityd
Piliatione
Adherencef
Twitching motilityf
Transformation frequencyg
Unfolding (t1) Unfolding (t2) 55 °C 64 °C 72 °C 55 °C 64 °C 72 °C 55 °C 64 °C 72 °C
milliunits/mg °C
HB27 NA NA NA NA NA ++ + + ++ + + + + + +
ΔpilF::bleo NA NA NA NA NA
Wild type 6.03 54.00 + 80.8 90.5 ++ + + ++ + + + + + +
C1A 5.65 46.32 + 78.6 91.0 +++ +/− + +/− + +/− +
C2A 5.16 49.86 + 71.6 91.2 ++ + + + + + +
HC2A 5.28 49.27 + 72.8 90.8 ++ + + + + + +
C3A 5.67 46.84 + 73.9 90.6 + +/− + +/− + +/− +
C4A 4.73 52.62 + 70.0 90.9 + +++
2CysA 1.26 53.16 + 65.4 90.6 +++ + + +
3CysA 0.86 46.84 + 65.5 90.3 +++ + + +
4CysA 0.28 48.25 + 66.3 90.7 +++ + + +

a Zinc content was analyzed by ICP-MS.

b ATPase activity of PilF variants was analyzed by the method described by Heinonen and Lahti (21).

c Complex formation of purified PilF proteins was analyzed by calibrated size exclusion chromatography.

d Thermostability was measured via thermofluor assays.

e Piliation was analyzed by electron microscopy (250 cells).

f Adherence was measured in microtiter adhesion assays. Twitching motility was analyzed on MM containing 1% BSA.

g Transformation frequencies were calculated as transformants per living count. +, wild-type phenotype; ++, increase compared to the wild-type; +++, strong increase compared to the wild-type; +/−, decrease compared to the wild-type; −, lack of the analyzed feature.