DYNAMICS IN OXYGEN-INDUCED CHANGES IN S-LAYER PROTEIN-SYNTHESIS FROM BACILLUS-STEAROTHERMOPHILUS PV72 AND THE S-LAYER-DEFICIENT VARIANT T5 IN CONTINUOUS-CULTURE AND STUDIES OF THE CELL-WALL COMPOSITION
M. Sara et al., DYNAMICS IN OXYGEN-INDUCED CHANGES IN S-LAYER PROTEIN-SYNTHESIS FROM BACILLUS-STEAROTHERMOPHILUS PV72 AND THE S-LAYER-DEFICIENT VARIANT T5 IN CONTINUOUS-CULTURE AND STUDIES OF THE CELL-WALL COMPOSITION, Journal of bacteriology, 178(7), 1996, pp. 2108-2117
Stable synthesis of the hexagonally ordered (p6) S-layer protein from
the wild-type strain of Bacillus stearothermophilus PV72 could be achi
eved in continuous culture on complex medium only under oxygen-limited
conditions when glucose was used as the sole carbon source. Depending
on the adaptation of the wild-type strain to low oxygen supply, the d
ynamics in oxygen-induced changes in S-layer protein synthesis was dif
ferent when the rate of aeration was increased to a level that allowed
dissimilation of amino acids, If oxygen supply was increased at the b
eginning of continuous culture, synthesis of the p6 S-layer protein fr
om the wild-type strain (encoded by the sbsA gene) was immediately sto
pped and replaced by that of a new type of S-layer protein (encoded by
the sbsB gene) which assembled into an oblique (p2) lattice. In cells
adapted to prolonged low oxygen supply, first, low-level p2 S-layer p
rotein synthesis and second, synchronous synthesis of comparable amoun
ts of both types of S-layer proteins could be induced by stepwise incr
easing the rate of aeration. The time course of changes in S-layer pro
tein synthesis was followed up by immunogold labelling of whole cells.
Synthesis of the p2 S-layer protein could also be induced in the p6-d
eficient variant T5. Hybridization data obtained by applying the radio
labelled N-terminal and C-terminal sbsA fragments and the N-terminal s
bsB fragment to the genomic DNA of all the three organisms indicated t
hat changes in S-layer protein synthesis were accompanied by chromosom
al rearrangement. Chemical analysis of peptidoglycan-containing saccul
i and extraction and recrystallization experiments revealed that at le
ast for the wild-type strain, a cell wall polymer consisting of N-acet
ylglucosamine and glucose is responsible for binding of the p6 S-layer
protein to the rigid cell wall layer.