FliI is a key component of the flagellar export apparatus in Salmonella typhimurium. It catalyzes the hydrolysis of ATP which is necessary for flagellar assembly. Affinity blotting experiments showed that purified flagellin and hook protein, two flagellar axial proteins, interact specifically with FliI. The interaction of either of the two proteins with FliI, increases the intrinsic ATPase activity. The presence of either flagellin or hook protein stimulates ATPase activity in a specific and reversible manner. A V-max of 0.12 nmol P-i min(-1) mu g(-1) and a K-m for MgATP of 0.35 mM was determined for the unstimulated FliI; the presence of flagellin increased the V-max to 0.35 nmol P-i min(-1) mu g(-1) and the K-m for MgATP to 1.1 mM. The stimulation induced by the axial proteins was fully reversible suggesting a direct link between the catalytic activity of FliI and the export process. (C) 1999 Elsevier Science B.V. All rights reserved.
Última actualización: 15/12/2017