The Agrobacterium tumefaciens T pilus composed of cyclic T pilin is highly resilient to extreme environments.
Agrobacterium tumefaciens T pili are long semi-rigid, flexuous filaments of 10 nm diameter that are primarily composed of T pilin cyclized protein subunits. The cyclic character of T pilin apparently confers a high level of structural stability on the T pilus. Purified T pili subjected to extreme environmental conditions such as acid and alkali, including glycerol remained relatively unaffected morphologically. T pili lost their semi-rigidity when subjected to high temperatures and high pH, and dissociated into donut shaped subunits when exposed to Triton X-100. Sodium dodecyl sulfate increased the uptake of uranyl acetate exposing a 2 nm wide lumen running the length of the T pilus filament.
Lai
Erh-Min
EM
Davis Crown Gall Group, University of California, One Shields Avenue, Davis 95616, USA.
Kado
Clarence I
CI
D016960:Agrobacterium tumefaciens / Q000235:genetics / Q000502:physiology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D036781:Fimbriae Proteins; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D018933:Pili, Sex / Q000737:chemistry* / Q000502:physiology*
D001426:Bacterial Proteins; D008565:Membrane Proteins; D036781:Fimbriae Proteins