Purification and characterization of the flagellar basal body of Rhodobacter sphaeroides.
Flagellar hook-basal body (HBB) complexes were purified from Rhodobacter sphaeroides. The HBB was more acid labile but more heat stable than that of Salmonella species, and protein identification revealed that HBB components were expressed only from one of the two sets of flagellar gene clusters on the R. sphaeroides genome, under the heterotrophic growth conditions tested here.
Kobayashi
K
K
Department of Biosciences, Teikyo University, 1-1 Toyosatodai, Utsunomiya 320-8551, Japan.
Saitoh
T
T
Shah
D S H
DS
Ohnishi
K
K
Goodfellow
I G
IG
Sockett
R E
RE
Aizawa
S-I
SI
D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D005407:Flagella / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*; D008854:Microscopy, Electron; D012242:Rhodobacter sphaeroides / Q000235:genetics / Q000254:growth & development / Q000378:metabolism / Q000648:ultrastructure*
D001426:Bacterial Proteins; C035832:hook protein, bacterial flagellum