Protease susceptibility of the Caulobacter crescentus flagellar hook–basal body: a possible mechanism of flagellar ejection during cell differentiation
When motile swarmer cells of Caulobacter crescentus differentiate into sessile stalked cells, the flagellum is ejected. To elucidate the molecular mechanism of the flagellar ejection, flagellar hook–basal body (HBB) complexes from C. crescentus were purified and characterized. The purified HBBs were less stable against acidic pH or protease treatment than HBBs of Salmonella typhimurium, supporting the view that flagellar ejection from C. crescentus is initiated by destruction of the fragile basal structures. In addition, protease treatment of the purified flagella resulted in the specific digestion of the MS ring complex, revealing for the first time the intact structure of the whole rod.
AizawaS.-I.,
DeanG. E.,
JonesC. J.,
MacnabR. M.,
YamaguchiS.
1985; Purification and characterization of the flagellar hook-basal body complex of Salmonella typhimurium
. J Bacteriol 161:836–849
AldridgeP.,
JenalU.
1999; Cell cycle-dependent degradation of a flagellar motor component requires a novel-type response regulator. Mol Microbiol 32:379–391[CrossRef]
AldridgeP.,
PaulR.,
GoymerP.,
RaineyP.,
JenalU.
2003; Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus. Mol Microbiol 47:1695–1708[CrossRef]
DePamphilisM. L.,
AdlerJ.
1971; Fine structure and isolation of the hook-basal body complex of flagella from Escherichia coli and Bacillus subtilis
. J Bacteriol 105:384–395
ElyB.,
ElyT. W.,
CrymesW. B.Jr, MinnichS. A.
2000; A family of six flagellin genes contributes to the Caulobacter crescentus flagellar filament. J Bacteriol 182:5001–5004[CrossRef]
JenalU.,
ShapiroL.
1996; Cell cycle-controlled proteolysis of a flagellar motor protein that is asymmetrically distributed in the Caulobacter predivisional cell. EMBO J 15:2393–2406
JuddE. M.,
RyanK. R.,
MoernerW. E.,
ShapiroL.,
McAdamsH. H.
2003; Fluorescence bleaching reveals asymmetric compartment formation prior to cell division in Caulobacter. Proc Natl Acad Sci U S A 100:8235–8240[CrossRef]
KobayashiK.,
SaitohT.,
ShahD. S. H.,
OhnishiK.,
GoodfellowI. G.,
SockettR. E.,
AizawaS.-I.
2003; Purification and characterization of the flagellar basal body of Rhodobacter sphaeroides
. J Bacteriol 185:5295–5300[CrossRef]
KuboriT.,
OkumuraM.,
KobayashiN.,
NakamuraD.,
IwakuraM.,
AizawaS.-I.
1997; Purification and characterization of the flagellar hook-basal body complex of Bacillus subtilis. Mol Microbiol 24:399–410[CrossRef]
SchoenhalsG. L.,
MacnabR. M.
1996; Physiological and biochemical analysis of FlgH, a lipoprotein forming the outer membrane L ring of the flagellar basal body of Salmonella typhimurium
. J Bacteriol 178:4200–4207
StallmeyerM. J. B.,
HahnenbergerK.,
SosinskyG. E.,
ShapiroL.,
DeRosierD. J.
1989; Image reconstruction of the flagellar basal body of Caulobacter crescentus
. J Mol Biol 205:511–518[CrossRef]
StephensC.,
ReisenauerA.,
WrightR.,
ShapiroL.
1996; A cell cycle-regulated bacterial DNA methyltransferase is essential for viability. Proc Natl Acad Sci U S A 93:1210–1214[CrossRef]
UenoT.,
OosawaK.,
AizawaS.-I.
1992; The M ring, S ring and proximal rod of the flagellar basal body of Salmonella typhimurium are composed of subunits of a single protein. FliF. J Mol Biol 227:672–677[CrossRef]
UenoT. K.,
Oosawa,
AizawaS.-I.
1994; Domain structures of the MS ring component protein (FliF) of the flagellar basal body of. Salmonella typhimurium J Mol Biol 235:546–555
Protease susceptibility of the Caulobacter crescentus flagellar hook–basal body: a possible mechanism of flagellar ejection during cell differentiation