Assembly of multiple CotC forms into the Bacillus subtilis spore coat.
We report evidence that the CotC polypeptide, a previously identified component of the Bacillus subtilis spore coat, is assembled into at least four distinct forms. Two of these, having molecular masses of 12 and 21 kDa, appeared 8 h after the onset of sporulation and were probably assembled on the forming spore immediately after their synthesis, since no accumulation of either of them was detected in the mother cell compartment, where their synthesis occurs. The other two components, 12.5 and 30 kDa, were generated 2 h later and were probably the products of posttranslational modifications of the two early forms occurring directly on the coat surface during spore maturation. None of the CotC forms was found either on the spore coat or in the mother cell compartment of a cotH mutant. This indicates that CotH serves a dual role of stabilizing the early forms of CotC and promoting the assembly of both early and late forms on the spore surface.
Isticato
Rachele
R
Dipartimento di Fisiologia Generale ed Ambientale, Università Federico II, Naples, Italy.
Esposito
Giovanni
G
Zilhão
Rita
R
Nolasco
Sofia
S
Cangiano
Giuseppina
G
De Felice
Maurilio
M
Henriques
Adriano O
AO
Ricca
Ezio
E
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013171:Spores, Bacterial / Q000737:chemistry* / Q000502:physiology; D020798:Two-Hybrid System Techniques
D001426:Bacterial Proteins; C077494:CotE protein, Bacillus subtilis; C101016:CotH protein, Bacillus subtilis