The IspA protease's involvement in the regulation of the sporulation process of Bacillus thuringiensis is revealed by proteomic analysis.
We have observed that the process of sporulation of the ispA-deficient mutant was delayed under phase-contrast microscopy. The protein profiles of the ispA-deficient mutant have been analyzed using two-dimensional gel electrophoresis. The results of a proteomic analysis using MALDI-TOF MS indicated that a sporulation-associated protein, pro- [Formula: see text], was upregulated, while two other sporulation-associated proteins, SpoVD and SpoVR, were downregulated in the ispA-deficient mutant. It has been known that pro- [Formula: see text] is a precursor of [Formula: see text] and is required for gene expression related to the late stage of sporulation. Moreover, SpoVD and SpoVR are known to be involved in the formation of the spore cortex. Based on these observations, we propose that the delay in the sporulation process observed in the ispA-deficient mutant may be due to a failure of [Formula: see text] to signal sporulation. This phenomenon may be further enhanced by insufficient amount of SpoVD and SpoVR for cortex formation. In this study, we have revealed for the first time a possible pathway for the regulation of sporulation-associated proteins via IspA.
Chen
Fu-Chu
FC
Institute of Biochemistry, National Yang Ming University, Shih-Pai, Taipei 11221, Taiwan, R.O.C.
Shen
Li-Fen
LF
Tsai
Ming-Chu
MC
Chak
Kin-Fu
KF
D001413:Bacillus thuringiensis / Q000201:enzymology / Q000502:physiology*; D001426:Bacterial Proteins / Q000502:physiology; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D040901:Proteomics / Q000379:methods*; D012697:Serine Endopeptidases / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013171:Spores, Bacterial / Q000254:growth & development*
D001426:Bacterial Proteins; D012697:Serine Endopeptidases