UMMS Affiliation

Department of Microbiology; Department of Microbiology and Physiological Systems

Publication Date


Document Type



Bacteriology | Biochemistry, Biophysics, and Structural Biology | Cellular and Molecular Physiology


Antibody specific to the 12,200-dalton spore coat protein of Bacillus subtilis was used to detect the synthesis of cross-reacting material during sporulation. Cross-reacting protein was first detected by immunoprecipitation after 4 h of development and represented at least 1 to 2% of the total soluble protein synthesis at 5.5 h. A polypeptide of 21,000 daltons was detected in immunoprecipitates by gel electrophoresis. This polypeptide did not accumulate in sporulating cells and was rapidly turned over at the time of coat deposition. In contrast, a 32,000-dalton polypeptide reacted with antibody when unlabeled cell protein was denatured with sodium dodecyl sulfate, separated by gel electrophoresis, and transferred to nitrocellulose paper. This polypeptide was not detected during cell growth or the first 3.5 h of development but was found to accumulate in sporulating cells at 5.5 h. The lack of detection of this polypeptide by immunoprecipitation of undenatured protein indicates that the antigenic sites which cross-reacted with antibody to the 12,200-dalton protein sequence were not exposed unless the molecular conformation was altered. The 32,000-dalton protein may be a primary translation product which is proteolytically processed into mature spore coat protein via a 21,000-dalton intermediate.


Bacillus subtilis, proteins

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Copyright © 1981, American Society for Microbiology. Publisher PDF posted as allowed by the publisher's copyright policy at


J Bacteriol. 1981 Sep;147(3):1040-8. Link to article on publisher's site

Journal/Book/Conference Title

Journal of bacteriology

Related Resources

Link to Article in PubMed

PubMed ID