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dc.contributor.authorGoldman, Robert C.
dc.contributor.authorTipper, Donald J.
dc.date2022-08-11T08:09:18.000
dc.date.accessioned2022-08-23T16:26:04Z
dc.date.available2022-08-23T16:26:04Z
dc.date.issued1981-09-01
dc.date.submitted2019-06-17
dc.identifier.citation<p>J Bacteriol. 1981 Sep;147(3):1040-8. <a href="https://jb.asm.org/content/147/3/1040" target="_blank" title="Link to article on publisher's site">Link to article on publisher's site</a></p>
dc.identifier.issn0021-9193 (Linking)
dc.identifier.pmid6792184
dc.identifier.urihttp://hdl.handle.net/20.500.14038/36484
dc.description.abstractAntibody 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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=6792184&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rightsCopyright © 1981, American Society for Microbiology. Publisher PDF posted as allowed by the publisher's copyright policy at https://journals.asm.org/content/copyright-transfer-and-supplemental-material-license-agreement-2017.
dc.subjectBacillus subtilis
dc.subjectproteins
dc.subjectBacteriology
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectCellular and Molecular Physiology
dc.titleCoat protein synthesis during sporulation of Bacillus subtilis: immunological detection of soluble precursors to the 12,200-dalton spore coat protein
dc.typeJournal Article
dc.source.journaltitleJournal of bacteriology
dc.source.volume147
dc.source.issue3
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1047&amp;context=maps_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/maps_pubs/47
dc.identifier.contextkey14751700
refterms.dateFOA2022-08-23T16:26:04Z
html.description.abstract<p>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.</p>
dc.identifier.submissionpathmaps_pubs/47
dc.contributor.departmentDepartment of Microbiology and Physiological Systems
dc.contributor.departmentDepartment of Microbiology
dc.source.pages1040-8


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