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dc.contributor.authorJohnson, W. Charles
dc.contributor.authorMahler, Inga
dc.contributor.authorPhillips, Kent
dc.contributor.authorTipper, Donald J.
dc.date2022-08-11T08:09:18.000
dc.date.accessioned2022-08-23T16:26:00Z
dc.date.available2022-08-23T16:26:00Z
dc.date.issued1985-08-01
dc.date.submitted2019-05-17
dc.identifier.citation<p>J Bacteriol. 1985 Aug;163(2):543-51. <a href="https://jb.asm.org/content/163/2/543.long" 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.pmid3926748
dc.identifier.urihttp://hdl.handle.net/20.500.14038/36468
dc.description.abstractThe major acid-soluble spore proteins (ASSPs) isolated from mature spores of Bacillus subtilis are designated alpha, beta, and gamma (about 60, 60, and 100 amino acids in length, respectively). Alpha and beta are very similar, and gamma is very similar to a less predominant ASSP called delta (about 115 amino acids). A minor and very basic ASSP called epsilon is the same size as alpha and beta but is unrelated antigenically. These and several minor ASSPs comprise at least three related families of sporulation-specific gene products. Expression of the alpha and beta genes, detectable as functional mRNA in vitro, coincides with the time of synthesis of all of the major ASSPs in vivo. This apparently coordinate expression is dependent on at least the spo0A, spoIIA, and spoIIIA loci, but not on the spoIVA or spoVA loci, consistent with the late stage of this expression (initiating at 3.5 h after the start of sporulation and peaking at 5 h after start of sporulation). A few minor ASSPs may be asynchronously expressed.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=3926748&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC219156/
dc.rightsCopyright © 1985, 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.subjectacid-soluble spore proteins (ASSPs)
dc.subjectBacillus subtilis
dc.subjectBacteriology
dc.subjectMicrobiology
dc.subjectPhysiology
dc.titleTranscriptional control of synthesis of acid-soluble proteins in sporulating Bacillus subtilis
dc.typeJournal Article
dc.source.journaltitleJournal of bacteriology
dc.source.volume163
dc.source.issue2
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1031&amp;context=maps_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/maps_pubs/32
dc.identifier.contextkey14524105
refterms.dateFOA2022-08-23T16:26:00Z
html.description.abstract<p>The major acid-soluble spore proteins (ASSPs) isolated from mature spores of Bacillus subtilis are designated alpha, beta, and gamma (about 60, 60, and 100 amino acids in length, respectively). Alpha and beta are very similar, and gamma is very similar to a less predominant ASSP called delta (about 115 amino acids). A minor and very basic ASSP called epsilon is the same size as alpha and beta but is unrelated antigenically. These and several minor ASSPs comprise at least three related families of sporulation-specific gene products. Expression of the alpha and beta genes, detectable as functional mRNA in vitro, coincides with the time of synthesis of all of the major ASSPs in vivo. This apparently coordinate expression is dependent on at least the spo0A, spoIIA, and spoIIIA loci, but not on the spoIVA or spoVA loci, consistent with the late stage of this expression (initiating at 3.5 h after the start of sporulation and peaking at 5 h after start of sporulation). A few minor ASSPs may be asynchronously expressed.</p>
dc.identifier.submissionpathmaps_pubs/32
dc.contributor.departmentDepartment of Microbiology and Physiological Systems
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.source.pages543-51


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