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. 1985 Aug;163(2):543–551. doi: 10.1128/jb.163.2.543-551.1985

Transcriptional control of synthesis of acid-soluble proteins in sporulating Bacillus subtilis.

W C Johnson, I Mahler, K Phillips, D J Tipper
PMCID: PMC219156  PMID: 3926748

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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