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Chapter 55 : Spore Structural Proteins

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Abstract:

Each spore coat and nucleoid structure contains a large amount of protein, with spore coats comprising ~50% and spore nucleoid proteins greater than are equal to 5% of total spore protein; spores of other species have comparable amounts of protein in these two structures. Thus, both spore coat and spore nucleoid components are major spore structural proteins; both types of proteins consist of multiple species coded for by monocistronic genes scattered around the chromosome. Understanding the structure and function of their individual protein components can give insight into spore coat and nucleoid structures. The majority of the spore coat appears to be composed of protein (~50% of total spore protein), although small amounts of lipid should be present in spore coat preparations, since the outer forespore membrane is often extracted with spore coat proteins. The proteins associated with the spore coat and nucleoid are unique both to the spore stage of the life cycle and also to this group of organisms. A number of the spore coat proteins have highly unusual amino acid compositions that may be important in their specific functions in the complex spore coat. α/ β-Type small acid-soluble spore proteins (SASP), on the other hand, do not have unusual amino acid compositions but have properties in vitro that clearly indicate how these proteins function in determining forespore nucleoid structure and properties in vivo.

Citation: Setlow P. 1993. Spore Structural Proteins, p 801-809. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch55

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Figures

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Figure 1

Electron micrograph of a dormant spore of PY79. Sporulation was caused by nutrient exhaustion, and spores were taken at for fixation. Methods for fixation and staining were as described in reference . The outer spore coat (oc), inner spore coat (ic), and spore cortex (cx) layers are noted. Bar for entire spore, 100 nm; bar for enlargement of the coat region, 50 nm.

Citation: Setlow P. 1993. Spore Structural Proteins, p 801-809. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch55
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Image of Figure 2
Figure 2

Primary sequence of SASP. Known amino acid sequences of SASP from and the protein specified by the gene (previously are shown in one-letter code and are taken from references and . The N-terminal methionine in the coding gene is included but is undoubtedly removed posttranslationally. The gene codes for SASP-, codes for SASP-, codes for SspC, and codes for SspD ( ). For the proteins specified by the genes, residues conserved in all known SASP from the line of sporeformers are in boldface type; residues that are similar in these SASP are underlined. A gap has been introduced in these sequences to maximize the alignment with SspF. The large downward-pointing arrow indicates the site of cleavage by the SASP-specific protease ( ). The two upward-pointing arrowheads indicate residues whose alteration in SspC (Gly→Ala or Lys→GIn) reduces or abolishes the ability of this protein to bind DNA in vivo or in vitro ( ). For the protein specified by the gene, residues identical to those conserved in other SASP are in boldface; residues similar to those in other SASP are underlined.

Citation: Setlow P. 1993. Spore Structural Proteins, p 801-809. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch55
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References

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Tables

Generic image for table
Table 1

Properties of spore coat proteins

Citation: Setlow P. 1993. Spore Structural Proteins, p 801-809. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch55
Generic image for table
Table 2

Properties of SASPa

Citation: Setlow P. 1993. Spore Structural Proteins, p 801-809. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch55

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