Nucleotide sequence of the sspE genes coding for γ-type small, acid-soluble spore proteins from the round-spore-forming bacteria Bacillus aminovorans, Sporosarcina halophila and S. ureae

Loshon, Charles A.; Beary, Katherine E.; Gouveia, Kristine; Grey, Elizabeth; Santiago-Lara, Leticia M.; Setlow, Peter

doi:10.1016/s0167-4781(97)00204-2

Cited by 3 publications

(8 citation statements)

References 18 publications

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“…1) (18,25,34), showed that ␥-type SASP exhibit some conserved sequences but are most notable for the following characteristics: (i) a significant enrichment of Gln and Asn (8-and 6-fold enriched with respect to normal frequencies in the proteomes of Paenibacillus sp. JDR-2 and Alicyclobacillus acidocaldarius [ϳ0.036 and 0.105, respectively]); (ii) very low levels of hydrophobic residues, with substantially lower hydrophobic residue abundances in ␥-type SASP, although these residues tend to be less naturally abundant in general (e.g., levels of L, I, and P are, respectively, 3, 2.5, and 1.8 standard deviations below proteomic backgrounds); and (iii) 1 to 3 repeats of the relatively well-conserved TEFASET GPR cleavage site, although the spacing between these last conserved sequences varies considerably (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…In particular, these proteins exhibit two 18-to 19-aa regions of a highly conserved sequence that are commonly separated by a 3-aa spacer (Fig. 2, red For species whose abbreviations are underlined, the amino acid sequences were from the sspE gene cloned from this species (18,25,33); all other sequences were from the species' completed genome sequences. The seven-residue sequences shaded in red are the sites for recognition and cleavage by the SASP-specific protease GPR during spore outgrowth, with cleavage between the bold residues (29,32).…”

Section: Resultsmentioning

confidence: 99%

“…The final tree (Fig. 5) includes the spore-forming Bacillales species with completed genomes, as well as those shown previously to contain an sspE gene, even though these species' genomes have not been sequenced (18,25,34), as well as members of other Firmicutes genera and species. Importantly, members of one such genus, Thermoactinomyces, are highly dissimilar to other Firmicutes and have very few closely matching neighbors.…”

Section: Discussionmentioning

confidence: 99%

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Extremely Variable Conservation of -Type Small, Acid-Soluble Proteins from Spores of Some Species in the Bacterial Order Bacillales

Vyas¹,

Cox²,

Setlow³

et al. 2011

Journal of Bacteriology

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␥-Type small, acid-soluble spore proteins (SASP) are the most abundant proteins in spores of at least some members of the bacterial order Bacillales, yet they remain an enigma from both functional and phylogenetic perspectives. Current work has shown that the ␥-type SASP or their coding genes (sspE genes) are present in most spore-forming members of Bacillales, including at least some members of the Paenibacillus genus, although they are apparently absent from Clostridiales species. We have applied a new method of searching for sspE genes, which now appear to also be absent from a clade of Bacillales species that includes Alicyclobacillus acidocaldarius and Bacillus tusciae. In addition, no ␥-type SASP were found in A. acidocaldarius spores, although several of the DNA-binding ␣/␤-type SASP were present. These findings have elucidated the phylogenetic origin of the sspE gene, and this may help in determining the precise function of ␥-type SASP.Bacterial spores of species of the Firmicutes phylum contain a number of small, acid-soluble proteins (SASP) that comprise 10 to 15% of the protein in the spore's central region or core (30, 32). The following two types of major SASP have been identified in spores: (i) ␣/␤-type SASP that are products of a multi-ssp gene family and have extremely similar sequences both within and across species and (ii) ␥-type SASP that are almost always encoded by a single sspE gene; this is the most abundant protein found in spores of a number of species and comprises 5 to 8% of total spore protein (18-20, 29-32, 39). In contrast to the highly conserved sequences of ␣/␤-type SASP, sequences of ␥-type SASP are not well conserved across species, and this has allowed the use of sspE and SASP-␥ sequences to distinguish closely related Bacillus strains and species (17).In Bacillus subtilis, genes encoding both ␣/␤-type and ␥-type SASP are transcribed in parallel late in spore development when the various SASP are synthesized, and the transcription of ssp genes is mediated by the RNA polymerase sigma factor, G (22). The SASP are degraded soon after spores complete the germination process and begin outgrowth, and one function of these proteins is to serve as a reservoir of amino acids (aa) for protein synthesis early in outgrowth (12,30,32). The latter is an important function, since spores become deficient in a number of amino acid biosynthetic enzymes during spore formation and synthesize these enzymes only during spore outgrowth. In addition to serving as a reservoir of amino acids, the ␣/␤-type SASP have an additional function, as these proteins saturate spore DNA and protect it from many types of damage and are thus very important for long-term spore survival (30-32). However, other than serving as an amino acid reservoir, no additional function has been demonstrated for ␥-type SASP (12, 30, 32).In the current work, we have examined genome sequence information for spore-forming Firmicutes and have confirmed that (i) spore-forming Clostridiales species appear to lack sspE genes; (ii) most bu...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Extremely Variable Conservation of -Type Small, Acid-Soluble Proteins from Spores of Some Species in the Bacterial Order Bacillales

Vyas¹,

Cox²,

Setlow³

et al. 2011

Journal of Bacteriology

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“…In contrast to their multiple α / β ‐type SASP, spores of Bacillus species contain only a single γ ‐type SASP that comprises ca . 40% of total SASP (Hackett and Setlow 1988; Setlow 1988; Loshon et al. 1998).…”

Section: Introductionmentioning

confidence: 99%

Studies on the mechanism of the osmoresistance of spores of Bacillus subtilis

et al. 2003

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Aims: To determine the reason that spores of Bacillus species, in particular Bacillus subtilis, are able to form colonies with high efficiency on media with very high salt concentrations. Methods and Results: Spores of various Bacillus species have a significantly higher plating efficiency on media with high salt concentration (termed osmoresistance) than do log or stationary phase cells. This spore osmoresistance is higher on richer media. Bacillus subtilis spores lacking various small, acid-soluble spore proteins (SASP) were generally significantly less osmoresistant than were wild-type spores, as shown previously (Ruzal et al. 1994). Other results included: (a) spore osmoresistance varied significantly between species; (b) the osmoresistance of spores lacking SASP was not restored well by amino acid osmolytes added to plating media, but was completely restored by glucose; (c) the osmoresistance of spores lacking SASP was restored upon brief germination in the absence of salt in a process that did not require protein synthesis; (d) significant amounts of amino acids generated by SASP degradation were retained within spores upon germination in a medium with high but not low salt; (e) slowing but not abolishing SASP degradation by loss of the SASP-specific germination protease (GPR) did not affect spore osmoresistance; (f) sporulation at higher temperatures produced less osmoresistant spores; and (g) spore osmoresistance was not decreased markedly by the absence of the stress sigma factor for RNA polymerase, r B . Conclusions: Spore osmoresistance appears as a result of three major factors: (1) specific characteristics of spores and cells of individual species; (2) the precise sporulation conditions that produce the spores; and (3) sufficient energy generation by the germinating and outgrowing spore to allow the spore to adapt to conditions of high osmotic strength; the substrates for this energy generation can come from either the endogenous generation of amino acids by SASP degradation or from the spore's environment, in the form of a readily taken up and metabolized energy source such as glucose. Signficance and Impact of Study: These results provide information on the mechanisms of spore osmoresistance, a spore property that can be of major applied significance given the use of high osmotic strength with or without high salt as a means of food preservation.

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“…A few studies targeted the analysis of the mechanism of spore formation (Loshon et al, 1998) and the production of urease (urea amidohydrolase; E.C. 3.5.1.5) by ureaseproducing species such as S. ureae (McCoy et al, 1992) and S. pasteuri (Achal et al, 2009b).…”

Section: Bacterial Isolation and Identificationmentioning

confidence: 99%

Bioconversion of l-arabinose and other carbohydrates from plant cell walls to α-glucan by a soil bacterium, Sporosarcina sp. N52

Zhang

Srichuwong

Kobayashi

et al. 2010

Bioresource Technology

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Nucleotide sequence of the sspE genes coding for γ-type small, acid-soluble spore proteins from the round-spore-forming bacteria Bacillus aminovorans, Sporosarcina halophila and S. ureae

Cited by 3 publications

References 18 publications

Extremely Variable Conservation of -Type Small, Acid-Soluble Proteins from Spores of Some Species in the Bacterial Order Bacillales

Extremely Variable Conservation of -Type Small, Acid-Soluble Proteins from Spores of Some Species in the Bacterial Order Bacillales

Studies on the mechanism of the osmoresistance of spores of Bacillus subtilis

Bioconversion of l-arabinose and other carbohydrates from plant cell walls to α-glucan by a soil bacterium, Sporosarcina sp. N52

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