"A La Recherche" of functions for the spore protein SASP-E from Bacillus subtilis
We previously observed that Bacillus subtilis spores from sspE mutants presented a lower germination capacity in media containing high salt concentrations (0. 9 M NaCl). This deficiency was attributed to the absence of SASP-E (gamma-type small-acid-soluble protein), rich in osmocompatible amino acid...
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todo:paper_10177825_v23_n1_p15_Ruzal2023-10-03T15:56:24Z "A La Recherche" of functions for the spore protein SASP-E from Bacillus subtilis Ruzal, S.M. Bustos, P.L. Sánchez-Rivas, C. Bacillus subtilis Coat Germination SASP-E Spores asparagine bacterial protein calcium dipicolinic acid fructose gamma type small acid soluble protein glucose hexadecane potassium chloride unclassified drug article autofluorescence Bacillus subtilis bacterial gene bacterium colony controlled study genetic complementation nonhuman phenotype plasmid protein determination protein function spore germination sspE gene wild type Bacillus subtilis Bacterial Proteins Gene Deletion Genetic Complementation Test Protein Multimerization Spores, Bacterial We previously observed that Bacillus subtilis spores from sspE mutants presented a lower germination capacity in media containing high salt concentrations (0. 9 M NaCl). This deficiency was attributed to the absence of SASP-E (gamma-type small-acid-soluble protein), rich in osmocompatible amino acids released by degradation. Herein we observed that, in addition, this mutant spore presented a reduced capacity to use L-alanine as germinant (L-ala pathway), required longer times to germinate in calcium dipicolinate (Ca2+-DPA), but germinated well in asparagine, glucose, fructose, and potassium chloride (AGFK pathway). Moreover, mild sonic treatment of mutant spores partially recovered their germination capacity in L-ala. Spore qualities were also altered, since sporulating colonies from the sspE mutant showed a pale brownish color, a higher adherence to agar plates, and lower auto-fluorescence, properties related to their spore coat content. Furthermore, biochemical analysis showed a reduced partition in hexadecane and a higher content of Ca2+-DPA when compared with its isogenic wild-type control. Coat protein preparations showed a different electrophoretic pattern, in particular when detected with antibodies against CotG and CotE. The complementation with a wild-type sspE gene in a plasmid allowed for recovering the wild-type coat phenotype. This is the first report of a direct involvement of SASP-E in the spore coat assembly during the differentiation program of sporulation. © the Korean Society for Microbiology and Biotechnology. Fil:Ruzal, S.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_10177825_v23_n1_p15_Ruzal |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Bacillus subtilis Coat Germination SASP-E Spores asparagine bacterial protein calcium dipicolinic acid fructose gamma type small acid soluble protein glucose hexadecane potassium chloride unclassified drug article autofluorescence Bacillus subtilis bacterial gene bacterium colony controlled study genetic complementation nonhuman phenotype plasmid protein determination protein function spore germination sspE gene wild type Bacillus subtilis Bacterial Proteins Gene Deletion Genetic Complementation Test Protein Multimerization Spores, Bacterial |
| spellingShingle |
Bacillus subtilis Coat Germination SASP-E Spores asparagine bacterial protein calcium dipicolinic acid fructose gamma type small acid soluble protein glucose hexadecane potassium chloride unclassified drug article autofluorescence Bacillus subtilis bacterial gene bacterium colony controlled study genetic complementation nonhuman phenotype plasmid protein determination protein function spore germination sspE gene wild type Bacillus subtilis Bacterial Proteins Gene Deletion Genetic Complementation Test Protein Multimerization Spores, Bacterial Ruzal, S.M. Bustos, P.L. Sánchez-Rivas, C. "A La Recherche" of functions for the spore protein SASP-E from Bacillus subtilis |
| topic_facet |
Bacillus subtilis Coat Germination SASP-E Spores asparagine bacterial protein calcium dipicolinic acid fructose gamma type small acid soluble protein glucose hexadecane potassium chloride unclassified drug article autofluorescence Bacillus subtilis bacterial gene bacterium colony controlled study genetic complementation nonhuman phenotype plasmid protein determination protein function spore germination sspE gene wild type Bacillus subtilis Bacterial Proteins Gene Deletion Genetic Complementation Test Protein Multimerization Spores, Bacterial |
| description |
We previously observed that Bacillus subtilis spores from sspE mutants presented a lower germination capacity in media containing high salt concentrations (0. 9 M NaCl). This deficiency was attributed to the absence of SASP-E (gamma-type small-acid-soluble protein), rich in osmocompatible amino acids released by degradation. Herein we observed that, in addition, this mutant spore presented a reduced capacity to use L-alanine as germinant (L-ala pathway), required longer times to germinate in calcium dipicolinate (Ca2+-DPA), but germinated well in asparagine, glucose, fructose, and potassium chloride (AGFK pathway). Moreover, mild sonic treatment of mutant spores partially recovered their germination capacity in L-ala. Spore qualities were also altered, since sporulating colonies from the sspE mutant showed a pale brownish color, a higher adherence to agar plates, and lower auto-fluorescence, properties related to their spore coat content. Furthermore, biochemical analysis showed a reduced partition in hexadecane and a higher content of Ca2+-DPA when compared with its isogenic wild-type control. Coat protein preparations showed a different electrophoretic pattern, in particular when detected with antibodies against CotG and CotE. The complementation with a wild-type sspE gene in a plasmid allowed for recovering the wild-type coat phenotype. This is the first report of a direct involvement of SASP-E in the spore coat assembly during the differentiation program of sporulation. © the Korean Society for Microbiology and Biotechnology. |
| format |
JOUR |
| author |
Ruzal, S.M. Bustos, P.L. Sánchez-Rivas, C. |
| author_facet |
Ruzal, S.M. Bustos, P.L. Sánchez-Rivas, C. |
| author_sort |
Ruzal, S.M. |
| title |
"A La Recherche" of functions for the spore protein SASP-E from Bacillus subtilis |
| title_short |
"A La Recherche" of functions for the spore protein SASP-E from Bacillus subtilis |
| title_full |
"A La Recherche" of functions for the spore protein SASP-E from Bacillus subtilis |
| title_fullStr |
"A La Recherche" of functions for the spore protein SASP-E from Bacillus subtilis |
| title_full_unstemmed |
"A La Recherche" of functions for the spore protein SASP-E from Bacillus subtilis |
| title_sort |
"a la recherche" of functions for the spore protein sasp-e from bacillus subtilis |
| url |
http://hdl.handle.net/20.500.12110/paper_10177825_v23_n1_p15_Ruzal |
| work_keys_str_mv |
AT ruzalsm alarechercheoffunctionsforthesporeproteinsaspefrombacillussubtilis AT bustospl alarechercheoffunctionsforthesporeproteinsaspefrombacillussubtilis AT sanchezrivasc alarechercheoffunctionsforthesporeproteinsaspefrombacillussubtilis |
| _version_ |
1807318690292563968 |