"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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Detalles Bibliográficos
Autores principales: Ruzal, S.M., Bustos, P.L., Sánchez-Rivas, C.
Formato: JOUR
Materias:
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
bacterial gene
bacterium colony
controlled study
genetic complementation
nonhuman
phenotype
plasmid
protein determination
protein function
spore germination
sspE gene
wild type
Bacterial Proteins
Gene Deletion
Genetic Complementation Test
Protein Multimerization
Spores, Bacterial
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_10177825_v23_n1_p15_Ruzal
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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.

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