Insertional Mutation of ftsH Gene in Streptococcus pneumoniae Causes Stress Sensitivities
Journal of Bacteriology and Virology
;
: 9-18, 2004.
Artículo
en Coreano
| WPRIM
| ID: wpr-144802
ABSTRACT
FtsH is a membrane-bound, ATP-dependent protease involved in various cellular functions. To understand its roles in Streptococcus pneumoniae and host-pathogen interactions, we inactivated the ftsH gene of D39 strain by inserting a tetracycline-resistance (tet) gene. Several recombinants containing the tet cassette within the ftsH gene were confirmed by Western immunoblotting for the absence of pneumococcal FtsH protein that could cross-react with antiserum raised against Escherichia coli FtsH. Compared with the wild-type D39 strain, the ftsH null mutants grew slowly with encapsulation and alpha-hemolysis on blood agar plates, but failed to grow in liquid media other than Todd Hewitt yeast extract broth. Even fresh cultures of ftsH null mutants appeared gram-negative. When the incubation temperature of liquid cultures was shifted from 37degrees C to 40degrees C, the mutants gradually lysed, whereas the shift to 30degrees C abolished further growth. The mutants also exhibited increased sensitivity to salt and remarkable growth inhibition by optochin. These observations suggest that no functional FtsH protein in pneumococcal cells causes a loss of cell surface integrity, resulting in impairment of cell growth under normal and stressful conditions.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Streptococcus
/
Streptococcus pneumoniae
/
Levaduras
/
Western Blotting
/
Agar
/
Proteasas ATP-Dependientes
/
Escherichia coli
/
Interacciones Huésped-Patógeno
Tipo de estudio:
Estudio diagnóstico
/
Estudio de etiología
Idioma:
Coreano
Revista:
Journal of Bacteriology and Virology
Año:
2004
Tipo del documento:
Artículo
Similares
MEDLINE
...
LILACS
LIS