Depletion of Bacillus subtilis histone-like protein, HBsu, causes defective protein translocation and induces upregulation of small cytoplasmic RNA.
Biochem Biophys Res Commun
; 258(1): 211-4, 1999 Apr 29.
Article
en En
| MEDLINE
| ID: mdl-10222262
ABSTRACT
Small cytoplasmic RNA (scRNA) is a metabolically stable homologue of mammalian SRP RNA that contains an Alu-like domain. The Bacillus subtilis histone-like protein HBsu can bind this domain. We demonstrate here that repressing the level of HBsu results in slow growth and the accumulation of precursor of beta-lactamase fusion proteins having the signal sequence of alkaline protease, penicillin binding protein 5* (PBP5*) or CGTase. The degree of the translocation defect varied among the various signal sequences tested. A pulse-chase experiment showed that processing the alpha-amylase signal sequence is significantly inhibited in HBsu-depleted cells. Northern blot analysis indicated that repressing the HBsu gene induces scRNA upregulation, indicating that the defective translocation of presecretory proteins is not due to a reduced scRNA level. The data presented here suggest that HBsu plays a pivotal role in SRP function rather than simply stabilizing the other SRP components such as scRNA.
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Banco de datos:
MEDLINE
Asunto principal:
Bacillus subtilis
/
Proteínas Bacterianas
/
ARN
/
Regulación hacia Arriba
/
Proteínas de Unión al ADN
Tipo de estudio:
Etiology_studies
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
1999
Tipo del documento:
Article
País de afiliación:
Japón