The filamentous bacteriophage assembly proteins require the bacterial SecA protein for correct localization to the membrane.
AUTOR(ES)
Rapoza, M P
RESUMO
The noncapsid assembly proteins pI and pI of the filamentous bacteriophage f1 are inserted into the inner membrane of Escherichia coli via an internal signal sequence. Inhibition of the activity of SecA with low concentrations of sodium azide results in rapid accumulation of pI and pI proteins in the cytoplasm. However, both proteins are inserted into the membrane under the same conditions when synthesized in bacteria containing a secA azide resistance mutation. The other noncapsid assembly protein, pIV, is an outer membrane protein synthesized with a cleavable signal sequence. Wild-type bacteria accumulate the precursor to pIV when protein synthesis is in the presence of low concentrations of sodium azide. These results suggest that the f1 bacteriophage assembly proteins require SecA and consequently the bacterial Sec system to reach their proper membrane location.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=203996Documentos Relacionados
- SecA protein is required for translocation of a model precursor protein into inverted vesicles of Escherichia coli plasma membrane.
- Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane
- A bacterial gene, fip, required for filamentous bacteriophage fl assembly.
- SecA proteins of Bacillus subtilis and Escherichia coli possess homologous amino-terminal ATP-binding domains regulating integration into the plasma membrane.
- Avirulence of rough mutants of Shigella flexneri: requirement of O antigen for correct unipolar localization of IcsA in the bacterial outer membrane.
