Cargando…
Recognition of secretory proteins in Escherichia coli requires signals in addition to the signal sequence and slow folding
BACKGROUND: The Sec-dependent protein export apparatus of Escherichia coli is very efficient at correctly identifying proteins to be exported from the cytoplasm. Even bacterial strains that carry prl mutations, which allow export of signal sequence-defective precursors, accurately differentiate betw...
Autores principales: | Mallik, Ipsita, Smith, Margaret A, Flower, Ann M |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2002
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC137694/ https://www.ncbi.nlm.nih.gov/pubmed/12427258 http://dx.doi.org/10.1186/1471-2180-2-32 |
Ejemplares similares
-
Effect of Signal Peptide on Stability and Folding of Escherichia coli Thioredoxin
por: Singh, Pranveer, et al.
Publicado: (2013) -
Folding and trimerization of signal sequence-less mature TolC in the cytoplasm of Escherichia coli
por: Masi, Muriel, et al.
Publicado: (2009) -
Correct folding of alpha-lytic protease is required for its extracellular secretion from Escherichia coli
Publicado: (1992) -
Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli
por: Elfageih, Rageia, et al.
Publicado: (2020) -
Optimized Signal Peptide for Secretory Expression of Human Recombinant Somatropin in E. coli
por: Ahmadi, Zeynab, et al.
Publicado: (2023)