Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli.
AUTOR(ES)
Akiyama, Y
RESUMO
The secY (prlA) gene product is an essential component of the Escherichia coli cytoplasmic membrane, and its function is required for the translocation of exocytoplasmic proteins across the membrane. We have analyzed the orientation of the SecY protein in the membrane by examining the hydropathic character of its amino acid sequence, by testing its susceptibility to proteases added to each side of the membrane, and by characterizing SecY-PhoA (alkaline phosphatase) hybrid proteins constructed by TnphoA transpositions. The orientation of the PhoA portion of the hybrid protein with respect to the membrane was inferred from its enzymatic activity as well as sensitivity to external proteases. The results suggest that SecY contains 10 transmembrane segments, five periplasmically exposed parts, and six cytoplasmic regions including the amino- and carboxyterminal regions.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=553804Documentos Relacionados
- The SecY membrane component of the bacterial protein export machinery: analysis by new electrophoretic methods for integral membrane proteins.
- Mutation that suppresses the protein export defect of the secY mutation and causes cold-sensitive growth of Escherichia coli.
- Characterization of cold-sensitive secY mutants of Escherichia coli.
- Escherichia coli SecB, SecA, and SecY proteins are required for expression and membrane insertion of the bacteriocin release protein, a small lipoprotein.
- SecY, a multispanning integral membrane protein, contains a potential leader peptidase cleavage site.