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SecA-dependence of the translocation of a large periplasmic loop in the Escherichia coli MalF inner membrane protein is a function of sequence context.
- Source :
-
Molecular membrane biology [Mol Membr Biol] 1995 Apr-Jun; Vol. 12 (2), pp. 209-15. - Publication Year :
- 1995
-
Abstract
- We have analysed the translocation of a large periplasmic loop in the Escherichia coli MalF inner membrane protein when placed in different sequence contexts and under conditions when the function of the SecA protein is inhibited. The results show that the degree of SecA-dependence varies with sequence context: while translocation of the large loop in its normal context is only minimally affected by SecA inhibition, translocation is much more sensitive to SecA inhibition when the loop is placed in the context of other inner membrane proteins. Conversely, when the large MalF loop is replaced by segments from other proteins, translocation of those segments is again very sensitive to SecA inhibition. Thus, SecA-dependence is not an all-or-none phenomenon and is not only a simple function of, e.g. the length of a translocated segment or the hydrophobicity of the flanking transmembrane segments.
- Subjects :
- Adenosine Triphosphatases pharmacology
Animals
Bacterial Proteins chemistry
Bacterial Proteins pharmacology
Carrier Proteins chemistry
Endopeptidases genetics
Escherichia coli chemistry
Escherichia coli ultrastructure
Maltose-Binding Proteins
Membrane Proteins chemistry
Protein Biosynthesis
Protein Conformation
Rabbits
Recombinant Fusion Proteins drug effects
Recombinant Fusion Proteins genetics
SEC Translocation Channels
SecA Proteins
Sequence Deletion
ATP-Binding Cassette Transporters
Adenosine Triphosphatases genetics
Bacterial Proteins genetics
Carrier Proteins genetics
Escherichia coli genetics
Escherichia coli Proteins
Membrane Proteins genetics
Membrane Transport Proteins
Monosaccharide Transport Proteins
Periplasmic Binding Proteins
Serine Endopeptidases
Subjects
Details
- Language :
- English
- ISSN :
- 0968-7688
- Volume :
- 12
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Molecular membrane biology
- Publication Type :
- Academic Journal
- Accession number :
- 7795711
- Full Text :
- https://doi.org/10.3109/09687689509027509