PMID:15476412
| Citation |
Wang, L, Miller, A, Rusch, SL and Kendall, DA (2004) Demonstration of a specific Escherichia coli SecY-signal peptide interaction. Biochemistry 43:13185-92 |
|---|---|
| Abstract |
Protein translocation in Escherichia coli is initiated by the interaction of a preprotein with the membrane translocase composed of a motor protein, SecA ATPase, and a membrane-embedded channel, the SecYEG complex. The extent to which the signal peptide region of the preprotein plays a role in SecYEG interactions is unclear, in part because studies in this area typically employ the entire preprotein. Using a synthetic signal peptide harboring a photoaffinity label in its hydrophobic core, we examined this interaction with SecYEG in a detergent micellar environment. The signal peptide was found to specifically bind SecY in a saturable manner and at levels comparable to those that stimulate SecA ATPase activity. Chemical and proteolytic cleavage of cross-linked SecY and analysis of the signal peptide adducts indicate that the binding was primarily to regions of the protein containing transmembrane domains seven and two. The signal peptide-SecY interaction was affected by the presence of SecA and nucleotides in a manner consistent with the transfer of signal peptide to SecY upon nucleotide hydrolysis at SecA. |
| Links |
PubMed PMC3084660 Online version:10.1021/bi049485k |
| Keywords |
Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Bacterial Proteins/metabolism; Biotin/metabolism; Cross-Linking Reagents; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Hydrolysis; Membrane Transport Proteins/metabolism; Molecular Sequence Data; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Phenylalanine/analogs & derivatives; Phenylalanine/metabolism; Photoaffinity Labels/metabolism; Protein Binding; Protein Precursors/chemistry; Protein Precursors/metabolism; Protein Sorting Signals; Protein Transport; Ultraviolet Rays |
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