The high affinity ATP binding site modulates the SecA-precursor interaction

Autor: Frank van Voorst, Ben de Kruijff, Ingrid J. Vereyken
Rok vydání: 2000
Předmět:
SecA
Protein Conformation
Lipid Bilayers
Signal sequence
medicine.disease_cause
environment and public health
Biochemistry
chemistry.chemical_compound
Adenosine Triphosphate
Structural Biology
ATP hydrolysis
Nucleotide
Integral membrane protein
Phospholipids
chemistry.chemical_classification
Adenosine Triphosphatases
biology
Diphosphonates
Chemistry
Escherichia coli Proteins
Hydrolysis
Adenosine Diphosphate
Phospholipid
Protein Transport
Cross-Linking Reagents
Protein Binding
Signal peptide
Azides
Adenylyl Imidodiphosphate
Biophysics
Porins
Protein Sorting Signals
Bacterial Proteins
Genetics
medicine
Escherichia coli
Amino Acid Sequence
Binding site
Protein Precursors
Molecular Biology
Phosphatidylglycerol
Protein translocation
Crosslinking
Binding Sites
SecA Proteins
Membrane Transport Proteins
Cell Biology
Amino Acid Substitution
Chaperone (protein)
Liposomes
Mutation
biology.protein
bacteria
Carrier Proteins
SEC Translocation Channels
Zdroj: FEBS letters. 486(1)
ISSN: 0014-5793
Popis: SecA is the central component of the protein-translocation machinery of Escherichia coli. It is able to interact with the precursor protein, the chaperone SecB, the integral membrane protein complex SecYEG, acidic phospholipids and its own mRNA. We studied the interaction between prePhoE and SecA by using a site-specific photocrosslinking strategy. We found that SecA is able to interact with both the signal sequence and the mature domain of prePhoE. Furthermore, this interaction was dependent on the type of nucleotide bound. SecA in the ADP-bound conformation was unable to crosslink with the precursor, whereas the ATP-bound conformation was active in precursor crosslinking. The SecA–precursor interaction was maintained in the presence of E. coli phospholipids but was loosened by the presence of phosphatidylglycerol bilayers. Examining SecA ATP binding site mutants demonstrated that ATP hydrolysis at the N-terminal high affinity binding site is responsible for the changed interaction with the preprotein.
Databáze: OpenAIRE
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