PMID:10213615
| Citation |
Fekkes, P, de Wit, JG, Boorsma, A, Friesen, RH and Driessen, AJ (1999) Zinc stabilizes the SecB binding site of SecA. Biochemistry 38:5111-6 |
|---|---|
| Abstract |
The molecular chaperone SecB targets preproteins to SecA at the translocation sites in the cytoplasmic membrane of Escherichia coli. SecA recognizes SecB via its carboxyl-terminal 22 aminoacyl residues, a highly conserved domain that contains 3 cysteines and 1 histidine residue that could potentially be involved in the coordination of a metal ion. Treatment of SecA with a zinc chelator resulted in a loss of the stimulatory effect of SecB on the SecA translocation ATPase activity, while the activity could be restored by the addition of ZnCl2. Interaction of SecB with the SecB binding domain of SecA is disrupted by chelators of divalent cations, and could be restored by the addition of Cu2+ or Zn2+. Atomic absorption and electrospray mass spectrometry revealed the presence of one zinc atom per monomeric carboxyl terminus of SecA. It is concluded that the SecB binding domain of SecA is stabilized by a zinc ion that promotes the functional binding of SecB to SecA. |
| Links |
PubMed Online version:10.1021/bi982818r |
| Keywords |
Adenosine Triphosphatases/antagonists & inhibitors; Adenosine Triphosphatases/metabolism; Adenosine Triphosphatases/physiology; Amino Acid Sequence; Anilino Naphthalenesulfonates/chemistry; Bacterial Proteins/antagonists & inhibitors; Bacterial Proteins/metabolism; Bacterial Proteins/physiology; Binding Sites/drug effects; Biological Transport/drug effects; Cations, Divalent; Chelating Agents/pharmacology; Cysteine/chemistry; Cysteine/metabolism; Escherichia coli; Escherichia coli Proteins; Ethylenediamines/pharmacology; Membrane Transport Proteins; Molecular Chaperones/metabolism; Molecular Chaperones/physiology; Molecular Sequence Data; Peptide Fragments/antagonists & inhibitors; Peptide Fragments/metabolism; Sulfhydryl Reagents; Zinc/chemistry |
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