Carboxy-terminal region of Escherichia coli SecA ATPase is important to promote its protein translocation activity in vivo

Biochem Biophys Res Commun. 1994 May 16;200(3):1477-83. doi: 10.1006/bbrc.1994.1617.

Abstract

The role of the carboxy-terminal region of E. coli SecA ATPase was investigated by using genetic methods to construct a truncated SecA protein missing the last 66 amino acid residues and by systematically substituting serine for each of four cysteine residues present in this protein. Truncation of SecA or alteration of any of the carboxy-terminal cysteine residues resulted in poor growth and a protein secretion defect, indicating that this region of SecA is important in its protein translocation activity. Biochemical analysis of the altered proteins revealed a modest increase in translocation ATPase activity, suggesting that the carboxy-terminal region of SecA may facilitate the coupling of its ATPase activity to cycles of protein translocation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Base Sequence
  • DNA Primers / chemistry
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins*
  • Genetic Complementation Test
  • Membrane Transport Proteins*
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • SEC Translocation Channels
  • SecA Proteins
  • Structure-Activity Relationship

Substances

  • Bacterial Proteins
  • DNA Primers
  • Escherichia coli Proteins
  • Membrane Transport Proteins
  • SEC Translocation Channels
  • Adenosine Triphosphatases
  • SecA Proteins