Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10873719 | FEBS Letters | 2005 | 5 Pages |
Abstract
Terminal residues in SecA, the dimeric ATPase motor of bacterial preprotein translocase, were proposed to be required for function and dimerization. To test this, we generated truncation mutants of the 901aa long SecA of Escherichia coli. We now show that deletions of carboxy-terminal domain (CTD), the extreme CTD of 70 residues, or of the N-terminal nonapeptide or of both, do not compromise protein translocation or viability. Deletion of additional C-terminal residues upstream of CTD compromised function. Functional truncation mutants like SecA9-861 are dimeric, conformationally similar to SecA, fully competent for nucleotide and SecYEG binding and for ATP catalysis. Our data demonstrate that extreme terminal SecA residues are not essential for SecA catalysis and dimerization.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Spyridoula Karamanou, Giorgos Sianidis, Giorgos Gouridis, Charalambos Pozidis, Yiannis Papanikolau, Efrosyni Papanikou, Anastassios Economou,