Title: Escherichia coli SecA truncated at its termini is functional and dimeric
Authors: Karamanou, Spyridoula ×
Sianidis, Giorgos
Gouridis, Giorgos
Pozidis, Charalambos
Papanikolau, Yiannis
Papanikou, Efrosyni
Economou, Anastassios #
Issue Date: Feb-2005
Publisher: Elsevier on behalf of the Federation of European Biochemical Societies
Series Title: FEBS Letters vol:579 issue:5 pages:1267-1271
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.
ISSN: 0014-5793
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Non-KU Leuven Association publications
× corresponding author
# (joint) last author

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