Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region.
Open Access
- 1 May 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (15) , 8760-8765
- https://doi.org/10.1016/s0021-9258(19)38953-7
Abstract
No abstract availableThis publication has 34 references indexed in Scilit:
- SecA protein is directly involved in protein secretion in Escherichia coliFEBS Letters, 1989
- ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particleCell, 1988
- The antifolding activity of SecB promotes the export of the E. coli maltose-binding proteinCell, 1988
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteinsCell, 1983
- A previously unidentified gene in the spc operon of Escherichia coli K12 specifies a component of the protein export machineryCell, 1982
- Direct and specific photochemical crosslinking of adenosine 5'-triphosphate to an aminoacyl-tRNA synthetaseBiochemistry, 1977
- β-Galactosidase α complementation: properties of the complemented enzyme and mechanism of the complementation reactionBiochemistry, 1976
- Replication control in a composite plasmid constructed by in vitro linkage of two distinct repliconsNature, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970