Open AccessPrecursors of three exported proteins in Escherichia coli.
Author(s) -
Linda L. Randall,
Simon Hardy,
LarsGöran Josefsson
Publication year - 1978
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.3.1209
Subject(s) - escherichia coli , maltose binding protein , polysome , biochemistry , cytoplasm , biology , in vitro , chemistry , fusion protein , ribosome , rna , gene , recombinant dna
Arabinose-binding protein, maltose-binding protein, and lambda receptor are synthesized in vitro on membrane-bound polysomes from Escherichia coli. All three proteins are exported from the cytoplasm of E. coli and all three are made in vitro in a form a few thousand daltons larger than the authentic protein. The larger form of arabinose-binding protein is also detected in vivo by pulse labeling. It is concluded that the larger forms of the exported proteins are precursors containing an extra sequence. In contrast to the above, when the intracellular protein elongation factor Tu is synthesized in vitro on free polysomes, it is not detectably larger than the authentic form.