J. Biol. Chem., Vol. 255, Issue 14, 6745-6750, Jul, 1980
The NH2-terminal sequence of a precursor form of the arabinose binding protein
VG Wilson and RW Hogg
Cell-free arabinose binding protein (ABP) was synthesized using a mRNA-
directed Escherichia coli S30 translation system. The source of the mRNA
was a total cellular RNA extract from cultures of E. coli B/r ara A 39,
induced for ABP production. Purification of in vitro ABP was effected by
affinity chromatography on a column of purified anti-ABP coupled to
Sepharose 4B, followed by Sephadex G-75 chromatography in 9% formic acid.
The purified in vitro ABP was found to have a molecular weight
approximately 3000 greater than native ABP. Comparison of the CNBr peptide
fragments of native and in vitro ABP demonstrated an NH2- terminal
extension of 23 amino acids not present in native ABP. The identities of 20
of the residues in the extension were established, and the characteristics
of this region resemble the features proposed for signal sequences that
function in protein secretion.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
