On the release of the formyl group from nascent protein

doi:10.1016/0022-2836(68)90307-0

Journal of Molecular Biology

Volume 33, Issue 3, 14 May 1968, Pages 571-574, IN4, 575-589

https://doi.org/10.1016/0022-2836(68)90307-0 Get rights and content

Abstract

Extracts from Escherichia coli and Bacillus stearothermophilus contain enzymes which liberate amino groups from formylmethionyl peptides. Both extracts cleave formyl-Met-Ala-Ser to yield formate and Met-Ala-Ser, but not formylmethionine, as products. A number of formylmethionyl peptides are hydrolyzed much faster than other formyl peptides, acetyl-Met-Ala or formylmethionine. Furthermore, a protein fraction from E. coli which contains the peptide deformylase removes formate from protein made in vitro. These findings argue that the function of the peptide deformylases is to remove the formyl group from nascent protein. Another enzyme in the E. coli extract hydrolyzes formylmethionine, but the presence of this enzyme probably is not significant, because it has been identified as acetylornithine deacetylase. The peptide deformylase of E. coli is quite labile under a variety of experimental conditions and is inhibited strongly by thiols; so far the instability has prevented any significant purification.

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^†: Present address: Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge, England.

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