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N-methylphenylalanine at the N-terminus of pilin isolated from Pseudomonas aeruginosa K.

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Abstract

AUTOMATED amino acid sequence analysis of pili protein isolated from the multi-piliated 2PfS mutant of Pseudomonas aeruginosa strain K (PAK)1 has shown that N-methylphenylalanine is the amino terminus. These pili, which mediate the infectious process of several Pseudomonas bacteriophages2, are composed of one protein subunit, pilin, of molecular weight 17,800 (ref. 1). Mass spectroscopy (MS), 270 MHz proton magnetic resonance spectroscopy (PMR), ultraviolet absorption spectroscopy, gas/liquid chromatography (GLC) and thin layer chromatography (TLC) have demonstrated the identity of the phenylthiohydantoin (PTH) derivative of the amino terminal amino acid (PTH–X) to be identical with synthetic PTH–N-methylphenylalanine.

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Authors and Affiliations

  1. Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada, T6G 2H7

    L. S. FROST, M. CARPENTER & W. PARANCHYCH

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  1. L. S. FROST
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  2. M. CARPENTER
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  3. W. PARANCHYCH
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FROST, L., CARPENTER, M. & PARANCHYCH, W. N-methylphenylalanine at the N-terminus of pilin isolated from Pseudomonas aeruginosa K.. Nature 271, 87–89 (1978). https://doi.org/10.1038/271087a0

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