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A survey of furin substrate specificity using substrate phage display.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wells, J. A. Matthews, D. J. Goodman, L. J. Gorman, C. M.
Description	Author Affiliation: Matthews DJ ( Department of Protein Engineering, Genentech, Inc., South San Francisco, California 94080.)
Abstract	The substrate specificity of furin, a mammalian enzyme involved in the cleavage of many constitutively expressed protein precursors, was studied using substrate phage display. In this method, a multitude of substrate sequences are displayed as fusion proteins on filamentous phage particles and ones that are cleaved can be purified by affinity chromatography. The cleaved phage are propagated and submitted to additional rounds of protease selection to further enrich for good substrates. DNA sequencing of the cleaved phage is used to identify the substrate sequence. After 6 rounds of sorting a substrate phage library comprising 5 randomized amino acids (xxxxx), virtually all clones had an RxxR motif and many had Lys, Arg, or Pro before the second Arg. Nine of the selected sequences were assayed using a substrate-alkaline phosphatase fusion protein system. All were cleaved after the RxxR, and some substrates with Pro or Thr in P2 were also found to be cleaved as efficiently as RxKR or RxRR. To further elaborate surrounding determinants, we constructed 2 secondary libraries (xxRx(K/R)Rx and xxRxPRx). Although no consensus developed for the latter library, many of the sequences in the the former library had the 7-residue motif (L/P)RRF(K/R)RP, suggesting that the furin recognition sequence may extend over more than 4 residues. These studies further clarify the substrate specificity of furin and suggest the substrate phage method may be useful for identifying consensus substrate motifs in other protein processing enzymes.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	8
Volume Number	3
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1994-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacteriophages Metabolism Subtilisins Amino Acid Sequence Cell Line, Transformed Chromatography, Affinity Embryo, Mammalian Furin Gene Library Kidney Kinetics Molecular Sequence Data Mutagenesis, Insertional Oligopeptides Chemistry Recombinant Fusion Proteins Structure-activity Relationship Substrate Specificity Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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