Signal peptidases in prokaryotes and eukaryotes--a new protease family.

[1]  G. Blobel,et al.  POST‐TRANSLATIONAL PROCESSING OF FULL‐LENGTH PRESECRETORY PROTEINS WITH CANINE PANCREATIC SIGNAL PEPTIDASE , 1980, Annals of the New York Academy of Sciences.

[2]  T. Date,et al.  Leader peptidase is found in both the inner and outer membranes of Escherichia coli. , 1981, The Journal of biological chemistry.

[3]  W. Wickner,et al.  Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope. , 1983, The Journal of biological chemistry.

[4]  W. DeGrado,et al.  Purification and properties of thiol beta-lactamase. A mutant of pBR322 beta-lactamase in which the active site serine has been replaced with cysteine. , 1984, The Journal of biological chemistry.

[5]  B. Guiard,et al.  One nuclear gene controls the removal of transient pre‐sequences from two yeast proteins: one encoded by the nuclear the other by the mitochondrial genome. , 1986, The EMBO journal.

[6]  S. Miura,et al.  A small hydrophobic domain anchors leader peptidase to the cytoplasmic membrane of Escherichia coli. , 1987, The Journal of biological chemistry.

[7]  M. Lively,et al.  Purification and characterization of hen oviduct microsomal signal peptidase. , 1987, Biochemistry.

[8]  R. Schekman,et al.  SEC11 is required for signal peptide processing and yeast cell growth , 1988, The Journal of cell biology.

[9]  J. Gordon,et al.  Substrate specificity of eukaryotic signal peptidase. Site-saturation mutagenesis at position -1 regulates cleavage between multiple sites in human pre (delta pro) apolipoprotein A-II. , 1988, The Journal of biological chemistry.

[10]  J. Gordon,et al.  Eukaryotic signal peptide structure/function relationships. Identification of conformational features which influence the site and efficiency of co-translational proteolytic processing by site-directed mutagenesis of human pre(delta pro)apolipoprotein A-II. , 1989, The Journal of biological chemistry.

[11]  R. Zimmermann,et al.  The reaction specificities of the thylakoidal processing peptidase and Escherichia coli leader peptidase are identical. , 1989, The EMBO journal.

[12]  G. von Heijne,et al.  Domain structure of mitochondrial and chloroplast targeting peptides. , 1989, European journal of biochemistry.

[13]  P. Novák,et al.  Minimum substrate sequence for signal peptidase I of Escherichia coli. , 1990, The Journal of biological chemistry.

[14]  G. Heijne,et al.  Protein targeting signals. , 1990 .

[15]  M. Chou,et al.  Polymeric sequences reveal a functional interrelationship between hydrophobicity and length of signal peptides. , 1990, The Journal of biological chemistry.

[16]  J. Gordon,et al.  Structural features in the NH2-terminal region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase. , 1990, The Journal of biological chemistry.

[17]  G. Blobel,et al.  Two subunits of the canine signal peptidase complex are homologous to yeast SEC11 protein. , 1990, The Journal of biological chemistry.

[18]  G. Vonheijne The signal peptide. , 1990 .

[19]  G. Heijne,et al.  Mapping of catalytically important domains in Escherichia coli leader peptidase. , 1990, The EMBO journal.

[20]  C. Robinson,et al.  Transport of proteins into chloroplasts. The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions. , 1991, The Journal of biological chemistry.

[21]  A. Kuhn,et al.  Use of site-directed mutagenesis to define the limits of sequence variation tolerated for processing of the M13 procoat protein by the Escherichia coli leader peptidase. , 1991, Biochemistry.

[22]  A. Schneider,et al.  Inner membrane protease I, an enzyme mediating intramitochondrial protein sorting in yeast. , 1991, The EMBO journal.

[23]  Identification of potential active-site residues in the Escherichia coli leader peptidase. , 1992, The Journal of biological chemistry.

[24]  S. Bron,et al.  Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases. , 1992, The EMBO journal.

[25]  A. Allsop,et al.  On the catalytic mechanism of prokaryotic leader peptidase 1. , 1992, The Biochemical journal.

[26]  G. A. Barkocy-Gallagher,et al.  Synthesis of precursor maltose-binding protein with proline in the +1 position of the cleavage site interferes with the activity of Escherichia coli signal peptidase I in vivo. , 1992, The Journal of biological chemistry.