Processing of Escherichia coli alkaline phosphatase: role of the primary structure of the signal peptide cleavage region 1 1Edited by A. R. Fersht

Karamyshev, A. L.; Karamysheva, Zemphyra N; Kajava, Andrey V.; Ksenzenko, V. N.; Nesmeyanova, M. A.

doi:10.1006/jmbi.1997.1617

Cited by 78 publications

(79 citation statements)

References 37 publications

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“…The high frequency of AQ cleavage suggests that the P. gingi alis signal peptidase may prefer this site. Signal peptidase I from E. coli also favours alanine in the k1 position, but has no preference for glutamine in the j1 position [41]. The P. gingi alis lipoprotein signal peptidase may prefer serine in the k1 position, since all four proteins predicted to be N-terminally attached to lipid had serine in this position (Figure 2).…”

Section: P Gingivalis Major Ompsmentioning

confidence: 99%

Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50

Veith

Talbo

Slakeski

et al. 2002

Biochemical Journal

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Porphyromonas gingivalis is an anaerobic, asaccharolytic Gram-negative rod associated with chronic periodontitis. We have undertaken a proteomic study of the outer membrane of P. gingivalis strain W50 using two-dimensional gel electrophoresis and peptide mass fingerprinting. Proteins were identified by reference to the pre-release genomic sequence of P. gingivalis available from The Institute for Genomic Research. Out of 39 proteins identified, five were TonB-linked outer membrane receptors, ten others were putative integral outer membrane proteins and four were putative lipoproteins. Pyroglutamate was found to be the N-terminal residue of seven of the proteins, and was predicted to be the N-terminal residue of 13 additional proteins. The RgpA, Kgp and HagA polyproteins were identified as fully processed domains in outer membranes prepared in the presence of proteinase inhibitors. Several domains were found to be C-terminally truncated 16–57 residues upstream from the N-terminus of the following domain, at a residue penultimate to a lysine. This pattern of C-terminal processing was not detected in a W50 strain isogenic mutant lacking the lysine-specific proteinase Kgp. Construction of another W50 isogenic mutant lacking the arginine-specific proteinases indicated that RgpB and/or RgpA were also involved in domain processing. The C-terminal adhesin of RgpA, designated RgpA27, together with RgpB and two newly identified proteins designated P27 and P59 were found to migrate on two-dimensional gels as vertical streaks at a molecular mass 13–42kDa higher than that calculated from their gene sequences. The electrophoretic behaviour of these proteins, together with their immunoreactivity with a monoclonal antibody that recognizes lipopolysaccharide, is consistent with a modification that could anchor the proteins to the outer membrane.

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Section: P Gingivalis Major Ompsmentioning

confidence: 99%

Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50

Veith

Talbo

Slakeski

et al. 2002

Biochemical Journal

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“…Analysis of the amino acid sequence of HS6ST1 in the culture medium revealed that its N-terminal amino acid started from tyrosine 25. Subsequent cDNA cloning showed that Tyr 25 and Gln 24 are conserved in all of the HS6ST isoforms (HS6ST1, -2, and -3) that have been identified to date in mice, humans, rats, dogs, chicken, and zebrafish (Fig. 1A).…”

Section: Resultsmentioning

confidence: 99%

“…4 We previously showed that 6-O-sulfotransferase activity could be detected in the conditioned medium of cultured CHO-K1 cells (19). Analysis of the amino acid sequence of HS6ST1 in the culture medium revealed that its N-terminal amino acid was Tyr 25 . Since Tyr 25 and Gln 24 are conserved in all HS6ST isoforms (HS6ST1, -2, and -3), we speculated that HS6ST3 may be cleaved at this position.…”

Section: ␤-Secretase Regulates Heparan Sulfate 6-o-sulfationmentioning

confidence: 97%

“…Signal peptides of secretory proteins, which are cleaved by the signal peptidase, are known to consist of three contiguous regions; a 1-5-amino acid region of positively charged residues, a 7-15-hydrophobic amino acid region, and a 5-7-amino acid region containing residues with small side chain at the Ϫ1-and Ϫ3-positions (25)(26)(27)(28). If the N-terminal hydrophobic sequence of HS6ST3 is cleaved by signal peptidase, adding several hydrophilic amino acids to its N terminus would compromise its recognition by the signal peptidase.…”

Section: ␤-Secretase Regulates Heparan Sulfate 6-o-sulfationmentioning

confidence: 99%

“…Analysis of the amino acid sequence of HS6ST1 in the culture medium revealed that its N-terminal amino acid was Tyr 25 . Since Tyr 25 and Gln 24 are conserved in all HS6ST isoforms (HS6ST1, -2, and -3), we speculated that HS6ST3 may be cleaved at this position. When the conserved QY residues were altered to AY, QA, and AA, the secretion of these mutant proteins was not affected or was even enhanced (Fig.…”

Section: ␤-Secretase Regulates Heparan Sulfate 6-o-sulfationmentioning

confidence: 99%

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Regulation of Heparan Sulfate 6-O-Sulfation by β-Secretase Activity

Nagai

Habuchi

Kitazume

et al. 2007

Journal of Biological Chemistry

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Heparan sulfate (HS) 2 proteoglycans play important roles in various biological processes by acting as co-receptors, by serving as reservoir molecules in morphogen gradient formation etc. (1-5). The sulfation domains (S domains) of HS are the binding sites for the growth factors and morphogens. Analyses of fruit fly, zebrafish, and mice mutants have revealed that the specific patterns of the sulfations determine the bioactivities of the HS proteoglycans (6 -10). In particular, 6-O-sulfation of HS has been shown to be required for the fibroblast growth factor (FGF) and Wnt signaling pathways in Drosophila and zebrafish (11,12). With regard to the link between 6-O-sulfation of HS and the FGF signaling pathway, heparan sulfate 6-O-sulfotransferase (HS6ST) RNA interference experiments in fruit fly have demonstrated that the interfered phenotype closely resembles those of mutants that are defective in FGF signaling components (11). In addition, by subjecting a sulfated octasaccharide library to an affinity chromatographic assay, have shown that the 6-O-sulfation of HS is important for binding activities of FGF-10, -4, and -7. With regard to the link between HS 6-O-sulfation and the Wnt signaling pathway, the knockdown of HS6ST in zebrafish with morpholino antisense oligonucleotides results in perturbed muscle differentiation that is associated with higher expression of the Wnt target genes myoD and eng2. QSulf1, the avian heparan sulfate 6-O-endosulfatases, is required for the activation of MyoD, which is a Wnt-induced regulator of muscle specification (14). Thus, the 6-O sulfation of HS plays important roles in regulating HS-binding growth factor signaling and morphogen gradient formation.Three isoforms of HS6STs have been identified in mice and humans (15-18). The expression patterns of these isoforms are regulated in spatially and temporally different manners. Their substrate specificities also differ (16, 17), since HS6ST1 preferentially catalyzes the sulfation of the L-iduronic acid (IdoA)-GlcNS disaccharide unit, whereas HS6ST2 prefers the D-glucuronic acid (GlcA)-GlcNS and IdoA(2S)-GlcNS disaccharides, and HS6ST3 has intermediate substrate specificity between *

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Pre‐Protein, Pre‐Pro‐Protein

Nakamura

Karamyshev

2002

Encyclopedia of Molecular Biology

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Processing of Escherichia coli alkaline phosphatase: role of the primary structure of the signal peptide cleavage region 1 1Edited by A. R. Fersht

Cited by 78 publications

References 37 publications

Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50

Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50

Regulation of Heparan Sulfate 6-O-Sulfation by β-Secretase Activity

Pre‐Protein, Pre‐Pro‐Protein

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