Signal peptide amino acid sequences in Escherichia coli contain information related to final protein localization. A multivariate data analysis.

Sjöstróm, Michael; Wold, Svante; Wieslander, Åke; Rilfors, Leif

doi:10.1002/j.1460-2075.1987.tb04825.x

Cited by 96 publications

(49 citation statements)

References 76 publications

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“…O1-ST, like other STas, may be biosynthesized in the cells as preprotoxin consisting of three regions: an N-terminal signal sequence segment, a C-terminal mature toxin segment and the "central" segment between them. This potential signal sequence, consisting of 18 amino acid residues, is similar to that of other Gram-negative bacteria (31,32), which is cleaved upon export into the periplasm (24). The "n region" containing a positive charge (Lys) was followed by a nine amino acid "h region," residues 4 (Leu) to 12 (Phe), in which eight amino acids are hydrophobic.…”

Section: Discussionmentioning

confidence: 79%

The Gene Encoding the Heat‐Stable Enterotoxin of Vibrio cholerae Is Flanked by 123‐Base Pair Direct Repeats

Takeda¹

1993

Microbiology and Immunology

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The heat-stable enterotoxin (O1-ST) gene (sto) was cloned from chromosome of the strain GP156 of Vibrio cholerae O1 (Inaba, El Tor) in Escherichia coli K-12, and its nucleotide seqence was determined. The nucleotide sequence of sto was very similar to that of NAG-ST gene (stn) of V. cholerae non-O1. Both sto and stn were flanked by 123-base pair direct repeats which had at least 93% homology to one another and included some inverted repeats. All the strains of V. cholerae, V. mimicus, V. metschnikovii, V. hollisae and Yersinia enterocolitica examined by colony hybridization had the direct repeat sequence regardless of ST-gene possession. The infant-mouse active methanol soluble heatstable enterotoxin (STa) is a small peptide toxin which is capable of causing cholera-like disease in humans by stimulating guanylate cyclase in the cells of small intestines (9,22,33). Various enteric bacteria such as Escherichia coli (7), Yersinia enterocolitica (8, 19), Vibrio cholerae non-O1 (1), V. mimicus (2) and Citrobacter freundii (11) have been demonstrated to produce STa. We have previously reported a nucleotide sequence of heatstable enterotoxin (NAG-ST) produced by V. cholerae non-O1 NRT 36 (18). NAG-ST resembles other STas in the amino acid sequence especially in the carboxyl terminal region. NAG-ST secreted extracellularly is comprised of 17 amino acids (28), but is produced on translation level as a precursor consisting of 78 amino acids. Three segments are assigned in the precursor of NAG-ST, like other STas which are the signal sequence segment (the Nterminal segment), mature toxin segment (the Cterminal segment) and the region between them. The nucleotide sequence of the former two segments of NAG-ST gene (stn) differs from those of the other STa genes, though mature toxin segment is relatively conserved.Toxinogenic strains of V. cholerae serogroup O1produce mainly cholera toxin which causes the copious outpouring of fluids characteristic of cholera. The association of STa with strains of V. cholerae O1 had not been known before we documented a strain GP156 (Inaba, El Tor) of V. cholerae O1 which produced STa (O1-ST) along with cholera toxin (30). In that paper, we described that the strain GP156 was isolated from the environment, and that the incidence of the O1-ST gene (sto) is low (0.5%) among V. cholerae isolates. These results indicate that the O1-ST is not an important virulence factor among them. However, we are interested in investigating how ST gene spread among various enteric bacteria. Since the E. coli STp has been shown to be encoded within a transposon (Tn 168 1) flanked by inverted repeats of insertion sequence 1 (IS1) and to possess ability to disseminate widely (25), O1-ST may also spread among V. cholerae O1. In V. cholerae O1, no

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Section: Discussionmentioning

confidence: 79%

The Gene Encoding the Heat‐Stable Enterotoxin of Vibrio cholerae Is Flanked by 123‐Base Pair Direct Repeats

Takeda¹

1993

Microbiology and Immunology

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“…3), suggesting that the charge character of their carboxamide side groups can actively promote MBP export. Again, both Asn and Gln are commonly found in the hydrophilic segments of prokaryotic signal peptides (35). Note that Asn is found at position 2 of the RBP signal peptide (Fig.…”

Section: Discussionmentioning

confidence: 87%

“…MBPA3-8 export was not affected by the substitution of Arg for Lys at position 2. Both of these basic residues are frequently encountered in the hydrophilic segments of signal peptides (35). Interestingly, the substitution of either Asn or Gln, both neutral residues, for Lys had only a minor adverse effect on MBPA3-8 export (Fig.…”

Section: Discussionmentioning

confidence: 93%

“…It is not evident why this is the case. Although there are a number of prokaryotic signal peptides that contain only a single basic residue in their hydrophilic segment, there is no example in which a single basic residue constitutes the entire region (save for the initiating Met) (35). The reductions in the efficiencies of MBPA3-8 and MBPA2-8 export probably result from the decreased length of the MBP signal peptide, as well as from the reduction in the net charge of the hydrophilic segment.…”

Section: Discussionmentioning

confidence: 99%

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Alterations in the hydrophilic segment of the maltose-binding protein (MBP) signal peptide that affect either export or translation of MBP

1992

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Mutations that reduce the net positive charge within the hydrophilic segments of the signal peptides of several prokaryotic exported proteins can result in a reduction in the rate of protein export, as well as a reduction in protein synthesis (M. N. Hall, J. Gabay, and M. Shwartz, EMBO J. 2:15-19, 1983 revealed that the role of the hydrophilic segment in the export process can be functionally separated from any role in translation. Taken together, these results strongly suggest that the hydrophilic segment of the MBP signal peptide is not involved in a mechanism that couples MBP translation to export and argue against the presence of a mechanism that obligatorily couples translation to protein export in Escherichia coli.Proteins destined for export in Escherichia coli are synthesized as precursor species with an amino-terminal extension termed the signal peptide that is responsible for initiating the export of proteins from the cytoplasm. The periplasmic maltose-binding protein (MBP) of E. coli, the product of the malE gene, is synthesized with a typical bacterial signal peptide that shares little primary amino acid homology with other signal peptides but does exhibit conserved features characteristic of signal peptides of both prokaryotic and eukaryotic origin. The first eight residues of the MBP signal peptide constitute the hydrophilic segment, a distinct region that carries a net positive charge due to the presence of three basic residues. The hydrophilic segment precedes the hydrophobic core, a region devoid of charged residues that is predicted to assume an a-helical conformation. Following the hydrophobic core is the cleavage site for signal peptidase I. (For a comprehensive review of the MBP signal peptide and MBP export, see reference 4.)A specific role for the basic residues of the hydrophilic segment in protein export was first suggested in the loop model (18). The basic residues were proposed to initiate an ionic interaction between the signal peptide and the nega-* Corresponding author.

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“…We called these three scales, z 1, z2, and z3, principal properties (PPs) of the amino acids. The PPs were used for a quantitative description of the variation in sequence in families of peptide analogues, thereby allowing the construction of models of the relation between structure and biological activity for these peptide families (3)(4)(5). Since amino acids other than the 20 coded ones are often included in synthetic peptide sequences, it is of interest to extend the z-scales to such noncoded acids.…”

Section: Introductionmentioning

confidence: 99%

Principal property values for six non-natural amino acids and their application to a structure–activity relationship for oxytocin peptide analogues

Wold¹,

Eriksson²,

Hellberg³

et al. 1987

Can. J. Chem.

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. Can. J. Chem. 65, 1814Chem. 65, (1987. Previously derived principal property scales for the 20 coded amino acids have been extended to six noncoded amino acids, namely ornithine, norvaline, norleucine, 0-methylated threonine, a-amino butyric acid, and citrulline. This has been done first, for the 20 coded amino acids, by developing PLS models for the relations between the previously derived scales (z, , z 2 , and z3) and newly measured thin-layer chromatography data, proton nuclear magnetic resonance data, plus literature data describing amino acid "bulk" (van der Waals volume and molecular mass). Thereafter, z values for the noncoded amino acids were calculated by inserting the same measured data for these compounds into the PLS models. As a validation, the calculated z values were then used to describe the structural variation of a set of 60 oxytocin peptide analogues for which literature data on biological measurements existed. The models explain 7 1-81% of the variance of the biological data and are highly significant according to cross-validation. Prediction errors of about twice the estimated biological measurement error are obtained for the 11 peptide analogues containing noncoded amino acids. Chem. 65, 1814Chem. 65, (1987.Des Cchelles de propriCtCs principales qui avaient CtC dCveloppCes antkrieurement pour les 20 acides aminCs codes ont Ct C Ctendues i six acides aminis non-codCs, soit l'ornithine, la norvaline, la norleucine, la thrConine 0-mCthylCe, l'acide a-aminobutyrique et la citrulline. Dans un premier temps, on a dCveloppC des modkles PLS pour les 20 acides aminCs codes en se basant sur les relations entre les Cchelles developpCes anterieurement ( z l , z 2 et z3) et les nouvelles donnCes mesuries par chromatographie en couche mince et par resonance magnktique nuclCaire ainsi que des donnCes de la littCrature dCcrivant le ccvolume~) des acides aminCs (volume de van der Waals et masse molCculaire). Ensuite, on a calculC les valeurs z des acides amines non-codes en insirant les mCmes donnCes pour ces composCs dans les modkles PLS. Afin de valider nos conclusions, on a ensuite utilisC les valeurs z pour dkcrire la variation de structure d'un ensemble de 60 analogues du peptide oxytocine pour lesquels des donnCes relatives aux mesures biologiques existent dans la litttrature. Les modkles expliquent de 7 1 a 81% de la variance des donnCes biologiques et, d'aprks des contre-validations, elles sont trks significatives. Pour 11 des analogues peptidiques contenant des acides aminis qui ne sont pas cod&, on peut prCdire des erreurs qui sont le double de l'erreur CvaluCe pour les mesures biologiques.[Traduit par la revue]

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Signal peptide amino acid sequences in Escherichia coli contain information related to final protein localization. A multivariate data analysis.

Cited by 96 publications

References 76 publications

The Gene Encoding the Heat‐Stable Enterotoxin of Vibrio cholerae Is Flanked by 123‐Base Pair Direct Repeats

The Gene Encoding the Heat‐Stable Enterotoxin of Vibrio cholerae Is Flanked by 123‐Base Pair Direct Repeats

Alterations in the hydrophilic segment of the maltose-binding protein (MBP) signal peptide that affect either export or translation of MBP

Principal property values for six non-natural amino acids and their application to a structure–activity relationship for oxytocin peptide analogues

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