Intracellular aminopeptidases inStreptomyces lividans 66

Butler, Michael J.; Aphale, Jayant S.; DiZonno, M A; Krygsman, Phyllis; Walczyk, Eva; Malek, Lawrence T.

doi:10.1007/bf01569658

Cited by 16 publications

(6 citation statements)

References 19 publications

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“…The expression pattern obtained by the northern blot does not correlate completely with the tissue distribution of the enzymatic X-prolyl amino peptidase activity reported before (Vanhoof et al, 1992b). These results provide evidence for the existence in mammals of multiple forms of the X-prolyl aminopeptidase gene, as was described for E. coli and S. lividans (Yoshimoto et al, 1989;Butler et al, 1994).Whether these multiple forms share identi cal enzymatic and functional characteristics remains to be established by further cloning and expression efforts. X-prolyl aminopeptidase is described in eukaryotes as a membranebound form (Vergas Romero et al, 1995) and as a cytosolic form (Harbeck and Mentlein, 1991;Vanhoof et al, 1992a) of the enzyme.…”

Section: Resultsmentioning

confidence: 68%

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Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P)

Vanhoof

Goossens²,

Juliano³

et al. 1997

Cytogenet Genome Res

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A novel human cDNA (XPNPEPL) encoding a protein of 623 amino acids exhibiting 44% sequence identity and 62 % sequence similarity to pig kidney X-prolyl aminopeptidase (aminopeptidase P; EC 3.4.11.9) was obtained by reverse transcription/polymerase chain reaction of phytohemagglutin-in-stimulated lymphocyte mRNA. Conserved sequences were found with the prokaryotic X-prolyl aminopeptidase encoding gene (pepP). The human gene translation product exhibits a high sequence homology to the Schizosaccharomyces pombe chromosome I hypothetical protein C22G7.01c and to the S. cerevisiae ORF yll029w. Northern blot analysis indicates an ubiquitous expression of the human XPNPEPL sequence.

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Section: Resultsmentioning

confidence: 68%

“…Recently, the complete amino acid sequence from the pig kidney enzyme has been published (Vergas Romero et al, 1995). The nucleotide sequences of the X-prolyl aminopeptidase encoding genes (pepP) from Escherichia coli (Yoshimoto et al, 1989), Myco plasma genitalium (Fraser et al, 1995), Streptomyces lividans (Butler et al. 1994).…”

mentioning

confidence: 99%

Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P)

Vanhoof

Goossens²,

Juliano³

et al. 1997

Cytogenet Genome Res

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“…Indeed, no experimental data concerning the regulation of expression are available for the actinomycete type I aminopeptidase N; the only hypothesis regards the aminopeptidase N of S. lividans 66, that was predicted to be constitutively expressed, as deduced by an hypothetical r 70 factor binding sequence found upstream of its coding sequence (Butler et al 1994a). In contrast, detailed investigations were carried out on the E. coli pepN promoter system that comprises two divergent elements: a weak constitutive promoter and another regulated by phosphate starvation (Foglino and Lazdunsky 1987).…”

Section: Discussionmentioning

confidence: 98%

“…cleavage of N-terminal lysine, arginine and leucine (Neviani et al 2002). Our interest in the characterization of the genetic determinants of PAB PepNs was motivated by evidence that well studied bacterial peptidase gene products, e.g., those from Escherichia coli (Chandu and Nandi 2003), Lactococcus lactis (van Alen-Boerritgher et al 1991), Streptomyces lividans (Butler et al 1994a) and Streptococcus thermophilus (Midwinter and Pritchard 1994) have a broad substrate specificity and play relevant roles in peptide substrate utilization.…”

Section: Introductionmentioning

confidence: 99%

Isolation of aminopeptidase N genes of food associated propionibacteria and observation of their transcription in skim milk and acid whey

Rossi

Busetto

Torriani

2006

Antonie van Leeuwenhoek

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In this study consensus oligonucleotides PN5/PN3 were designed by aligning the aminopeptidase N genes (pepN) of various actinobacteria and applied to the isolation of the pepN genes of dairy propionibacteria (PAB) and closely related species associated with food. This allowed sequencing of a pepN gene region from Propionibacterium jensenii LMG 16541. The sequence of this gene was completed by inverse PCR. Consensus primer pairs NU1/D1 and NU2/D1 were derived from the alignment of the new sequence with its homologues in Propionibacterium acnes and other actinobacteria; these were used to start sequencing of the pepN genes of Propionibacterium freudenreichii, Propionibacterium thoenii, Propionibacterium microaerophilum, Propionibacterium acidipropionici, Propioni bacterium cyclohexanicum and Propionibacterium microaerophilum. Reverse transcription coupled with PN5/PN3 and NU1/D1 PCR tests indicated that the pepN genes of P. jensenii and P. freudenreichii are expressed during growth in skim milk and acid whey.

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“…Aminopeptidase G (EC 3.4.11.-) [Butler et al, 1994] EC 3. Bacteriophage T7 Internal virion protein B, part of the T7 pore complex [Dunn and Studier, 1983] Chlorophyll biosynthesis (58.6%) Photosystem I (58.6%) TC 1.C.…”

Section: Streptomyces Lividansmentioning

confidence: 99%

Prediction of Functional Class of Novel Bacterial Proteins without the Use of Sequence Similarity by a Statistical Learning Method

Cui¹,

Han²,

Cai³

et al. 2005

Microb Physiol

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A substantial percentage of the putative protein-encoding open reading frames (ORFs) in bacterial genomes have no homolog of known function, and their function cannot be confidently assigned on the basis of sequence similarity. Methods not based on sequence similarity are needed and being developed. One method, SVMProt (http://jing.cz3.nus.edu.sg/cgi-bin/svmprot.cgi), predicts protein functional family irrespective of sequence similarity (Nucleic Acids Res. 2003;31:3692–3697). While it has been tested on a large number of proteins, its capability for non-homologous proteins has so far been evaluated for a relatively small number of proteins, and additional tests are needed to more fully assess SVMProt. In this work, 90 novel bacterial proteins (non-homologous to known proteins) are used to evaluate the capability of SVMProt. These proteins are such that none of their homologs are in the Swiss-Prot database, their functions not clearly described in the literature, and they themselves and their homologs are not included in the training sets of SVMProt. They represent proteins whose function cannot be confidently predicted by sequence similarity methods at present. The predicted functional class of 76.7% of each of these proteins shows various levels of consistency with the literature-described function, compared to the overall accuracy of 87% for the SVMProt functional class assignment of 34,582 proteins that have at least one homolog of known function. Our study suggests that SVMProt is capable of assigning functional class for novel bacterial proteins at a level not too much lower than that of sequence alignment methods for homologous proteins.

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Intracellular aminopeptidases inStreptomyces lividans 66

Cited by 16 publications

References 19 publications

Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P)

Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P)

Isolation of aminopeptidase N genes of food associated propionibacteria and observation of their transcription in skim milk and acid whey

Prediction of Functional Class of Novel Bacterial Proteins without the Use of Sequence Similarity by a Statistical Learning Method

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