Mechanism of C-terminal amide formation by pituitary enzymes

Bradbury, A. F.; Finnie, M. D. A.; Smyth, Derek G.

doi:10.1038/298686a0

Cited by 666 publications

(259 citation statements)

References 12 publications

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“…as compared with the mature Ts VII. Accordingly, the Lys residue have to be removed by a basic residue-specific carboxypeptidasc (CPAse B-like activity), after which the remaining Gly-extended peptide will be converted into a des-Gly peptide amine by an a-amidating enzyme [21]. The resulting Cys-amide residue correlates with that chemically determined on the native Ts VII [3].…”

Section: Resultsmentioning

confidence: 99%

Molecular cloning and nucleotide sequence analysis of a cDNA encoding the main β‐neurotoxin from the venom of the South American scorpion Tityus serrulatus

et al. 1992

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A cDNA encoding the main T@II,F .wwhru.r ,%ncurotoxin was isolated from a venom gland cDNA library by using an oligonuclcotidc probe, The amino iICid scqucncr deduced I'rom the cDNA nucteotidc sequcncc indicated that the toxin is the processed product or a precursor containing:(i) a signal peptide of 20 residues: (ii) the amino acid sequence of the mature loxin: and (iii) an extra Gly-Lys-Lya tail al the C-terminal end before the termination codon. Thus, in addition to the remov;ll of the signal peptide by a signal pcptidasc, the generation of the mature toxin requires both a post-translational ClCUvagC by a carboxypcplidasc specific for basic rcsiducs and the XIion of an a-amidating enzyme. These results also show that the biosynthetic pathwuy for &toxins of"Ncw World' scorpion venoms is similar LO Ihat already described for a-toxins of 'Old World' scorpion venoms.

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Section: Resultsmentioning

confidence: 99%

Molecular cloning and nucleotide sequence analysis of a cDNA encoding the main β‐neurotoxin from the venom of the South American scorpion Tityus serrulatus

et al. 1992

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“…Of major interest is the presence of a glycine codon at the 3' end of the coding sequence for diptericin, which indicates that the C-terminal residue of diptericin is amidated (see [17,181). C-terminal amidation is also observed in other antibacterial peptides from insects .…”

Section: Discussionmentioning

confidence: 99%

Insect immunity. Isolation of cDNA clones corresponding to diptericin, an inducible antibacterial peptide from Phormia terranovae (Diptera)

Reichhart¹,

Essrich²,

Dimarcq³

et al. 1989

European Journal of Biochemistry

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We have previously isolated and characterized a family of novel 8-kDa cationic antibacterial peptides synthesized by larvae of Phorrnia terranovae (Diptera) in response to various injuries. These molecules have been named diptericins. The peptide sequence of diptericin A was used to prepare oligonucleotides for screening cDNA libraries and we report in the present paper the isolation of several cDNA clones encoding diptericin. The analysis of the nucleotide sequences indicates that diptericin is synthesized as a prepeptide which is matured in two steps: (a) cleavage of a signal peptide and (b) amidation of the C-terminal residue. Interestingly, the 3' untranslated region of the mRNA contains a consensus sequence TTATTTAT which is also observed in the mRNA of another insect antibacterial peptide (attacin-related sarcotoxin IIA) and in mRNAs encoding proteins related to the inflammatory response in mammals. Our data illustrate that diptericins form a polymorphic family of immune peptides. The transcription of the diptericin genes is rapidly induced in the fat body after inoculation of bacteria, as evidenced by the transcriptional profile.Our knowledge of the biochemical aspects of the immune response in insects has developed significantly over the last decade. It has been clearly established that in the higher insect orders, namely Lepidoptera and Diptera, injection of live or killed bacteria and even a simple injury, induce the rapid appearance in the haemolymph of several families of antibacterial peptides (reviewed in [I -31). We have recently isolated from the immune haemolymph of larvae of the dipteran Pliormiu terranovae three heat-stable peptides active on Gramnegative bacteria. We have established the full amino acid sequence of one of these molecules which contains 82 residues and has a relative molecular mass of 8610. The two other peptides have only been partially sequenced (the first 40 residues from the N-terminus) and exhibit marked similarities, indicating that the three peptides belong to a common family [4]. They are not structurally related to other known antibacterial peptides from insects [lysozymes, cecropins (including sarcotoxins 1) and attacins (including sarcotoxins II)] and have no significant similarity with other reported peptide sequences. These novel antibiotic molecules have been named diptericins (diptericin A referring to the fully sequenced peptide [4]). The present paper reports the isolation of several cDNA clones for diptericins from which the structure of the diptericin precursor molecule is deduced. In addition, some of these clones served to investigate the transcriptional profiles for the diptericin genes during immunization. This infor- mation is one of the prerequisites for the analysis of the mechanism of selective induction of the immune genes, a question which will be addressed in a subsequent study. MATERIALS AND METHODS InsectsThird instar wandering larvae (crop half empty), 2-day-old pupae and 1-week-old male and female adults of P. terrnnovae were isolated and kept...

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“…Nonessential criteria, which are nonetheless characteristic of many neuropeptide precursors, were used as supporting evidence for the identification of ESTs encoding putative neuropeptide precursors. These included the repetition of homologous variations of a putative neuropeptide sequence within the protein and the presence of a glycine residue at the C-terminal of the putative neuropeptide(s), a structural prerequisite for C-terminal amidation that is a characteristic feature of many neuropeptides [27].…”

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confidence: 99%

Discovery of a second SALMFamide gene in the sea urchin Strongylocentrotus purpuratus reveals that L-type and F-type SALMFamide neuropeptides coexist in an echinoderm species

Rowe

Elphick

2010

Marine Genomics

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The SALMFamides are a family of neuropeptides that act as muscle relaxants in the phylum Echinodermata. Two types of SALMFamides have been identified in echinoderms: firstly, the prototypical L-type SALMFamide peptides with the Cterminal sequence Leu-X-Phe-NH 2 (where X is variable), which have been identified in several starfish species and in the sea cucumber Holothuria glaberrima; secondly, F-type SALMFamide peptides with the C-terminal sequence Phe-X-Phe-NH 2 , which have been identified in the sea cucumber Apostichopus japonicus. However, the genetic basis and functional significance of the occurrence of these two types of SALMFamides in echinoderms are unknown. Here we have obtained a new insight on this issue with the discovery that in the sea urchin Strongylocentrotus purpuratus there are two SALMFamide genes. In addition to a gene encoding seven putative Ftype SALMFamide neuropeptides with the C-terminal sequence Phe-X-Phe-NH 2 (SpurS1-SpurS7), which has been reported previously (Elphick and Thorndyke, 2005; J. Exp. Biol., 208, 4273-4282 [1]), we have identified a gene that is expressed in the nervous system and that encodes a precursor of two putative L-type SALMFamide neuropeptides with the C-terminal sequences Ile-X-Phe-NH 2 (SpurS8) and Leu-XPhe-NH 2 (SpurS9). Our discovery has revealed for the first time that L-type and Ftype SALMFamide neuropeptides can coexist in an echinoderm species but are encoded by different genes. We speculate that this feature of Strongylocentrotus purpuratus may apply to other echinoderms and further insights on this issue will be possible if genomic and/or neural cDNA sequence data are obtained for other echinoderm species.3

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Mechanism of C-terminal amide formation by pituitary enzymes

Cited by 666 publications

References 12 publications

Molecular cloning and nucleotide sequence analysis of a cDNA encoding the main β‐neurotoxin from the venom of the South American scorpion Tityus serrulatus

Molecular cloning and nucleotide sequence analysis of a cDNA encoding the main β‐neurotoxin from the venom of the South American scorpion Tityus serrulatus

Insect immunity. Isolation of cDNA clones corresponding to diptericin, an inducible antibacterial peptide from Phormia terranovae (Diptera)

Discovery of a second SALMFamide gene in the sea urchin Strongylocentrotus purpuratus reveals that L-type and F-type SALMFamide neuropeptides coexist in an echinoderm species

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