Evidence for the presence of a secondary structure at the dibasic processing site of prohormone: the pro-ocytocin model

Détails

ID Serval
serval:BIB_7BA03C0A3E58
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Evidence for the presence of a secondary structure at the dibasic processing site of prohormone: the pro-ocytocin model
Périodique
EMBO Journal
Auteur(s)
Paolillo  L., Simonetti  M., Brakch  N., D'Auria  G., Saviano  M., Dettin  M., Rholam  M., Scatturin  A., Di Bello  C., Cohen  P.
ISSN
0261-4189 (Print)
Statut éditorial
Publié
Date de publication
07/1992
Volume
11
Numéro
7
Pages
2399-405
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jul
Résumé
Bioactivation of pro-proteins by limited proteolysis is a general mechanism in the biosynthesis of hormones, receptors and viral protein precursors. This proceeds by cleavage of peptide bonds at the level of single or pairs of basic residues in the proforms. Examination of a number of cleavage loci in various precursors failed to reveal any consensus primary sequence around the dibasic cleavage sites. Thus it has been proposed, on the basis of secondary structure predictions [Rholam, M., Nicolas, P. and Cohen, P. (1986) FEBS Lett., 207, 1-6], that those basic residues which operate as signal loci for the proteolytic enzyme machinery are situated in, or next to, privileged precursor regions most often constituted by flexible and exposed motifs, e.g. beta-turns and/or loops. Peptides reproducing the N-terminal processing domain of the hormone precursor, pro-ocytocin-neurophysin, were examined by a combination of spectroscopical techniques including circular dichroism, infrared Fourier transform and one- and two-dimensional proton NMR. The results indicate that: (i) the region situated on the N terminus of the Lys-Arg doublet is organized as a beta-turn in solution; (ii) the sequential organization of the residues participating in the beta-turn determines the privileged relative orientation of the basic amino acid side chains and the subtype of turn; (iii) the peptide segment situated on the C-terminal side of the dibasic, corresponding to the N-terminal octapeptide of neurophysin, is organized as an alpha-helix.(ABSTRACT TRUNCATED AT 250 WORDS)
Mots-clé
Amino Acid Sequence Animals Cattle Circular Dichroism Endopeptidases/metabolism Fourier Analysis Kinetics Magnetic Resonance Spectroscopy Molecular Sequence Data Oxytocin/*chemistry/metabolism Peptides/chemical synthesis/metabolism Protein Conformation Protein Precursors/*chemistry/metabolism *Protein Processing, Post-Translational Spectrophotometry, Infrared
Pubmed
Web of science
Création de la notice
28/01/2008 11:34
Dernière modification de la notice
03/03/2018 18:36
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