title: Polyproteins in structural biology.
abstract: Polyproteins are chains of covalently conjoined smaller proteins that occur in nature as versatile means to organize the proteome of viruses including HIV. During maturation, viral polyproteins are typically cleaved into the constituent proteins with different biological functions by highly specific proteases, and structural analyses at defined stages of this maturation process can provide clues for antiviral intervention strategies. Recombinant polyproteins that use similar mechanisms are emerging as powerful tools for producing hitherto inaccessible protein targets such as the influenza polymerase, for high-resolution structure determination by X-ray crystallography. Conversely, covalent linking of individual protein subunits into single polypeptide chains are exploited to overcome sample preparation bottlenecks. Moreover, synthetic polyproteins provide a promising tool to dissect dynamic folding of polypeptide chains into three-dimensional architectures in single-molecule structure analysis by atomic force microscopy (AFM). The recent use of natural and synthetic polyproteins in structural biology and major achievements are highlighted in this contribution.
authors.affiliation: Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France. Electronic address: crepin@embl.fr.
authors.forename: Thibaut
authors.initials: T
authors.lastname: Crépin
authors.affiliation: Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France.
authors.forename: Christopher
authors.initials: C
authors.lastname: Swale
authors.affiliation: Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France.
authors.forename: Alexandre
authors.initials: A
authors.lastname: Monod
authors.affiliation: Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France; The European Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, BP181, 38042 Grenoble Cedex 9, France.
authors.forename: Frederic
authors.initials: F
authors.lastname: Garzoni
authors.affiliation: Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France; The European Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, BP181, 38042 Grenoble Cedex 9, France.
authors.forename: Maxime
authors.initials: M
authors.lastname: Chaillet
authors.affiliation: Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France; The European Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, BP181, 38042 Grenoble Cedex 9, France; The School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom. Electronic address: iberger@embl.fr.
authors.forename: Imre
authors.initials: I
authors.lastname: Berger
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray / Q000379:methods; D006801:Humans; D018625:Microscopy, Atomic Force / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020815:Polyproteins / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D014764:Viral Proteins / Q000737:chemistry; D014780:Viruses / Q000737:chemistry
chemical_list: D020815:Polyproteins; D011994:Recombinant Proteins; D014764:Viral Proteins